Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A1Z9L3 | DHX8_DROME | MDELQKLEYLSLVSKICTELDNHLGINDKDLAEFIIDLENKNRTYDTFRKALLDNGAEFPDSLVQNLQRIINLMRPSRPGGASQEKTVGDKKEDKKSQLLKMFPGLALPNDTYSKKEESDDDEKVKAKPEKHSETHKKTDMSDVDAAMMELEALAPGEGATLVRPHKEVSSRDRHKRRSRDRDTKRRSRSREDRHSDRRRSRSRDKERRRRSRSRDNRRRSRSREDRDRDRDRRHKSSSSRDHHERRRRSRSRSTERRDRRDRSRDCSEKMPPPSAAMTDDPEAGKIYSGKIANIVPFGCFVQLFGLRKRWEGLVHISQLRAEGRVTDVTEVVTRNQTVKVKVMSITGQKVSLSMKEVDQDSGKDLNPLSHAPEDDESLRDRNPDGPFSSSTSMLNLQGNGMEGDEHESRKRVTRISSPERWEIKQMISSGVLDRSEMPDFDEETGLLPKDEDDEADIEIEIVEEEPPFLSGHGRALHDLSPVRIVKNPDGSLAQAAMMQSALSKERREQKMLQREQEIEAMPTSLNKNWIDPLPEDESRSLAANMRGMAAAPPEVPEWKKHVIGGKKSSFGKKTDLTLVEQRQSLPIYKLRDDLIKAVTDNQILIVIGETGSGKTTQITQYLGECGFTARGKIGCTQPRRVAAMSVAKRVAEEYGCRLGQEVGYTIRFEDCTSPETIIKYMTDGMLLRECLMEAELKSYSVIMLDEAHERTIHTDVLFGLLKTAVQKRPELKLIVTSATLDAVKFSQYFFKAPIFTIPGRTFPVEVLYTKEPETDYLDASLITVMQIHLREPPGDILLFLTGQEEIDTACEILYERMKSLGPDVPELIILPVYSALPSEMQTRIFDPAPAGSRKVVIATNIAETSLTIDGIFYVVDPGFVKQKVYNSKTGMDSLVVTPISQAAAKQRAGRAGRTGPGKTYRLYTERAYRDEMLPTPVPEIQRTNLATTVLQLKTMGINDLLHFDFMDAPPVESLVMALEQLHSLSALDDEGLLTRLGRRMAEFPLEPNLSKMLIMSVALQCSDEILTIVSMLSVQNVFYRPKDKQALADQKKAKFNQAEGDHLTLLAVYNSWKNNKFSNAWCYENFVQIRTLKRSQDVRKQLLGIMDRHKLDVVSAGKNSVRIQKAICSGFFRNAAKKDPQEGYRTLVDSQVVYIHPSSALFNRQPEWVIYHELVQTTKEYMREVTTIDPKWLVEFAPSFFRFSDPTKLSKFKKNQRLEPLYNKYEEPNAWRISRVRRRRN | 3.6.4.13 | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; mRNA splicing, via spliceosome [GO:0000398]; oogenesis [GO:0048477]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; spliceosomal complex disassembly [GO:0000390]; ventral cord development [GO:0007419] | catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; spliceosomal complex [GO:0005681] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF21010;PF04408;PF00271;PF07717;PF00575; | 1.20.120.1080;2.40.50.140;3.40.50.300; | DEAD box helicase family, DEAH subfamily, DDX8/PRP22 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18981222}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P24384}; | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:18981222, PubMed:24244416). Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome (By similarity). Before and after egg-chamber formation, required for nurse-cell chromatin dispersal (NCCD) probably by playing a role in spliceosome localization to chromatin/interchromatin spaces (PubMed:24244416). {ECO:0000250|UniProtKB:Q14562, ECO:0000269|PubMed:24244416, ECO:0000303|PubMed:18981222}. | Drosophila melanogaster (Fruit fly) |
A1Z9P3 | SHRM_DROME | MKMRNHKENGNGSEMGESTKSLAKMEPENNNKISVVSVSKLLLKDSNGANSRSSNSNASFSSASVAGSVQDDLPHHNSSSSQLGQQHGSSLDQCGLTQAGLEEYNNRSSSYYDQTAFHHQKQPSYAQSEGYHSYVSSSDSTSATPFLDKLRQESDLLSRQSHHWSENDLSSVCSNSVAPSPIPLLARQSHSHSHSHAHSHSNSHGHSHGHAHSASSSSSSNNNSNGSATNNNNNNSSESTSSTETLKWLGSMSDISEASHATGYSAISESVSSSQRIVHSSRVPTPKRHHSESVLYLHNNEEQGDSSPTASNSSQMMISEEANGEESPPSVQPLRIQHRHSPSYPPVHTSMVLHHFQQQQQQQQDYQHPSRHHTNQSTLSTQSSLLELASPTEKPRSLMGQSHSMGDLQQKNPHQNPMLGRSAGQQHKSSISVTISSSEAVVTIAPQPPAGKPSKLQLSLGKSEALSCSTPNMGEQSPTNSIDSYRSNHRLFPVSTYTEPVHSNTSQYVQHPKPQFSSGLHKSAKLPVITPAGATVQPTWHSVAERINDFERSQLGEPPKFAYLEPTKTHRLSNPALKALQKNAVQSYVERQQQQQKEEQQLLRPHSQSYQACHVERKSLPNNLSPIMVGLPTGSNSASTRDCSSPTPPPPPRRSGSLLPNLLRRSSSASDYAEFRELHQAQGQVKGPSIRNISNAEKISFNDCGMPPPPPPPRGRLAVPTRRTSSATEYAPMRDKLLLQQAAALAHQQHHPQQHRHAQPPHVPPERPPKHPNLRVPSPELPPPPQSELDISYTFDEPLPPPPPPEVLQPRPPPSPNRRNCFAGASTRRTTYEAPPPTAIVAAKVPPLVPKKPTSLQHKHLANGGGGSRKRPHHATPQPILENVASPVAPPPPLLPRARSTAHDNVIASNLESNQQKRSNSKASYLPRQSLEKLNNTDPDHGIYKLTLTSNEDLVAHTKPSYGVTGKLPNNLPDVLPLGVKLHQQPKLQPGSPNGDANVTLRYGSNNNLTGNSPTVAPPPYYGGGQRYSTPVLGQGYGKSSKPVTPQQYTRSQSYDVKHTSAVTMPTMSQSHVDLKQAAHDLETTLEEVLPTATPTPTPTPTPTPPRLSPASSHSDCSLSTSSLECTINPIATPIPKPEAHIFRAEVISTTLNTNPLTTPPKPAMNRQESLRENIEKITQLQSVLMSAHLCDASLLGGYTTPLITSPTASFANEPLMTPPLPPSPPPPLEPEEEEEQEENDVHDKQPEIEELQLMQRSELVLMVNPKPSTTDMACQTDELEDRDTDLEAAREEHQTRTTLQPRQRQPIELDYEQMSRELVKLLPPGDKIADILTPKICKPTSQYVSNLYNPDVPLRLAKRDVGTSTLMRMKSITSSAEIRVVSVELQLAEPSEEPTNLIKQKMDELIKHLNQKIVSLKREQQTISEECSANDRLGQDLFAKLAEKVRPSEASKFRTHVDAVGNITSLLLSLSERLAQTESSLETRQQERGALESKRDLLYEQMEEAQRLKSDIERRGVSIAGLLAKNLSADMCADYDYFINMKAKLIADARDLAVRIKGSEEQLSSLSDALVQSDC | null | null | actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; actomyosin structure organization [GO:0031032]; apical constriction [GO:0003383]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; embryonic morphogenesis [GO:0048598]; establishment of planar polarity of embryonic epithelium [GO:0042249]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; melanosome organization [GO:0032438]; protein localization involved in establishment of planar polarity [GO:0090251]; protein localization to adherens junction [GO:0071896] | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoskeleton [GO:0005856]; microtubule [GO:0005874]; plasma membrane [GO:0005886] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; kinase binding [GO:0019900]; protein homodimerization activity [GO:0042803] | PF08687; | 6.10.250.3120; | Shroom family | null | SUBCELLULAR LOCATION: [Isoform D]: Cell junction, adherens junction {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320, ECO:0000269|PubMed:24535826}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:20549743}. Note=In adherens junctions, enriched in discrete spots and in tricellular junctions (PubMed:20549743, PubMed:22493320). In adherens junctions, localization requires Rho1 GTPase activity and interaction with the F-actin cytoskeleton (PubMed:20549743, PubMed:24535826). {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320, ECO:0000269|PubMed:24535826}.; SUBCELLULAR LOCATION: [Isoform F]: Apical cell membrane {ECO:0000269|PubMed:20549743}; Peripheral membrane protein. Note=Localization to the apical cell membrane depends on N-terminal region (PubMed:20549743). Excluded from the lateral membrane (PubMed:20549743). {ECO:0000269|PubMed:20549743}. | null | null | null | null | null | FUNCTION: Binds to Rho-kinase Rok and targets it to the apical cell cortex where it mediates apical constriction (PubMed:20549743, PubMed:22493320). During embryogenic axis elongation, required for the localization to adherens junctions and the establishment of planar polarization of both Rho-kinase Rok and myosin regulatory light chain sqh (PubMed:24535826). May be involved in the assembly of microtubule arrays during cell elongation (By similarity). {ECO:0000250|UniProtKB:Q27IV2, ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320, ECO:0000269|PubMed:24535826}. | Drosophila melanogaster (Fruit fly) |
A1Z9S1 | BL1S1_DROME | MLTSMVKEHHKEQAKRKQEQEVRRKEAIEASNELTQSLVDTLNVGVAQAYLNQKRLDAEAKQLHLGATNFAKQTHQWLQLIDQFSTALKDLGDVENWARSIEGDMHTINQTLELAYKASRATQTSSGAGTSLEASTSASASANPSAT | null | null | autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; eye pigment granule organization [GO:0008057]; neuromuscular synaptic transmission [GO:0007274]; olfactory learning [GO:0008355]; regulation of synaptic vesicle cycle [GO:0098693]; synapse organization [GO:0050808]; synaptic vesicle recycling via endosome [GO:0036466]; synaptic vesicle transport [GO:0048489] | BLOC-1 complex [GO:0031083]; neuromuscular junction [GO:0031594]; presynapse [GO:0098793] | null | PF06320; | null | BLOC1S1 family | null | null | null | null | null | null | null | FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses (PubMed:20015953, PubMed:28317021). In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn, plays a role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes (PubMed:28317021). {ECO:0000269|PubMed:20015953, ECO:0000269|PubMed:28317021}. | Drosophila melanogaster (Fruit fly) |
A1Z9X0 | APKC_DROME | MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTPSRLFFVIEFVRGGDLMYHMQRQRRLPEEHARFYAAEISLALNFLHEKGIIYRDLKLDNVLLDHEGHIKLTDYGMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLLYEMLAGRSPFDLAGASENPDQNTEDYLFQVILEKTIRIPRSLSVRAASVLKGFLNKNPADRLGCHRESAFMDIVSHPFFKNMDWELLERKQVTPPFKPRLDSDRDLANFPPEFTGEAVQLTPDDDHVIDNIDQSEFEGFEYVNPLLMSLEDCV | 2.7.11.13 | null | adherens junction organization [GO:0034332]; apical protein localization [GO:0045176]; asymmetric neuroblast division [GO:0055059]; asymmetric protein localization involved in cell fate determination [GO:0045167]; branching involved in open tracheal system development [GO:0060446]; cell-cell junction assembly [GO:0007043]; compound eye retinal cell programmed cell death [GO:0046667]; epithelial cell morphogenesis [GO:0003382]; establishment of epithelial cell apical/basal polarity [GO:0045198]; establishment of epithelial cell planar polarity [GO:0090163]; establishment of mitotic spindle orientation [GO:0000132]; establishment or maintenance of cell polarity [GO:0007163]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; establishment or maintenance of neuroblast polarity [GO:0045196]; establishment or maintenance of polarity of embryonic epithelium [GO:0016332]; establishment or maintenance of polarity of follicular epithelium [GO:0016334]; exocyst localization [GO:0051601]; germarium-derived oocyte fate determination [GO:0007294]; intracellular signal transduction [GO:0035556]; maintenance of cell polarity [GO:0030011]; melanotic encapsulation of foreign target [GO:0035011]; memory [GO:0007613]; morphogenesis of a polarized epithelium [GO:0001738]; negative regulation of hippo signaling [GO:0035331]; nuclear envelope budding [GO:0140591]; oocyte anterior/posterior axis specification [GO:0007314]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of smoothened signaling pathway [GO:0045880]; protein localization to plasma membrane [GO:0072659]; protein phosphorylation [GO:0006468]; regulation of intracellular mRNA localization [GO:1904580]; regulation of polarized epithelial cell differentiation [GO:0030860]; sensory organ development [GO:0007423]; spermatogenesis [GO:0007283]; synapse assembly [GO:0007416]; terminal branching, open tracheal system [GO:0007430]; zonula adherens assembly [GO:0045186] | apical cortex [GO:0045179]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell cortex [GO:0005938]; nucleus [GO:0005634]; subapical complex [GO:0035003] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00564;PF00069;PF00433; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}. Apicolateral cell membrane {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}; Peripheral membrane protein {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}. Note=Cytoplasmic at interphase but localizes to the apical cell cortex during mitosis. {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification factors and for the posterior establishment of the microtubule organizing center within the presumptive oocyte. Phosphorylates l(2)gl which restricts l(2)gl activity to the oocyte posterior and regulates posterior enrichment of par-1, leading to establishment of correct oocyte polarity. Essential for apical localization of l(2)gl and par-6 in neuroblasts and for exclusion of mira from the apical cortex. Phosphorylates baz which is required for targeting of baz to the postsynaptic region where it is involved in actin organization, and for apical exclusion of baz which is necessary for establishment of the apical/lateral border in epithelial cells. Phosphorylates yrt which prevents its premature apical localization and is necessary for correct epithelial cell polarization. Required for the establishment of mitotic spindle orientation during symmetric division of epithelial cells and for apical exclusion of raps/Pins. Involved in symmetric adherens junction positioning during embryogenesis. Required for polarization of the spermatid cyst which is necessary for sperm differentiation. Required for stimulation of the Toll signaling pathway which activates Dif and dl and plays a role in innate immunity. Plays a role in memory enhancement. {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:11914720, ECO:0000269|PubMed:12446795, ECO:0000269|PubMed:14657233, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:15907474, ECO:0000269|PubMed:17488624, ECO:0000269|PubMed:18094021, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:19472188, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:22223679, ECO:0000269|PubMed:24515345, ECO:0000269|PubMed:24830287}. | Drosophila melanogaster (Fruit fly) |
A1ZA47 | ZASP_DROME | MAQPQLLQIKLSRFDAQPWGFRLQGGTDFAQPLLVQKVNAGSLSEQAGLQPGDAVVKINDVDVFNLRHKDAQDIVVRSGNNFVITVQRGGSTWRPHVTPTGNVPQPNSPYLQTVTKTSLAHKQQDSQHIGCGYNNAARPFSNGGDGGVKSIVNKQYNTPVGIYSDESIAETLSAQAEVLAGGVLGVNFKKNEKEYQGDRSEVLKFLREEETGQSTPAFGNSHYEHDAPQQLQQPQQQYNQHQQHYHQQQQQQQSSTTRHVSAPVNSPKPPSTGGLPTGQNICTECERLITGVFVRIKDKNLHVECFKCATCGTSLKNQGYYNFNNKLYCDIHAKQAAINNPPTGTEGYVPVPIKPNTKLSASTISSALNSHGYGGHSNGYSNGNSTPAPAPVASSQATATVATVAPSAATAATAAATPQAATATDSPAATASSSDNMSAYVADEPSSIYGQISAESVALAPPPPQPPTAGGGDQPFEYVTLTGNVIRSVQAPGKGACPSYKVNQGYARPFGAAAPKSPVSYPPQQQQQSPRPAPGGQNPYATLPRSNVGQQGGEAVEELQPEFEEEDCYEMDIEVALAASRQSQRGSSFTWPPPQDDSHLAPTAAPLYIPPPETQHVVVSNPVQQVPPLPPGGATARLDPQPVVGTSANGAPQWQSYSAPQLTTASARQLAEQESSSDSYTSTSTTTTTTSEEYQRMYAAQVQAYQMQEQSGSEFDYQVDYASTQDSVQDYPSGRRSAQECVDSLAVPLSTYKLVDMVREVTPSPVTTPTQTPAPAAPTTRRVVFNDEPEIKELPQLPAELETIPEASEAVEDREGLVIEQRCQILESERKFQPTPEIKIEIAPVRQIPPTKIPNPMPKEWINPMIRVLTTAPEVPFHLVECPFPRPCGDDFEAEAAAAEAAKTQEVPEPLPPQVSAAPPATVSVEPSPAPLRESPPRGSRLSQAMVTAPEFELKFAPPADQGIPLPEETEPYMPPPIDTKPYLREDYRPKSPFVSALTTAPDRPFEGHFDKDVPIHMIDLPTPKEHLSMCDALCTAPERGYTPLNPENAMHRVDEEQKQQELKKREFQVLDHEEELGIRPEPPQSVEYYETRRDQPRKSSAFAAMQAFQPSREPLSSNTVSNAGSVADTPRASIVSALKEETDLEYQKYLKAQQRNQKRLDYFHQKEEELSGLQGQQLTQLQRELSNQQQNLLSQQQLQQSKLLQLQQCVQSQELQQQVQHLTQKSQQQPPQANQQQQQQQQQRGTQQQQHSQVTQRTQQQQQQVPQQVTQQQQQEHSLLSQTTLAETQTLQANAQSQSSASYSSKATACSNSSSTVPPANTSTAFAPAPAPAPTSIPVRPSAIAVQSSYCSSQFDVHELIEETAEELEHSEVLFPPPSPLSHLTKQGKAVQSGLHKADSIPKYQRNWTVLPTQSPIRTPEPQELRENVPLAFVDAPKAPVTSDSSTVHRPIAQVAAPTTVVAPSREREKERRPQLSVPIIVEDRSGPVTMAFQPLDELVRPDQALTPTRPYTPSLTNKPAPIVPFYQTEEKLVFEECSATHARNYNELNASPFPDRTRSPAPGPPPNPLNAIRAPRMKEPETKSNILSVSGGPRLQTGSITTGQSYQGQLLAHSEQSSQSASQSYNQQPERITEQRVGNLNIQQREQSSQLQQQAQSQTQSQTRSQVGNTQIERRRKVTEEFERTQSAKTIEIRTGSQSVSQSKAQSQSISQAQTQAQSQSQNQSDTERRSSYGKTGFVASQAKRLSCMEEEISSLTSQSQAISARASALGEGCFPNLRSPTFDSKFPLKPAPAESIVPGYATVPAATKMLTAPPPGFLQQQQQQQQRSAFSGYQATTSSVQQSSFASSSKATTSSLSSSSASASASASVARSSQSLTQASAITTTTNNQATTAYRSSNGSITKPNLASRPSIASITAPGSASAPAPVPSAAPTKATAPFKAPIVPKSVIANAVNAAAPPAPAVFPPDLSDLNLNSNVDNSPGAGGKSAGAFGATSAPKRGRGILNKAAGPGVRIPLCNSCNVQIRGPFITALGRIWCPDHFICVNGNCRRPLQDIGFVEEKGDLYCEYCFEKYLAPTCSKCAGKIKGDCLNAIGKHFHPECFTCGQCGKIFGNRPFFLEDGNAYCEADWNELFTTKCFACGFPVEAGDRWVEALNHNYHSQCFNCTFCKQNLEGQSFYNKGGRPFCKNHAR | null | null | actin cytoskeleton organization [GO:0030036]; heart development [GO:0007507]; muscle structure development [GO:0061061]; myofibril assembly [GO:0030239]; regulation of cell-matrix adhesion [GO:0001952] | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; apical part of cell [GO:0045177]; basal part of cell [GO:0045178]; basolateral plasma membrane [GO:0016323]; cell leading edge [GO:0031252]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; muscle tendon junction [GO:0005927]; stress fiber [GO:0001725]; Z disc [GO:0030018]; zonula adherens [GO:0005915] | actin binding [GO:0003779]; actinin binding [GO:0042805]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371] | PF15936;PF00412;PF00595; | 2.30.42.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18166658}. Note=Regulates or strengthens the link of integrins to the actin cytoskeleton. {ECO:0000269|PubMed:18166658}. | null | null | null | null | null | FUNCTION: Regulator of cell matrix adhesion having two related functions, one upstream of Actn organizing the Z line and the other downstream of integrins regulating assembly of integrin adhesion sites. Also required for the formation of myotendinous junctions in muscles. {ECO:0000269|PubMed:18166658}. | Drosophila melanogaster (Fruit fly) |
A1ZA55 | CGLR1_DROME | MAMNLENIVNQATAQYVKIKEHREPYTAHYNALKDKVYSEWKSSAVLGKLLKGSTLCGGYGDKLKVSIPDEFDLLIHLVFPENDKIIVKADASKPGNVILDMTKVMEIIGSQEHNKPVFDRLQKIVNNKKQLLEDKLNSFLESIMTQTLNKMGNQIEVAGRISHLQYKKCGPAHTIFVKGSCKYSVDFVPAIRLSAAQVVLAPEQRIHFGETLYWDAIPKPMKPAKTDNTSFTSSFYEAERRLLYGKQFLKPAIRLMKQNRNVKNKANLKSYHIKTLFLWQVIQQDPSYWSNSPKDIFIEMLGKLADSLALTPKKGKLPFFWDPKLDMFAQLTDSQRTDLYNHFRKCEYTFRKDNGNVNDCTENNVHSSFSKNTTYKL | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:34261127}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34261127}; | cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; immune response involved in response to exogenous dsRNA [GO:1902615]; innate immune response [GO:0045087]; response to exogenous dsRNA [GO:0043330] | cytosol [GO:0005829] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; 3',2'-cyclic GMP-AMP synthase activity [GO:0140700]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',2'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:68344, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:177334; Evidence={ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68345; Evidence={ECO:0000269|PubMed:34261127}; | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in antiviral innate immunity (PubMed:34261127, PubMed:34261128). Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG (PubMed:34261127). Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses (PubMed:34261127). Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',2'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:34261127, PubMed:34261128). 3',2'-cGAMP is protected from poxin cleavage (PubMed:34261127). {ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128}. | Drosophila melanogaster (Fruit fly) |
A1ZAB5 | CLU_DROME | MALETEAKNSNATATGDATATATKASGKAKENNNTAGGKKNLNPNSNQQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPTEPTTEAVLSNGHAEKPTVVDAVEDNADTNANVEKPQEGGAPDAEADGDDIDLDALQDIGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKSINNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPEYVTPGVSDPPILPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFFINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWAAPILEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDTKMQMFIWNNIFFSMGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVVDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHVVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVNFIRIAAARLQQLTTIKQSEKSEANPVPALEGAEAASKVNGAEKPDDKEKKNEEEEKKERSTSGEARAAAIVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHADGEEGTSLAKQKVLVQEAAEFLVLKQIPAFIKEHMSHSSSPIDGQSLTESLHSHGINVRYLGKVIKILSQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQTTGNQNGSSSGSSNSSSASDWTLMTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLMRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPIVKHISPRATDAYNFYTTGQAKIQQGLFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKDMHVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTRDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKTDSTENEVNDAINSIVAAANNNGEAEDAVSKDIKEQPEAGKQLTNGDKAAATEATSS | null | null | asymmetric neuroblast division [GO:0055059]; intracellular distribution of mitochondria [GO:0048312]; mitochondrion localization [GO:0051646] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extrinsic component of mitochondrial outer membrane [GO:0031315]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; outer mitochondrial membrane protein complex [GO:0098799] | mRNA binding [GO:0003729]; ribosome binding [GO:0043022] | PF13236;PF15044;PF12807;PF05303;PF13374;PF13424; | 3.30.2280.10;1.25.40.10; | CLU family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}. | null | null | null | null | null | FUNCTION: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}. | Drosophila melanogaster (Fruit fly) |
A1ZAJ2 | KIF1A_DROME | MSSVKVAVRVRPFNSREIARESKCIIEMAGATTAITNPKVPPNTSDSVKRFNFDYSYWSHDHHDADFSTQSMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICKDLFTRIQDTETDDLKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDLMTNLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKNTKKADFIPYRDSALTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRDLLKAEGIEVQEEDELTKSTVIKSPTKSRNRNGSTTEMAVDQLQASEKLIAELNETWEEKLKRTEEIRVQREAVFAEMGVAVKEDGITVGVFSPKKTPHLVNLNEDPNLSECLLYYIKEGLTRLGTHEANVPQDIQLSGSHILKEHCTFENKNSTVTLLPHKDAIIYVNGRKLVEPEVLKTGSRVILGKNHVFRFTNPEQARELRDKIETENEAENEVEKTDTQQVDWNFAQCELLEKQGIDLKAEMKKRLDNLEEQYKREKLQADQQFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDVYTNPMYESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELASTVAPVHQEDEFGAPPVSKTLVAVEVTDTKNGATHHWSLEKLRQRLELMREMYHNEAEMSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFIYLSNLLYPVPLVHKVAIVNERGDVRGYLRIAVQPVLDEESIDFNNGVKQSARLVFNEDDAKPKYRALNEKDDVQRYIDNGGLDSKLEELEDVDSGRGIDSNSASECHENSEEPGEHLQVGKEFTFRVTVLQATGIGAEYADIFCQFNFLHRHEEAFSTEPVKNSASGAPLGFYHVQNITVPVTKSFIEYLKTQPIMFKIFGHYQTHPLHKDAKQDFVSRPPPRRMLPPSIPISQPVRSPKFGPLPCAPTSTVLAKHDVLVWFEICELAPNGEYVPSVVEHSDDLPCRGLFLLHQGIQRRIRITIVHEPTTEVKWKDINELVVGRIRNTPESSDEQDEDACVLSLGLFPGEALEVPGDDRSFYRFEAAWDSSLHNSALLNRVSQGGETIYITLSAYLELENCARPAIITKDLSMVIYGRDARTGPRSLKHLFSGQYRNPEANRLTGVYELALRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRMRHLLLLRERLGMDTNPNPTTKTEKDVCNLAARAATSPVHMVIPQSPQTPVKDPQQIIPEREYNQREQDLMLKCLKLVQGRYTKSEANDTQTQSDVSPSDEGCADMTVSCISSNSMENNKFVIRRRLCSPDRADAPNGWEAPAPATQPALPLRLYVPELEEIRVSPVVARKGLLNVLEHGGSGWKKRWVIVRRPYVFIYRSEKDPVERAVLNLATAHVECSEDQAAMVKIPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIKSRLARRTLEPASQTASQIQATNAANANSASK | null | null | anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; axo-dendritic transport [GO:0008088]; axonal transport [GO:0098930]; cytoskeleton-dependent intracellular transport [GO:0030705]; filopodium assembly [GO:0046847]; larval locomotory behavior [GO:0008345]; microtubule-based movement [GO:0007018]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; neuromuscular junction development [GO:0007528]; positive regulation of insulin secretion [GO:0032024]; protein transport [GO:0015031]; regulation of dendrite morphogenesis [GO:0048814]; regulation of locomotion [GO:0040012]; regulation of synapse assembly [GO:0051963]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle transport [GO:0048489]; vesicle transport along microtubule [GO:0047496]; vesicle-mediated transport [GO:0016192] | axon [GO:0030424]; axon cytoplasm [GO:1904115]; axon terminus [GO:0043679]; dendrite [GO:0030425]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GTP-dependent protein binding [GO:0030742]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF12473;PF00498;PF12423;PF00225;PF16183;PF00169; | 2.60.200.20;6.10.250.2520;3.40.850.10;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17643120}. Cell projection, axon {ECO:0000269|PubMed:30174114}. Note=Microtubule-associated. {ECO:0000269|PubMed:17643120}. | null | null | null | null | null | FUNCTION: Required for presynaptic maturation, has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors, components required for the morphological transformation of axonal growth cones to mature boutons. {ECO:0000269|PubMed:17643120, ECO:0000269|PubMed:30174114}. | Drosophila melanogaster (Fruit fly) |
A1ZAU8 | PTRO_DROME | MDVETQEIRQARQRASVKWLLSKAFNNRVPDNLKEPFYRDHENQERLKPQIIVELGNATLYCQTLANLYSDPNYQSMNHWSIIQTLARKGVPVAESADMPITETVLIQTNPLRINAHMSVIESLMVLYAKEISSGDRVMAAIRRISGNNYQAPTGQSYEQALLGWISHACAALKKRIIKEVDAGLPDDNGSRLQTPDIPPVRDFQDLCDGICLALLISYYCPKVVPWTSVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMHMTPEDVTYMRGSMKLNLVVLLTDLFNLFEIHPAKCVCYPGMDGQVPHSNSFGGGLNRRSTPPNEYQTVQSNNFDGNHAEAFVVHKSRGITTLASMHSQQQQQLHQQQQHQQQYHQQPLQQHPSQSQLQIQQQEPLVPARLRQAKEKTNVESKADERGRRSRRNSSSEDSQLTIENFGGSQDQLNTLGRYERDRERKLSNTSVGSYPVEPAVAVRSSIADARGTLQLGYDTDSGSEKQDRETEKYSMRRQVSVDNVPTVSSHNLSNAGSPLPVARHKQHSSDKDYSSNSGMTPDAYNDSRSTSGYDPESTPVRKSSTSSMPASPAAWQLDVGDDDMRSLENASKLSTIRMKLEEKRRRIEQDKRKIEMALLRHQEKEDLESCPDVMKWETMSNESKRTPDMDPVDLDKYQQSIAIMNMNLQDIQQDIHRLATQQSQMQAQHLQAQQLMQAQQIANMLNQAYNAPVSAYSSRPPSRDPYQQQLHHQQQQPMPMPQPMQYVNEHGQYMSPPQPAHYMPQQAQQPQSIYSDNGAAYNHSNHSPYGGTPQYRSSVVYDDYGQPTNHFYLHESSPQPQAHQHPQRRTWAHSAAAAAYEQQQQIQPSLVDVNAWQTQQHQKQKQTWMNRPPSSAGAPSPGSFMLHQNGGGGGGGGGGGELQHLFQVQASPQHGQRQVSGSNGVQRQQSLTNLRDNRSPKAPQNMGMPMGMPMQQEDMMAPQSICFIGDEEDVDELERNIIESMQSTHISDFVHQQQQQHQHQQQLQQQQRLQGHSGRGSSSEDYDSGEMISNKLNITSGNLTYRIPSPSRPSIQANSFQDPRAMAAASGGEDQPPEKGFYISFDDEQPKRPKPPLRAKRSPKKESPPGSRDSVDNQATLKRESLSHLHNNNNIGFGNDDVNSKPVTRHSIHGLNNSNSVKSPGNATYNKYTDEPPIQLRQLAVSGAMSPTSNERHHLDDVSNQSPQQTQQPMSPTRLQQSSNNAEAAKNKALVIGADSTNLDPESVDEMERRKEKIMLLSLQRRQQQEEAKARKEIEASQKREKEREKEEERARKKEEQMARRAAILEQHRLKKAIEEAEREGKTLDRPDLHVKLQSHSSTSTTPRLRQQRTTRPRPKTIHVDDASVDISEASSISSRGKKGSSSNLTGYGQLSSNSMKRDYYRGSQDSLTVKESPDDYPSTSSTPIGRRGSYKTSREPAGVERGRTLSRISVAKGSTLNFRGRKSNSLMNLCGPKLYKQPAAKSNRGIILNAVEYCVFPGVVNREAKQKVLEKIARSEAKHFLVLFRDAGCQFRALYSYQPETDQVTKLYGTGPSQVEEVMFDKFFKYNSGGKCFSQVHTKHLTVTIDAFTIHNSLWQGKRVQLPSKKDMALVI | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; centrosome duplication [GO:0051298]; cortical microtubule organization [GO:0043622]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle asymmetry [GO:0061867]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]; negative regulation of hippo signaling [GO:0035331]; negative regulation of microtubule depolymerization [GO:0007026]; neuron projection development [GO:0031175] | anterior cell cortex [GO:0061802]; centrosome [GO:0005813]; lateral cell cortex [GO:0097575]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]; subapical part of cell [GO:0120219] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:24100293}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20946984}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32066907}. Note=Localizes to centrosomes in prophase, to the midbody during cytokinesis, diffusely throughout the metaphase spindle and to punctae in interphase that often overlap with MTs (PubMed:20946984). Colocalizes with Sas-4 and SAK at the microtubule organizing center (MTOC) (PubMed:20946984). In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) (PubMed:32066907). {ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32066907}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of microtubules and regulates their dynamics and organization (PubMed:17412918, PubMed:20946984, PubMed:24100293, PubMed:26246606, PubMed:32066907). Involved in mitotic spindle assembly (PubMed:17412918, PubMed:26246606). Regulates microtubule (MT) severing (PubMed:17412918). Antagonizes the activity of the kinesin-13 depolymerase Klp10A thereby switching off the depolymerization of the MTs at their pole-associated minus ends, which turns off poleward flux and induces anaphase B spindle elongation (PubMed:20946984, PubMed:24100293). Involved in asymmetric cell division of sensory organ precursor (SOP) cells by playing a role in the asymmetric localization of Sara-expressing endosomes to the pIIa daughter cell but not to the pIIb cell. Klp98A targets Sara-expressing endosomes to the central spindle which is symmetrically arranged in early cell division. During late cytokinesis, central spindle asymmetry is generated by enrichment of Patronin on the pIIb side which protects microtubules from depolymerization by Klp10A while unprotected microtubules on the pIIa side are disassembled by Klp10A, leading to the asymmetric delivery of Sara-expressing endosomes to the pIIa daughter cell (PubMed:26659188). In fat body cells, part of perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) which function to accommodate the organization of microtubule (MT) networks to control nuclear positioning and dynein motor-based retrograde endosomal trafficking (PubMed:32066907). Within the ncMTOC, Msp300 and shot anchors the ncMTOC at the nuclear surface and recruits the MT minus-end regulators Patronin and Nin for assembly, anchoring and/or stabilization of circumferential and radial MTs at the ncMTOCs (PubMed:32066907). This protein, and perhaps Nin, recruits msps to the ncMTOC for the gamma-tubulin-independent elongation of radial MTs (PubMed:32066907). {ECO:0000269|PubMed:17412918, ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:24100293, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:26659188, ECO:0000269|PubMed:32066907}. | Drosophila melanogaster (Fruit fly) |
A1ZAW0 | DCR2_DROME | MEDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDSVTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSKPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHYYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:35768513}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:15066283, ECO:0000269|PubMed:15550672, ECO:0000269|PubMed:24488111, ECO:0000269|PubMed:29269422, ECO:0000269|PubMed:29550490, ECO:0000269|PubMed:35768513}; | apoptotic DNA fragmentation [GO:0006309]; cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; detection of virus [GO:0009597]; dosage compensation by hyperactivation of X chromosome [GO:0009047]; dsRNA transport [GO:0033227]; global gene silencing by mRNA cleavage [GO:0098795]; heterochromatin formation [GO:0031507]; lncRNA catabolic process [GO:0110064]; locomotory behavior [GO:0007626]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of innate immune response [GO:0045089]; positive regulation of Toll signaling pathway [GO:0045752]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; RISC complex assembly [GO:0070922]; siRNA processing [GO:0030422] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; bidentate ribonuclease III activity [GO:0016443]; deoxyribonuclease I activity [GO:0004530]; helicase activity [GO:0004386]; mRNA 3'-UTR binding [GO:0003730]; ribonuclease III activity [GO:0004525]; RNA binding [GO:0003723]; siRNA binding [GO:0035197] | PF00270;PF03368;PF20931;PF00035;PF00271;PF02170;PF00636; | 3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10; | Helicase family, Dicer subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26257286}. Cytoplasm {ECO:0000269|PubMed:26257286}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:26257286}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000269|PubMed:15066283, ECO:0000269|PubMed:21419681, ECO:0000269|PubMed:24488111, ECO:0000269|PubMed:27872309, ECO:0000269|PubMed:28416567, ECO:0000269|PubMed:28874570, ECO:0000269|PubMed:29269422, ECO:0000269|PubMed:29550490, ECO:0000269|PubMed:32843367, ECO:0000269|PubMed:34257295}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 nM for 515 bp dsRNA {ECO:0000269|PubMed:21419681}; KM=2 nM for 515 bp dsRNA (in the presence of r2d2) {ECO:0000269|PubMed:21419681}; KM=0.4 nM for 515 bp dsRNA (in the presence of loqs isoform PD) {ECO:0000269|PubMed:21419681}; KM=14000 nM for ATP (in the presence of 515 bp dsRNA) {ECO:0000269|PubMed:21419681}; Note=kcat is 0.03 min(-1) for dsRNA consumption (PubMed:21419681). kcat is 0.03 min(-1) for dsRNA consumption (in the presence of r2d2) (PubMed:21419681). kcat is 0.03 min(-1) for dsRNA consumption (in the presence of loqs isoform PD) (PubMed:21419681). kcat is 4 min(-1) for siRNA production (PubMed:21419681). kcat is 93 min(-1) for ATP hydrolysis in the presence of dsRNA (PubMed:21419681). {ECO:0000269|PubMed:21419681}; | null | null | null | FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs) (PubMed:15066283, PubMed:16554838, PubMed:18953338, PubMed:19635780, PubMed:21419681, PubMed:23063653, PubMed:24009507, PubMed:24488111, PubMed:25891075, PubMed:27872309, PubMed:28416567, PubMed:28874570, PubMed:29040648, PubMed:29317541, PubMed:29550490, PubMed:32843367, PubMed:34257295, PubMed:34590626, PubMed:35768513). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin (PubMed:15066283, PubMed:16554838, PubMed:18953338, PubMed:21419681, PubMed:23063653, PubMed:24009507, PubMed:24488111, PubMed:27872309, PubMed:28416567, PubMed:28874570, PubMed:29040648, PubMed:29317541, PubMed:29550490, PubMed:32843367, PubMed:34257295, PubMed:34590626, PubMed:35768513). Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation (PubMed:29317541). As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC (PubMed:15066283, PubMed:15550672, PubMed:21245036, PubMed:21419681, PubMed:26257286, PubMed:27872309, PubMed:28416567, PubMed:34590626, PubMed:35768503). Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length (PubMed:15066283, PubMed:21419681, PubMed:23063653, PubMed:24488111, PubMed:27872309, PubMed:28416567, PubMed:28874570, PubMed:29269422, PubMed:29550490, PubMed:32843367, PubMed:34257295, PubMed:35768513). Displays a preference for binding and processing blunt termini (BLT), likely non-self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs (PubMed:25891075, PubMed:29269422, PubMed:29550490, PubMed:32843367, PubMed:34257295, PubMed:34590626). According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate (PubMed:21419681, PubMed:25891075, PubMed:28416567, PubMed:29269422, PubMed:32843367, PubMed:34590626). BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates (PubMed:21419681, PubMed:25891075, PubMed:28416567, PubMed:29269422, PubMed:29550490, PubMed:32843367, PubMed:34590626). In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides (PubMed:25891075, PubMed:29269422, PubMed:32843367, PubMed:34590626). However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates (PubMed:34257295). This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage (PubMed:34257295). During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2 (PubMed:15550672, PubMed:21245036, PubMed:24009507, PubMed:28416567, PubMed:28874570, PubMed:29040648, PubMed:29550490). Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs (PubMed:15550672, PubMed:21245036, PubMed:28416567, PubMed:35768503). Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs (PubMed:21245036, PubMed:24009507, PubMed:28874570, PubMed:29040648, PubMed:29550490, PubMed:34257295). In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC (PubMed:21245036). Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi (PubMed:24009507, PubMed:25891075, PubMed:29269422, PubMed:29550490, PubMed:32843367, PubMed:34590626). This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini (PubMed:29269422, PubMed:32843367). However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD (PubMed:34257295). Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation (PubMed:15066283). The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC (PubMed:29040648, PubMed:35768503). Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2 (PubMed:15550672, PubMed:29040648, PubMed:35768503). Both r2d2 and Dcr-2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2 (PubMed:15550672). The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation (PubMed:15550672). Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts (PubMed:26601278, PubMed:29317541). Consequently it is involved in the post-transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections (PubMed:26601278, PubMed:29317541). As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs (PubMed:26601278, PubMed:29317541). {ECO:0000269|PubMed:15066283, ECO:0000269|PubMed:15550672, ECO:0000269|PubMed:16554838, ECO:0000269|PubMed:18953338, ECO:0000269|PubMed:19635780, ECO:0000269|PubMed:21245036, ECO:0000269|PubMed:21419681, ECO:0000269|PubMed:23063653, ECO:0000269|PubMed:24009507, ECO:0000269|PubMed:24488111, ECO:0000269|PubMed:25891075, ECO:0000269|PubMed:26257286, ECO:0000269|PubMed:26601278, ECO:0000269|PubMed:27872309, ECO:0000269|PubMed:28416567, ECO:0000269|PubMed:28874570, ECO:0000269|PubMed:29040648, ECO:0000269|PubMed:29269422, ECO:0000269|PubMed:29317541, ECO:0000269|PubMed:29550490, ECO:0000269|PubMed:32843367, ECO:0000269|PubMed:34257295, ECO:0000269|PubMed:34590626, ECO:0000269|PubMed:35768503, ECO:0000269|PubMed:35768513}. | Drosophila melanogaster (Fruit fly) |
A1ZAY1 | DLISH_DROME | MAFLCPVRMRRDKKKATNASIERDLPAVGVLGMGRITGSSSIETLVRVGIEKEHGLSPDSKMVVLHDFTPCVDDELEVKRGQLVNILYRENDWVYVIGQDSRQEGFIPFSYCAPCNTQLADLAVKKKLPREQCPEQPIEENIPLLGTDNKLDVLCDETLNPGSANSIENTLLVEPECTPFVKEPSGRCIVLYTFIARDENDLSVERGEFVTVLNREDPDWFWIMRSDGQEGFVPASFIYPADSVRVLQQQKATLNAMETILQQGQQGQQSQQQQQPQLGLGTDDLRYHGTELVMLYDYKAQAPDDLYLSVRRGDWIYADLTNQTVDGWLWAYAPKTRKYGFIPKAYARPPAMTSL | null | null | establishment of epithelial cell planar polarity [GO:0090163]; establishment of planar polarity [GO:0001736]; negative regulation of hippo signaling [GO:0035331]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein localization involved in establishment of planar polarity [GO:0090251] | apical cortex [GO:0045179]; apicolateral plasma membrane [GO:0016327]; cilium [GO:0005929]; cytoplasm [GO:0005737]; subapical part of cell [GO:0120219] | cadherin binding [GO:0045296] | PF07653;PF14604; | 2.30.30.40; | null | PTM: Palmitoylated by app. {ECO:0000269|PubMed:27692068}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27692068}. Cytoplasm, cell cortex {ECO:0000269|PubMed:27692068}. Note=Low levels are found diffusely in the cytoplasm with high levels concentrated at the subapical cell cortex. {ECO:0000269|PubMed:27692068}. | null | null | null | null | null | FUNCTION: Required for the apical cell cortex localization, total cellular level and full activity of dachs. {ECO:0000269|PubMed:27692068}. | Drosophila melanogaster (Fruit fly) |
A1ZBD6 | MCTP_DROME | MSRIQYVDQVDQVELDQQQQPGSSSTVSGSTPPLQISPHGSPSLQQSQRLGKHLSKSASELNGHDCHLSESPHISPKRAKSAVAQQLAGVSSGGVASGVGVLQKTHGFFNNLRHRWSRAKSKDRLGRKSPSDFLEESTDYAADYSSEGSSVTHSPRHRSTTIGGSPLAREFRATAKMAQVIQRFGGSMEGRIDEHPENGSAGCSPPELSTQQQLEALQANELRRKREAQLRQFVFFQLRVHLKSGSDLVAMDKNGLSDPYVKFKVGGRLLHKSRTIHRDLNPVWDEVFIVPIEDPFQPIIVKVFDYDWGLQDDFMGSAKLDLTQLELGKAEDIHLQLCDSSGNGGSGLGEILINLTLWPRSQEDKEMHFQRNSKLAESSKRLKSQIWSSVVTILLVKAKDLPLAEDGSKLNDTHFKFRLGNEKYKSKSSWTERWLEQFDLHLFDEDQNLEIALWNRNTLYGKAIIDLSVFQRENTHGIWKPLEDCPGEVHLMLTISGTTALETISDLKAFKEDPREAQLLRERYKFLRCLQNLRDVGHLTVKVFGATGLAAADIGGKSDPFCVLELGNARLQTQTEYKTLTPNWNKIFTFNVKDITQVLEITVFDEDRDHRVEFLGKLVIPLLRIKSGVKRWYTLKDKNLCVRAKGNSPQIQLELTVVWSEIRAVCRALQPKEEKLIQQEAKFKRQLFLRNVNRLKEIIMDILDAARYVQSCFEWESPVRSSIAFVFWIVACVYGDLETVPLVLLLIILKNWLVRLITGTTDAAAHYDYEYDEDDDDDKEKEEKKSIKERLQAIQEVSQTVQNTIGYLASLGESTINTFNFSVPELTWLAVVLLLGAILVLHFVPLRWLLLFWGLMKFSRRLLRPNTIPNNELLDFLSRVPDNEEINQYRELPPSAPTDQTRNNPKKKLKGS | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:28485711}; Note=Binds Ca(2+) via the C2 domains in absence of phospholipids. {ECO:0000269|PubMed:28485711}; | regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928]; synaptic vesicle exocytosis [GO:0016079] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509] | PF00168;PF08372; | 2.60.40.150; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28485711}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (PubMed:28485711). {ECO:0000269|PubMed:28485711}. | Drosophila melanogaster (Fruit fly) |
A2A259 | PK2L1_MOUSE | MNSMESPKNQELQTLGNRAWDNPAYSDPPSPNRTLRICTVSSVALPETQPKKPEVRCQEKTQRTLVSSCCLHICRSIRGLWGTTLTENTAENRELYVKTTLRELVVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDSGVSFQTISSMSDFWDFAQGPLLDSLYWTKWYNNQSLGRGSHSFIYYENLLLGAPRLRQLRVRNDSCVVHEDFREDILNCYDVYSPDKEDQLPFGPQNGTAWTYHSQNELGGSSHWGRLTSYSGGGYYLDLPGSRQASAEALQGLQEGLWLDRGTRVVFIDFSVYNANINLFCILRLVVEFPATGGTIPSWQIRTVKLIRYVNNWDFFIVGCEVVFCVFIFYYVVEEILEIHLHRLRYLSSVWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPDTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAIMFFIVFFAYAQLGYLLFGTQVENFSTFVKCIFTQFRIILGDFDYNAIDNANRILGPVYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDQLQLSDFLKQSYNKTLLRLRLRKERVSDVQKVLKGGEPEIQFEDFTSTLRELGHEEHEITAAFTRFDQDGDHILDEEEQEQMRQGLEEERVTLNAEIENLGRSVGHSPPGELGAEAARGQSWVSGEEFDMLTRRVLQLQCVLEGVVSQIDAVGSKLKMLERKGELAPSPGMGEPAVWENLYNPS | null | null | cellular response to acidic pH [GO:0071468]; cellular response to pH [GO:0071467]; detection of chemical stimulus involved in sensory perception of sour taste [GO:0001581]; detection of chemical stimulus involved in sensory perception of taste [GO:0050912]; detection of mechanical stimulus [GO:0050982]; inorganic cation transmembrane transport [GO:0098662]; monoatomic cation transport [GO:0006812]; potassium ion transmembrane transport [GO:0071805]; protein homotetramerization [GO:0051289]; protein tetramerization [GO:0051262]; response to water [GO:0009415]; smoothened signaling pathway [GO:0007224] | actin cytoskeleton [GO:0015629]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; ciliary membrane [GO:0060170]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-activated potassium channel activity [GO:0015269]; identical protein binding [GO:0042802]; monoatomic cation channel activity [GO:0005261]; muscle alpha-actinin binding [GO:0051371]; sodium channel activity [GO:0005272]; transmembrane transporter binding [GO:0044325] | PF18109;PF08016;PF20519; | 1.10.287.70;1.20.5.340;1.10.238.10;1.20.120.350; | Polycystin family | PTM: Palmitoylation is important for expression at the cell membrane and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}. | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:25820328}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle {ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or PKD1L3 is required for localization to the cell membrane. {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}. | null | null | null | null | null | FUNCTION: Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca(2+) (PubMed:15548533, PubMed:16891422, PubMed:19464260, PubMed:20538909, PubMed:21185261, PubMed:22420714, PubMed:25820328, PubMed:28904867, PubMed:29567962). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration (PubMed:24336288, PubMed:24336289). The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription (PubMed:24336288). Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells (PubMed:16891422, PubMed:16929298, PubMed:20406802, PubMed:21098668, PubMed:21625513). The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again (PubMed:18535624, PubMed:19464260, PubMed:20406802, PubMed:20538909, PubMed:22420714, PubMed:28904867, PubMed:29567962). May play a role in the perception of carbonation taste (PubMed:19833970). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (PubMed:28553944). {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:19833970, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:28553944, ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}. | Mus musculus (Mouse) |
A2A288 | ZC12D_HUMAN | MEHPSKMEFFQKLGYDREDVLRVLGKLGEGALVNDVLQELIRTGSRPGALEHPAAPRLVPRGSCGVPDSAQRGPGTALEEDFRTLASSLRPIVIDGSNVAMSHGNKETFSCRGIKLAVDWFRDRGHTYIKVFVPSWRKDPPRADTPIREQHVLAELERQAVLVYTPSRKVHGKRLVCYDDRYIVKVAYEQDGVIVSNDNYRDLQSENPEWKWFIEQRLLMFSFVNDRFMPPDDPLGRHGPSLSNFLSRKPKPPEPSWQHCPYGKKCTYGIKCKFYHPERPHHAQLAVADELRAKTGARPGAGAEEQRPPRAPGGSAGARAAPREPFAHSLPPARGSPDLAALRGSFSRLAFSDDLGPLGPPLPVPACSLTPRLGGPDWVSAGGRVPGPLSLPSPESQFSPGDLPPPPGLQLQPRGEHRPRDLHGDLLSPRRPPDDPWARPPRSDRFPGRSVWAEPAWGDGATGGLSVYATEDDEGDARARARIALYSVFPRDQVDRVMAAFPELSDLARLILLVQRCQSAGAPLGKP | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; negative regulation of cell growth [GO:0030308]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932] | metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA endonuclease activity [GO:0004521] | PF11977;PF18039; | 3.40.50.11980; | ZC3H12 family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:26134560}. Note=Colocalizes with ZC3H12A in GW bodies (GWBs) (PubMed:26134560). {ECO:0000269|PubMed:26134560}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=Localized as discrete granules. Colocalized with mRNA-processing body markers, AGO2 and DCP1A, but not with a stress granule maker, TIA1, in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: May regulate cell growth likely by suppressing RB1 phosphorylation (PubMed:19531561). May function as RNase and regulate the levels of target RNA species (Potential). In association with ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in activated macrophages (PubMed:26134560). Serve as a tumor suppressor in certain leukemia cells (PubMed:17210687). Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation (PubMed:19531561). {ECO:0000269|PubMed:17210687, ECO:0000269|PubMed:19531561, ECO:0000269|PubMed:26134560, ECO:0000305}. | Homo sapiens (Human) |
A2A2Y4 | FRMD3_HUMAN | MFASCHCVPRGRRTMKMIHFRSSSVKSLSQEMRCTIRLLDDSEISCHIQRETKGQFLIDHICNYYSLLEKDYFGIRYVDPEKQRHWLEPNKSIFKQMKTHPPYTMCFRVKFYPHEPLKIKEELTRYLLYLQIKRDIFHGRLLCSFSDAAYLGACIVQAELGDYDPDEHPENYISEFEIFPKQSQKLERKIVEIHKNELRGQSPPVAEFNLLLKAHTLETYGVDPHPCKDSTGTTTFLGFTAAGFVVFQGNKRIHLIKWPDVCKLKFEGKTFYVIGTQKEKKAMLAFHTSTPAACKHLWKCGVENQAFYKYAKSSQIKTVSSSKIFFKGSRFRYSGKVAKEVVEASSKIQREPPEVHRANITQSRSSHSLNKQLIINMEPLQPLLPSPSEQEEELPLGEGVPLPKEENISAPLISSSPVKAAREYEDPPSEEEDKIKEEPLTISELVYNPSASLLPTPVDDDEIDMLFDCPSRLELEREDTDSFEDLEADENAFLIAEEEELKEARRALSWSYDILTGHIRVNPLVKSFSRLLVVGLGLLLFVFPLLLLLLESGIDLSFLCEIRQTPEFEQFHYEYYCPLKEWVAGKVHLILYMLGCS | null | null | actomyosin structure organization [GO:0031032] | cytoskeleton [GO:0005856]; membrane [GO:0016020] | cytoskeletal protein binding [GO:0008092] | PF08736;PF09380;PF00373;PF09379; | 1.20.80.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer. {ECO:0000269|PubMed:17260017}. | Homo sapiens (Human) |
A2A432 | CUL4B_MOUSE | MSRSTRSKERRENDTDSEDNSSETSNQERRRCRQGPPRPPYPPLLPPVFPPPTPPPQVRRTRGLQDLGAMKSVCPGTSGFSSPNPSAASAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSNSSNEREDFDSTSSSSTPPQPRDSASPSTSSFCLGVPVATSSHVPIQKKLRFEDTLEFVGIDTKMAEESSSSSSSSSPTAATSQQQQQQQLKTKSILISSVASVHHANGLAKSSTAVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSHKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQTKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQQFLQETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIASVEKQLLGEHLTAILQKGLNSLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDTCFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTMVLLMFNEGEEFSLEEIKHATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA | null | null | astrocyte differentiation [GO:0048708]; cell cycle [GO:0007049]; cellular response to UV [GO:0034644]; DNA damage response [GO:0006974]; gene expression [GO:0010467]; neuron projection development [GO:0031175]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of protein catabolic process [GO:0045732]; proteasomal protein catabolic process [GO:0010498]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; ribosome biogenesis [GO:0042254]; ubiquitin-dependent protein catabolic process [GO:0006511]; UV-damage excision repair [GO:0070914] | Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; ubiquitin protein ligase binding [GO:0031625] | PF00888;PF10557; | 1.20.1310.10;1.10.10.10; | Cullin family | PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity). {ECO:0000250|UniProtKB:Q13620}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24357321}. Nucleus {ECO:0000269|PubMed:24357321}. Note=More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes. {ECO:0000269|PubMed:24357321}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:35197566}. | null | null | FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35197566). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:35197566). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:35197566). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (By similarity). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (By similarity). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (By similarity). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (By similarity). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (By similarity). Component of the DCX(WDR77) complex, which mediates ubiquitination and degradation of Irgm1 in intestinal cells (PubMed:35197566). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (By similarity). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (By similarity). With CUL4A, contributes to ribosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q13620, ECO:0000269|PubMed:35197566}. | Mus musculus (Mouse) |
A2A5K6 | ZN335_MOUSE | MEENEVESSSDAAPRPGQPEEPSESGLGVCTSEAVSADSSDAATVPGLTEADDSGVGQSSDGGNHSVEEVSESISTDPLPHGCLPDSSSVSRGPVAEMPGGPPALVHSSVLPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSACLEPPEEPQGDPSSVAQQPPAPVTEELDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAAAAAATGKRGRVRKWGTSTKTTEEDRPEEEEEDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTPRPRRRPGRPRKLPRLETSDLHDGVGQPLVSSQSTQSPPELQDLEAPSSSGLRALGKVGRGLVESGVSQSDAENAAPSCQDEADAPPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPYLCRICGSRFLSHEDLRFHVNSHEAGDPQLFRCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSQDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHANSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSTAPGPPLSSPGPEAPQEPAPFQSPETPPLLCPDALGGTTIIYQQGAEESTAVATQTALDLLLNMSAQRELGATALQVAVVKSEGIEAELTSTGGQPSPEDTTPRVVTLHMAESGSSVAAESQLGPSDLQQIALPSGPFGGASYSVITAPPVEGRTSASGPPYREEPPGEAAQAVVVSDTLKEAGTHYIMAADGTQLHHIELTADGSISFPSPDTLAPGTKWPLLQCGGPPRDGSEVLSPTKTHHMGGSQGSSTPPPAASHTLGLVVPQSPPSAAASSTKKFSCKVCSEAFPSRAEMESHKRAHAGPAAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCNQCSFASKNKKDLRRHMLTHTNEKPFSCHVCGQRFNRNGHLKFHIQRLHSIDGRKTGTSTARAPAQTIILNSEEETLATLHTAFQSSHGVLGTERLQQALSQEHIIVAQEQTVTNQEEATYIQEITADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPDGHHIQVQEGQITHIQYEQGTPFLQESQIQYVPVSPSQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTEEAVPEQIHQLQHQGIEYDVITLSDD | null | null | brain development [GO:0007420]; brain morphogenesis [GO:0048854]; cerebral cortex neuron differentiation [GO:0021895]; epigenetic regulation of gene expression [GO:0040029]; in utero embryonic development [GO:0001701]; neuron projection morphogenesis [GO:0048812]; positive regulation of lymphocyte proliferation [GO:0050671]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neurogenesis [GO:0050769]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of neurogenesis [GO:0050767] | histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634] | histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00096;PF13912;PF13909; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23178126}. | null | null | null | null | null | FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST (PubMed:23178126). Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (By similarity). {ECO:0000250|UniProtKB:Q9H4Z2, ECO:0000269|PubMed:23178126}. | Mus musculus (Mouse) |
A2A5N8 | LMBL1_MOUSE | MEGHTDMEILRTVKGSSTGEVNVHLVARDSAGPHPQLPTTAFIIPTNAATLGLPSTALDVPYPREPVHVGALERVAGSEPVTATILPQLSTGTGTNSTVRLLDWTGVSAPLPGSGMRFRINEYAPLNMIGVERPRSPEQRHEGGMARRDAGIQHPDVHQDRQDITSLEPPVDASSCKCQACGPQQSSGLDVGSSGDRCSQPFQKRSVIVENSGCTIASELLKPMKKRKHKEYQSPSEESEPEAVKQGEGKDAEREPTPSTPENEEWSRSQLVSSEKKDGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQLPKGYKEEEFSWSQYLRSTKAQAAPKHLFVSQSHSTPPVGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDDWGDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDSFCWEKYLEETGTSAVPNWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKLHFDGWSHNYDFWIDADHPDIHPAGWCSKTGHPLEPPLRPRESSSVSPGGCPPLSHRSPPHTKTSKYNFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAEKNQSRLKAELSDSETAARKKNPSNLSPRKKPRHQGRIGRPPKYRKIPEEDLQALPPSVVHQSLFMSTLPTHADRPLSVCWEQHCKLLPGVAGISASTVSKWTIEEVFGFVQTLTGSEDQARLFKDEMIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNTDDAFK | null | null | chromatin organization [GO:0006325]; epigenetic regulation of gene expression [GO:0040029]; hemopoiesis [GO:0030097]; heterochromatin formation [GO:0031507]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of mitotic nuclear division [GO:0007088] | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; condensed chromosome [GO:0000793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; nucleosome binding [GO:0031491]; zinc ion binding [GO:0008270] | PF02820;PF00536;PF01530; | 2.30.30.140;4.10.320.30;1.10.150.50; | null | PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Does not colocalize with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2A5R2 | BIG2_MOUSE | MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQSKPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEPDRALGALECQECAVPPGVDENSQTNGIADDRQSLSSADNLEPDVQGHQVAARFSHILQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIQDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYDEIEGKKIAMKETKEHTIATKSTKQSVASEKQRRLLYNVEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFKTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLSSIDRNASERGQSQLSNPTDDSWKGAPYAHQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDAEIHIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWDEIQQRLLRVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKISDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFLRIGLVYKIWIPEEPSQVPAALSSTW | null | null | endomembrane system organization [GO:0010256]; endosome organization [GO:0007032]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; intracellular signal transduction [GO:0035556]; positive regulation of tumor necrosis factor production [GO:0032760]; protein transport [GO:0015031]; receptor recycling [GO:0001881]; regulation of ARF protein signal transduction [GO:0032012] | asymmetric synapse [GO:0032279]; axonemal microtubule [GO:0005879]; centrosome [GO:0005813]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; presynapse [GO:0098793]; recycling endosome [GO:0055037]; symmetric synapse [GO:0032280]; trans-Golgi network [GO:0005802] | GABA receptor binding [GO:0050811]; guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11; | null | PTM: In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2A5Z6 | SMUF2_MOUSE | MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVPLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE | 2.3.2.26 | null | negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of trophoblast cell migration [GO:1901165]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151] | identical protein binding [GO:0042802]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitin protein ligase activity [GO:0061630] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | PTM: Auto-ubiquitinated and ubiquitinated in the presence of RNF11 and UBE2D1 (By similarity). Ubiquitinated by the SCF(FBXL15) complex and TTC3, leading to its degradation by the proteasome (By similarity). 'Lys-48'-linked polyubiquitination mediated by TRAF4 at Lys-119 leads to SMURF2 proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9HAU4}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane {ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft {ECO:0000250|UniProtKB:Q9HAU4}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts. {ECO:0000250|UniProtKB:Q9HAU4}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q9HAU4}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation. {ECO:0000250|UniProtKB:Q9HAU4}. | Mus musculus (Mouse) |
A2A6C4 | SPP2C_MOUSE | MACLGSLHPLGSLLLLFLLLLLSPEARGEYGLVRVVSKNWSKDYCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSFHQAQDSSPRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQGLLIVSRARNQQCSDTISKPQDPSKPWPALTIPVAVLRYTDMLDIVSHTYGDTDVRVAMFAPLEPVTDYNMAIIFILAVGTVAAGGYWAGLMEANKLQRRQAQRGGGLGGHNQQQTVAAERSQRAWEDDDFEDAPMDFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLPLWRYQWVLPGQRVSVTWPLLLLAGLCAMVTVLWVIHRNEDHWAWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLFTKTGESIMVEVASGPADSSSHERLPMVLKVPRLSFSALTLCNQPFSILGFGDIVVPGFLVAYCHRFDMQVQSRQVYYMACTVAYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQGRAKIPAEPVAQPCIASAVGSKMKLEDAKDSRTTNRFEQAVDGESGDLESSTGDDMAEMVTLSEDEATSPEGHSESSEGWSDTNLDPNELPSGSPMALEAMLIPLIQPIPHPSELGHIRTQSRVHDSSLPWMGLHKRKGLKVKKSMSAQAPL | 3.4.23.- | null | acrosome assembly [GO:0001675]; intracellular calcium ion homeostasis [GO:0006874]; membrane protein intracellular domain proteolysis [GO:0031293]; membrane protein proteolysis [GO:0033619] | cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; endoplasmic reticulum membrane [GO:0005789]; Golgi-associated vesicle membrane [GO:0030660]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803] | PF02225;PF04258; | 3.50.30.30; | Peptidase A22B family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P49768}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30733280, ECO:0000269|PubMed:30733281, ECO:0000269|PubMed:35960805}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IUH8}; Lumenal side {ECO:0000269|PubMed:30733280}. | null | null | null | null | null | FUNCTION: Sperm-specific intramembrane-cleaving aspartic protease (I-CLiP) that cleaves distinct tail-anchored proteins and SNARE proteins (PubMed:30733280, PubMed:30733281, PubMed:35960805). In elongated spermatids, modulates intracellular Ca(2+) homeostasis by controlling PLN abundance through proteolytic cleavage (PubMed:30733280). During spermatogenesis, processes SNARE proteins and impacts vesicular trafficking which supports compartmental reorganization in maturating spermatids and may play a role in formation of the acrosome (PubMed:30733281). {ECO:0000269|PubMed:30733280, ECO:0000269|PubMed:30733281, ECO:0000269|PubMed:35960805}.; FUNCTION: In round spermatids, acts as a scaffold protein supporting FREY1 in IZUMO1 recruitment at the endoplasmic reticulum membrane and coordination of IZUMO1 complex assembly. Stabilizes FREY1 at the endoplasmic reticulum membrane through interaction. May recruit IZUMO1 interaction partners. {ECO:0000269|PubMed:35960805}.; FUNCTION: [Isoform 2]: No difference in cleavage specificity compared to isoform 1. {ECO:0000269|PubMed:30733280}. | Mus musculus (Mouse) |
A2A6Q5 | CDC27_MOUSE | MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDLVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKLTSLQNFSSCLPNTCTTLVSNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSTVISPDNVPLGPGTAILSKQVQNKPKTGRSLLGGPTALSPLTPSFGILPLETPSPGDGSYLQNYTNTPSVIDVAPTGAPTKKSVARMGQTGTKSVFSQSGNSREVTPVLVAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGLTQPSINDSLEITKLDSSIISEGKITTVTPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYSTGWVLCQIGRAYFELSEYMQAERIFSEVRRIESFRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell division [GO:0051301]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; protein K11-linked ubiquitination [GO:0070979]; protein ubiquitination [GO:0016567] | anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819] | protein phosphatase binding [GO:0019903] | PF12895;PF00515;PF13181; | 1.25.40.10; | APC3/CDC27 family | PTM: Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs specifically during mitosis (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30260}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P30260}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2A7Q9 | RN19B_MOUSE | MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDSASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQVAEKEEEGNGAGGGSGGSEDDPPYKHQSCEQKDCLASKAWDISLAQPESIRSDLESSDTQSDDVPDITSDECGSPRSHAAACPSTPQVHGAPSPSAHKNLAAPAEGQTVLKSEEYEVE | 2.3.2.31 | null | adaptive immune response [GO:0002250]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ubiquitin ligase complex [GO:0000151] | ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01485; | 1.20.120.1750;2.20.25.20;3.30.40.10; | RBR family, RNF19 subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death (By similarity). {ECO:0000250|UniProtKB:Q6ZMZ0}. | Mus musculus (Mouse) |
A2A825 | CPLN2_MOUSE | MARPPMHGSVIVPDWHETVEGKEYLACILRKNRRREFGLLERPVLPPSVVIDTASYKIFVSGKSGVGKTALVAKLAGLEVPIVHHETTGIQTTVVFWPAKLKASDCVVMFRFEFWDCGESALKKFDHMLPACKENADAFLFLFSFTDRASFEDLPGQLTRVAGEAPGLVKIVIGSKFDQYMHTDVPARDLTAFRQAWELPLFRVKSVPGRRLADGRTLDGRAGLADTAHVLNGLAEQLWHQDQVAAGLLPSSPESAPG | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cranial skeletal system development [GO:1904888]; endocardial cushion fusion [GO:0003274]; exocytosis [GO:0006887]; limb development [GO:0060173]; protein localization [GO:0008104]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation of exocytosis [GO:0017157]; regulation of smoothened signaling pathway [GO:0008589]; regulation of vesicle fusion [GO:0031338]; smoothened signaling pathway [GO:0007224] | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6GNL4}. | null | null | null | null | null | FUNCTION: Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity). {ECO:0000250|UniProtKB:Q6GNL4}. | Mus musculus (Mouse) |
A2A863 | ITB4_MOUSE | MAGPCCSPWVKLLLLAAMLSASLPGDLANRCKKAQVKSCTECIRVDKSCAYCTDELFKERRCNTQAELLAAGCRGESILVMESSLEITENTQIDTSLHRSQVSPQGLQVRLRPGEERSFVFQVFEPLESPVDLYILMDFSNSMSDDLDNLKQMGQNLAKILRQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTENVEEFWNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRADSTHLLVFSTESAFHYEADGANVLAGIMNRNDEKCHLDASGAYTQYKTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHKYFPVSSLGVLQEDSSNIVELLEEAFYRIRSNLDIRALDSPRGLRTEVTSDTLQKTETGSFHIKRGEVGTYNVHLRAVEDIDGTHVCQLAKEDQGGNIHLKPSFSDGLRMDASVICDVCPCELQKEVRSARCHFRGDFMCGHCVCNEGWSGKTCNCSTGSLSDTQPCLREGEDKPCSGHGECQCGRCVCYGEGRYEGHFCEYDNFQCPRTSGFLCNDRGRCSMGECVCEPGWTGRSCDCPLSNATCIDSNGGICNGRGYCECGRCHCNQQSLYTDTTCEINYSAIRLGLCEDLRSCVQCQAWGTGEKKGRACDDCPFKVKMVDELKKAEEVVEYCSFRDEDDDCTYSYNVEGDGSPGPNSTVLVHKKKDCPPGSFWWLIPLLIFLLLLLALLLLLCWKYCACCKACLGLLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDTVRWKITNNVQRPGFATHAASTSPTELVPYGLSLRLGRLCTENLMKPGTRECDQLRQEVEENLNEVYRQVSGAHKLQQTKFRQQPNTGKKQDHTIVDTVLLAPRSAKQMLLKLTEKQVEQGSFHELKVAPGYYTVTAEQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPVGTATLGRRLVNITIIKEQASGVVSFEQPEYSVSRGDQVARIPVIRHILDNGKSQVSYSTQDNTAHGHRDYVPVEGELLFHPGETWKELQVKLLELQEVDSLLRGRQVRRFQVQLSNPKFGARLGQPSTTTVILGEHDETDRSLINQTLSSPPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPPGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNEDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQGGEDYENFLMYSDDVLRSPASSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSDEDGSVAGGVEGEGSGWIRGATPRPPGEHLVNGRMDFAYPGSANSLHRMTAANVAYGTHLSPHLSHRVLSTSSTLTRDYHSLTRTEHSHSGTLPRDYSTLTSLSSQDSRGAVGVPDTPTRLVFSALGPTSLKVSWQEPQCDRMLLGYSVEYQLLNGGEMHRLNIPNPGQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDILGYLVTCEMAQGGAPARTFRVDGDNPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQVGGPFPQLGSHSGLFQNPVQSEFSSVTSTHSTTTEPFLMDGLTLGTQRLEAGGSLTRHVTQEFVTRTLTASGSLSTHMDQQFFQT | null | null | autophagy [GO:0006914]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell motility [GO:0048870]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; filopodium assembly [GO:0046847]; hemidesmosome assembly [GO:0031581]; integrin-mediated signaling pathway [GO:0007229]; mesodermal cell differentiation [GO:0048333]; myelination in peripheral nervous system [GO:0022011]; nail development [GO:0035878]; peripheral nervous system myelin formation [GO:0032290]; response to wounding [GO:0009611]; skin morphogenesis [GO:0043589]; trophoblast cell migration [GO:0061450] | basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell surface [GO:0009986]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; hemidesmosome [GO:0030056]; integrin complex [GO:0008305]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235] | G protein-coupled receptor binding [GO:0001664]; insulin-like growth factor I binding [GO:0031994]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; neuregulin binding [GO:0038132] | PF03160;PF00041;PF18372;PF07965;PF00362;PF17205; | 2.60.40.2030;4.10.1240.30;2.60.40.10;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-proximal region, enhancing stability and cell surface expression. Palmitoylation also promotes secondary association with tertaspanins (By similarity). {ECO:0000250|UniProtKB:P16144}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}. Note=Colocalizes with DST at the leading edge of migrating keratinocytes. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling. {ECO:0000250|UniProtKB:P16144}. | Mus musculus (Mouse) |
A2A884 | ZEP3_MOUSE | MDPDQSIKGTKKADGSPRKRLTKGEAIQTSVSSSAPYPGSGTTAPSESATQELLATQPFSGPSQEKTGQQQKPARRPSIEASVHISQLPQHPLTPAFMSPGKPEHLLEGSTWQLVDPMRPGPSGSFVAPGLHPQSQLLPSHASILPPEELPGIPKVFVPRPSQVSLKPAEEAHKKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGSSSEMYPPGLEMERIPGEEFEEPTEGESTDSEEETGAASGPSTDVLPKPKHPLLSSSLYSSGSHGSSQERCSLSQSSTGPSLEDPAPFAEASSEHPLSHKPEDTHTIKQKLALRLSERKKLIEEQTFLSPGSKGSTESGYFSRSESAEQQVSPPNTNAKSYAEIIFGKCGRIGQRTSMLASTSTQPLLPLSSEDKPSLVPLSVPRTQVIEHITKLITINEAVVDTSEIDSVKPRRSSLTRRSSVESPKSSLYRDSLSSHGEKTKQEQSLLSLQHPPSSTHPVPLLRSHSMPSAACTISTHHHTFRGSYSFDDHVADPEVPSRNTPVFTSHPRMLKRQPAIELPLGGEYSSEEPGPSSKDPTSKPSDEPEPKESDLTKKTKKGFKTKGANYECTICGARYKKRDNYEAHKKYYCSELQITKAHSVGAHEVEKTQAEPEPWSQMMHYKLGATLELTPLRKRRKEKSLGDEEEPPAFGSPGPSETAHNRPLGSTKSPAEASKSAPSLEGPTSFQPRTPKPGAGSEPGKERRTMSKEISVIQHTSSFEKSDPPEQPSGLEEDKPPAQFSSPPPAPHGRSAHSLQPRLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESSISLSGSSRSASFDREDHGKAEAPGPFSDTRSKTLGSHMLTVPSHHPHAREMRRSASEQSPNVPHSSHMTETRSKSFDYGSLSPTGPSLAVPAAPPPPAAPPERRKCFLVRQASLNRPPEAELEAVPKGKQESSEEPAASKPSTKSSVPQISVGTTQGGPSGGKSQMQDRPPLGSSPPYTEALQVFQPLGTQLPPPASLFSLQQLLPQEQEQSSEFFPTQAMAGLLSSPYSMPPLPPSLFQAPPLPLQPTVLHPSQLHLPQLLPHAADIPFQQPPSFLPMPCPAPSTLSGYFLPLQSQFALQLPGEIESHLPPVKTSLPPLATGPPGPSSSTEYSSDIQLPPVTPQATSPAPTSAPPLALPACPDAMVSLVVPVRIQTHMPSYGSAMYTTLSQILVTQSPGSPASTALTKYEEPSSKSMTVCEADVYEAEPGPSSISKEQNRGYQTPYLRVPERKGTSLSSEGILSLEGCSSTASGSKRVLSPAGSLELTMETQQQKRVKEEEASKADEKLELVSTCSVVLTSTEDRKKTEKPHVGGQGRSRREAETLSSLSSDVSDPKELSPLSHSTLSHGTAPGSEALKEYAQPSSKAHRRGLPPMSVKKEDPKEQTDLPPLAPPSSLPLSDTSPKPAKLQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGWCISLYNPNLPGVSTKAALSLLRSKQKVSKETYTMATAPHPEAGRLVPSNSRKPRMTEVHLPSLVSPESQKDPARVEKEEKQGKAEEGTPTSKRGEPARVKIFEGGYKSNEEYIYVRGRGRGRYVCEECGIRCKKPSMLKKHIRTHTDVRPYVCKHCHFAFKTKGNLTKHMKSKAHSKKCQETGVLEELEAEEGTSDDLHQDSEGQEGAEAVEEHQFSDLEDSDSDSDLDEDEEEEEEEEESQDELSGPCSEAAPPCLPPTLQENSSPVEGPQAPDSTSDEVPQGSSISEATHLTASSCSTPSRGTQGLPRLGLAPLEKDMSSAPSPKATSPRRPWSPSKEAGSRPSLTRKHSLTKNDSSPQQCSPAREAQASVTSTPGPQMGPGRDLGPHLCGSPRLELSCLTPYPIGREAPAGLERATDTGTPRYSPTRRWSLGQAESPPQTVLPGKWALAGPCSPSADKSGLGLGPVPRALLQPVPLPHTLLSRSPETCTSAWRKTESRSPSAGPAPLFPRPFSAPHDFHGHLPSRSEENLFSHLPLHSQLLSRAPCPLIPIGGIQMVQARPGAQPTVLPGPCAAWVSGFSGGGSDLTGAREAQERSRWSPTESPSASVSPVAKVSKFTLSSELEEERTGRGPGRPPDWEPHRAEAPPGPMGTHSPCSPQLPQGHQVAPSWRGLLGSPHTLANLKASSFPPLDRSSSMDCLAETSTYSPPRSRNLSGEPRTRQGSPELLGRGELRTPLFLPKGSGPPSI | null | null | positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [GO:0035914] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | null | PTM: Phosphorylated on threonine and serine residues. Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3 DNA binding affinity, and by epidermal growth factor receptor kinase increases its DNA binding affinity. {ECO:0000269|PubMed:9862992}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804591}. Nucleus {ECO:0000269|PubMed:11804591}. | null | null | null | null | null | FUNCTION: Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and pro-inflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation. {ECO:0000269|PubMed:10625627, ECO:0000269|PubMed:11035930, ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:12001065, ECO:0000269|PubMed:12193271, ECO:0000269|PubMed:14530385, ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}. | Mus musculus (Mouse) |
A2A891 | CMTA1_MOUSE | MWRAEGKWLPKTSRKSVSQSVFCGTSTYCVLNTVPPIEDDHGNSNSSHVKIFLPKKLLECLPKCSSLPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKYRKDGYCWKKRKDGKTTREDHMKLKVQGVECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVPAIEDCGKPCGPILCSINTDKKEWAKWTKEELIGQLKPMFHGIKWTCSNGNSSSGFSVEQLVQQILDSHQTKPQPRTHNCLCTGSLGAGSSVHHKCNSAKHRIISPKVEPRAGGYGGHSEVQHNDVSEGKHEPSHGRSTSREKRNGKVAKPALLHQNSTEVSSTNQVEVPDTTQSSPVSISSGLNSDPDMVDSPVVTGVSSMAVASVMGGLSQSATVFMSEVTNEAVYTMSPTAGPNHHLLSPDASQGLVLAVSSDGHKFAFPTTGSSDSLSMLPANVSEELVLSTTLDGGRKIPETAMNFDPDCFLNNPKQGQTYGGGGLKAEMVSTNIRHSPPAERSFGFTSVLTKEIKTEDTSFEQQMAKEAAYSSSAAAAASSSLTLTAAGSSLLPSGGGLSPSTTLEQMDFSAIDSNKDYASSFSQTGHSPHIHQTPSPSFFLQDASKPLPLEQNTHSSLSESGAAFVMPTVKTEASSQTSSCSGHVETRIESTSSLHLMQFQANFQAMAAEGEVTMETSQAAEGNEVLLKSGELQACGSEHYLQPETNGVIRSAGGVPLLPSNVVQGLYPVAQPSLGNSSNMELSLDHFDISFSNQFSDLINDFISVEGGSGTIYGHQLVSGDSAALSQSEDGARAPFTQAEMCIPCCSPQQGSLQLSSAEGGPSTMAYMHVAEVVSAASAQGALGMLQQSGRVFMVTDYSPEWSYPEGGVKVLITGPWQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNNQIISNSVVFEYKARALPTLPSSQHDWLSLDDNQFRMSILERLEQMERRMAEMTGSQQHKQASGGGGSGSGSGSGAGGGQAQCASGAGTLGSCFESRVVVVCEKMMSRACWAKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLIKWRTKHADSIDLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYKWDRRAISIPDSLGRLPLGIARSRGHVKLAECLEHLQRDEQAQLGQASRIHCAPSEEPTTDSWMAQWQREAMSPPEIPKGVTVIASTNPELRRPRSEPSNYYSTEGHKDYPAPKKHKLNPESFQARQEKLLCTALSLEQPNIRKQSPRSKQPSPETISPSEGVREYSREAAPPTPETAASQASASQPVVKWSAKDLYIGVSTVQVTGNPKGTSVVKDAAPSQVRPREPMSVLMLANREVVNTEMGAYRDRTEHEDCPQPMDDIQVNMMTLAEHIIEATPDRIKQENFVPMESSALERTDPATISSTMSWLASYLADADRLPSAAHIRSAYTEPLTPSSNASLSPAGSPVSEVAFEKPSLPSAADWSEFLSASTSEKVESELAQLTLSDHEQRELYEAARLVQTAFRKYKGRPLREQQEVAAAVIQRCYRKYKQLTWIALKYALYKKMTQAAILIQSKFRSYYEQKRFQQSRRAAVLIQNFYRSYKKCGRRRPARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLRRCRHSPLVDHRLYKRSERIEKGQGT | null | null | neuromuscular process controlling balance [GO:0050885]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; sequence-specific DNA binding [GO:0043565]; transcription coregulator activity [GO:0003712] | PF12796;PF03859;PF01833; | 1.20.5.190;1.25.40.20;2.60.40.10; | CAMTA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6Y1, ECO:0000255|PROSITE-ProRule:PRU00767}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Y1}. | null | null | null | null | null | FUNCTION: Transcriptional activator. {ECO:0000250}. | Mus musculus (Mouse) |
A2A8L1 | CHD5_MOUSE | MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSSKGKRKKKEGSNDEMSDNEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKEKKEKRKKRGEDEDDNDDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQTLPIRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEREDSDLDNASIHSSSVRSECSAALGKKNKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDEEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFVVGLPGPEVEPGMPPPRPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMVHRILNHSFDKKGDIHYLIKWKDLPYDQCTWEIDEIDIPYYDNLKQAYWGHRELMLGEDARLPKRLVKKGKKLKDDKQEKPPDTPIVDPTVKFDKQPWYIDATGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRGGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPTTPIPDIQSTKGGSLTAGAKKKHGSTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREVIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLVPEGAEGKKPGEVISSDPNTPVPASPAQLPPAPLGLTDKMEAQLGYTDEKESGMQKPKKSLEIQTLPTALDRVEGEDKHQSSDSKDRAREERTEEVEKAQGSPEQPLKEEVLPDKEPIPDKPELSLGHSGDFRPDDPKTEEKEPGETQQNGDREEDEEGKKEDKNGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYEIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEIHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQTSSRRRDFPLFQRSFPAEPSHLPNPRGREKLQPF | 3.6.4.12 | null | cerebral cortex neuron differentiation [GO:0021895]; chromatin remodeling [GO:0006338]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; regulation of cell differentiation [GO:0045595]; sperm DNA condensation [GO:0035092]; transcription by RNA polymerase II [GO:0006366] | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; NuRD complex [GO:0016581] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; H3K27me3 modified histone binding [GO:0061628]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872] | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | PTM: Methylated at Gln-1392 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23318260, ECO:0000269|PubMed:23948251}. Chromosome {ECO:0000269|PubMed:27806305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription (PubMed:23318260). May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 (PubMed:23318260, PubMed:23948251). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:27806305). Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation (PubMed:23948251, PubMed:27806305). In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages (PubMed:23948251). Regulates the expression of genes involved in cell proliferation and differentiation (PubMed:17289567). Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation (PubMed:17289567). In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa (PubMed:24252660). {ECO:0000269|PubMed:17289567, ECO:0000269|PubMed:23318260, ECO:0000269|PubMed:23948251, ECO:0000269|PubMed:24252660, ECO:0000269|PubMed:27806305}. | Mus musculus (Mouse) |
A2A8L5 | PTPRF_MOUSE | MAPEPAPGRRMVPLVPALVMLGLMAGAHGDSKPVFVKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEDQLPSGFPTIDMGPQLKVVEKGRTATMLCAAGGNPDPEISWFKDFLPVDPAASNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVMRSANYTCVAISSLGMIEATAQVTVKALPKPPIDLVVTETTATSVTLTWDSGNTEPVSFYGIQYRAAGTDGPFQEVDGVASTRYSIGGLSPFSEYAFRVLAVNSIGRGPPSEAVRARTGEQAPSSPPRRVQARMLSASTMLVQWEPPEEPNGLVRGYRVYYTPDSRRPLSAWHKHNTDAGLLTTVGSLLPGITYSLRVLAFTAVGDGPPSPTIQVKTQQGVPAQPADFQANAESDTRIQLSWLLPPQERIVKYELVYWAAEDEGQQHKVTFDPTSSYTLEDLKPDTLYHFQLAARSDLGVGVFTPTVEARTAQSTPSAPPQKVTCVSTGSTTVRVSWVPPPADSRNGIITQYSVAYEAVDGEDRKRHVVDGISREHSSWDLLGLEKWTEYRVWVRAHTDVGPGPESSPVLVRTDEDVPSGPPRKVEVEPLNSTAVHVSWKLPVPNKQHGQIRGYQVTYVRLENGEPRGQPIIQDVMLAEAQETTISGLTPETTYSITVAAYTTKGDGARSKPKVVTTTGAVPGRPTMMVSTTAMHTALLQWHPPKELPGELLGYRLQYRRADEARPNTIDFGKDDQHFTVTGLHKGATYVFRLAAKNRAGPGEEFEKEITTPEDVPSGFPQNLRVTGLTTSTTELTWDPPVLAERNGHITNYTVVYRDINSQLELQNVTNDTHLTLLGLKPDTTYDIKVRAHTSKGAGPLSPSIQSRTMPVEQVFAKNFRVAAAMKTSVLLSWEVPDSYKSAVPFKILYNGQSVEVDGHSMRKLIADLQPNTEYSFVLMNRGSSAGGLQHLVSIRTAPDLLPQKPLPASAFIEDGRFSLSMPQVQDPSLVRWFYIVVVPIDRVGGNLLAPRWNTPEELELDELLEAIEQGEEKQRRRRRQAERLKPYVAAQVDVLPDTFTLGDKKSYRGFYNRPLSPDLSYQCFVLASLKEPMDQKRYASSPYSDEIVVQVTPAQQQEEPEMLWVTGPVLAVILIILIVIAILLFKRKRTHSPSSKDEQSIGLKDSLLAHSSDPVEMRRLNYQTPGMRDHPPIPITDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNSEVNKPKNRYANVIAYDHSRVLLTSIDGVPGSDYINANYIDGYRKQNAYIATQGPLPETMGDFWRMVWEQRTATVVMMTRLEEKSRVKCDQYWPVRGTETYGLIQVTLVDTVELATYTMRTFALHKSGSSEKRELRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPLDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYVFIHEALLEAAMCGHTEVLARNLYAHIQKLGQVPPGESVTAMELEFKLLANSKAHTSRFVSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAESTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT | 3.1.3.48 | null | cell migration [GO:0016477]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell projection organization [GO:0031345]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of neurotrophin TRK receptor signaling pathway [GO:0051387]; negative regulation of receptor binding [GO:1900121]; nervous system development [GO:0007399]; neuron projection regeneration [GO:0031102]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of apoptotic process [GO:0043065]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of axon regeneration [GO:0048679]; regulation of neuron projection development [GO:0010975]; regulation of postsynapse organization [GO:0099175]; regulation of synapse structure or activity [GO:0050803]; synaptic membrane adhesion [GO:0099560] | endosome [GO:0005768]; excitatory synapse [GO:0060076]; growth cone [GO:0030426]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; postsynaptic density membrane [GO:0098839]; receptor complex [GO:0043235] | cell adhesion molecule binding [GO:0050839]; chondroitin sulfate proteoglycan binding [GO:0035373]; heparin binding [GO:0008201]; insulin receptor binding [GO:0005158]; phosphate ion binding [GO:0042301]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00041;PF07679;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2A8U2 | TM201_MOUSE | MEGVSALLASCPTAGLAGGLGVTACAAAGVVLYRIARRVKPTHTMVNCWFCNHDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYMEHLNHVVSSVPSPRDPAQPQQWVSSQVLLCRRCSHHQTTKIKQLAAFTPREEGRYDEEIEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFRRREADQAHGQSFSSSAVKAPFQVILLRALAFLACAFLLFTTLYGPSEPFTPGAALPPALPPGGNSSAASDNTTSQAEGWQQLLGLLPEHATEKLHEAWAFGQSHQTSIVAVGLLTCLLAMLLAGRIRLRRIDAFSTCLWALLLGLHLAEHYLQAASPGWLDTLKFSTTSLCCLVGFTAAVATRKSTGPRRFRPRRYFSGDSASLFPSSPSLAVPYPSVTSSPASLFIPTPPGFLPLTKQQLFRSPRRVSPSSLPGRLSRALSLGTIPPLTRTDSGYLFSGSRPPSRVSPAGEVSLSDYFSLLSSSFPASPLPSPAPSVASSVASSSGSLRHRRPLISPARLNLKGQKLLLFSSPGEAPNTPSSSEEFSPPNGSLFIESPQLPQRNHTRDTKHTMEMRSMLARDSARSSHSIKKEDESSQSSTCVVDTTTKGCSEETTPWKARVSPSLVRGLLAVSLAVNALFTSAYLYQSLR | null | null | fibroblast migration [GO:0010761]; nuclear migration [GO:0007097]; nuclear migration along microtubule [GO:0030473] | nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965] | actin filament binding [GO:0051015]; lamin binding [GO:0005521] | PF10476;PF09779; | null | TMEM201 family | null | SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q5SNT2}. | null | null | null | null | null | FUNCTION: Involved in nuclear movement during fibroblast polarization and migration (PubMed:22349700). May recruit Ran GTPase to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}.; FUNCTION: [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle. Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina. {ECO:0000250|UniProtKB:Q5SNT2}.; FUNCTION: [Isoform 3]: Proposed to be involved in actin-dependent nuclear movement; via SUN2 associates with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow. {ECO:0000305|PubMed:22349700}. | Mus musculus (Mouse) |
A2A935 | PRD16_MOUSE | MRSKARARKLAKSDGDVVNNMYEPDPDLLAGQSAEEETEDGILSPIPMGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEMLTDTEVSSQESCIKKQISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAPSLDEDPTFRCDECDELFQCRLDLRRHKKYACSSAGAQLYEGLGEELKPEGLGVGSDGQAHECKDCERMFPNKYSLEQHMIVHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKRFECENCVKVFTDPSNLQRHIRSQHVGARAHACPDCGKTFATSSGLKQHKHIHSTVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHYTPGSIFTPGLPLTPSPMMDKTKPSPTLNHGGLGFSEYFPSRPHPGSLPFSAAPPAFPALTPGFPGIFPPSLYPRPPLLPPTPLLKSPLNHAQDAKLPSPLGNPALPLVSAVSNSSQGATAATGSEEKFDGRLEDAYAEKVKNRSPDMSDGSDFEDINTTTGTDLDTTTGTGSDLDSDLDSDRDKGKDKGKPVESKPEFGGASVPPGAMNSVAEVPAFYSQHSFFPPPEEQLLTASGAAGDSIKAIASIAEKYFGPGFMSMQEKKLGSLPYHSVFPFQFLPNFPHSLYPFTDRALAHNLLVKAEPKSPRDALKVGGPSAECPFDLTTKPKEAKPALLAPKVPLIPSSGEEQPLDLSIGSRARASQNGGGREPRKNHVYGERKPGVSEGLPKVCPAQLPQQPSLHYAKPSPFFMDPIYRVEKRKVADPVGVLKEKYLRPSPLLFHPQMSAIETMTEKLESFAAMKADSGSSLQPLPHHPFNFRSPPPTLSDPILRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCNRCFGQQTNLDRHLKKHEHEGAPVSQHSGVLTNHLGTSASSPTSESDNHALLDEKEDSYFSEIRNFIANSEMNQASTRMDKRPEIQDLDSNPPCPGSASAKPEDVEEEEEEELEEEDDDSLAGKSQEDTVSPTPEPQGVYEDEEDEEPPSLTMGFDHTRRCVEERGGGLLALEPTPTFGKGLDLRRAAEEAFEVKDVLNSTLDSEVLKQTLYRQAKNQAYAMMLSLSEDTPLHAPSQSSLDAWLNITGPSSESGAFNPINHL | 2.1.1.367 | null | brown fat cell differentiation [GO:0050873]; heterochromatin organization [GO:0070828]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of granulocyte differentiation [GO:0030853]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neurogenesis [GO:0022008]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cellular respiration [GO:0043457]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; somatic stem cell population maintenance [GO:0035019]; stem cell population maintenance [GO:0019827]; tongue development [GO:0043586]; white fat cell differentiation [GO:0050872] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9me2 methyltransferase activity [GO:0140947]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; SMAD binding [GO:0046332]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712] | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | PRDM16 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAZ2}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367; Evidence={ECO:0000269|PubMed:22939622}; | null | null | null | null | FUNCTION: Binds DNA and functions as a transcriptional regulator (PubMed:18483224). Displays histone methyltransferase activity and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (PubMed:22939622). Probably catalyzes the monomethylation of free histone H3 in the cytoplasm which is then transported to the nucleus and incorporated into nucleosomes where SUV39H methyltransferases use it as a substrate to catalyze histone H3 'Lys-9' trimethylation (PubMed:22939622). Likely to be one of the primary histone methyltransferases along with MECOM/PRDM3 that direct cytoplasmic H3K9me1 methylation (PubMed:22939622). Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism (PubMed:17618855, PubMed:18483224). Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells (PubMed:18719582, PubMed:19641492). Functions as a repressor of TGF-beta signaling. {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:22939622}. | Mus musculus (Mouse) |
A2A974 | CP4CB_MOUSE | MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKAHGSYRFLAPWIGRGLLLLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVHVMLDKWEQIVGQDSTLEIFQHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNNLFFLRVRNIFHQNDIIYRVSSNGCLANSACQLAHDHTDQVIKSRRSQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGASITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKLQ | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P20817}; | arachidonic acid metabolic process [GO:0019369]; fatty acid metabolic process [GO:0006631]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651]; omega-hydroxylase P450 pathway [GO:0097267] | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; arachidonic acid omega-hydroxylase activity [GO:0052869]; aromatase activity [GO:0070330]; fatty acid omega-hydroxylase activity [GO:0120250]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39811, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63590; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76627; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76624; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39791, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76639; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39783, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76635; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784; Evidence={ECO:0000305|PubMed:17112342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:17112342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000305|PubMed:17112342}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for dodecanoic acid {ECO:0000269|PubMed:17112342}; KM=43 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (without cytochrome b5) {ECO:0000269|PubMed:17112342}; KM=72 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (with cytochrome b5) {ECO:0000269|PubMed:17112342}; KM=41 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (without cytochrome b5) {ECO:0000269|PubMed:17112342}; KM=62 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (with cytochrome b5) {ECO:0000269|PubMed:17112342}; Vmax=40 nmol/min/nmol enzyme toward dodecanoic acid {ECO:0000269|PubMed:17112342}; Vmax=10 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (without cytochrome b5) {ECO:0000269|PubMed:17112342}; Vmax=19 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (with cytochrome b5) {ECO:0000269|PubMed:17112342}; Vmax=15 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (without cytochrome b5) {ECO:0000269|PubMed:17112342}; Vmax=30 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (with cytochrome b5) {ECO:0000269|PubMed:17112342}; | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:17112342}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:17112342). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:17112342). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids (PubMed:17112342). May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney (PubMed:17112342). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:17112342). Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoc acid (EPA). Catalyzes the epoxidation of the last double bond of EPA with no preferred stereoselectivity, producing both (R,S) and (S,R) stereoisomers (PubMed:17112342). Can also catalyze the omega-1 and omega-2 oxidation of fatty acids with lower efficiency (PubMed:17112342). {ECO:0000269|PubMed:17112342}. | Mus musculus (Mouse) |
A2A9A2 | DMTA2_MOUSE | MELRSELPSVPGAATAAATATGPPVASVASVAAAAAAAASLPVSVAGGLLRAPPLLLRAAEKYPRTPKCARCRNHGVVSALKGHKRYCRWKDCLCAKCTLIAERQRVMAAQVALRRQQAQEENEARELQLLYGTAEGLALAAANGIIPPRPAYEVFGSVCATDGGGPGAGAPAGSAGGAGGAEAKLQKFDLFPKTLLQAGRPDSPQPPPGKPLSPDGADSGPRTSSPEVRPGSGSENGDGESFSGSPLARASKEAGGSCPGSAGAGGGGEEDSPGSSSPLGSESGSEADKEEAEAAPTPGLGGGPGPRQRTPLDILTRVFPGHRRGVLELVLQGCGGDVVQAIEQVLNHHRGGLAAGLGPAAPLEKAAVSAAVEDAWPGRVEAAAAGGAGLPAPLQTGPTAPPHHRPLLAGAMTPGALGSLSSRSAFSPLQPNASHFGADAGAYPLGAPLGLSPLRLAYSAAAAHSRGLAFMAPYSTAGLVPTLGFRPPMDYAFSDLMRDRSAAAAAAVHKEPGYGGGLYGPMVNGTPEKQ | null | null | cerebral cortex regionalization [GO:0021796]; dopaminergic neuron differentiation [GO:0071542]; germ cell development [GO:0007281]; neuroblast proliferation [GO:0007405]; neuron fate specification [GO:0048665]; positive regulation of neuroblast proliferation [GO:0002052]; regulation of transcription by RNA polymerase II [GO:0006357]; sex differentiation [GO:0007548]; skeletal muscle cell differentiation [GO:0035914]; stem cell differentiation [GO:0048863]; stem cell fate specification [GO:0048866] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00751;PF03474;PF20624; | 4.10.1040.10; | DMRT family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. | null | null | null | null | null | FUNCTION: May be involved in sexual development. | Mus musculus (Mouse) |
A2A9C3 | SZT2_MOUSE | MASERPEPEVEEAGQVFLLMKKDYRISRNVRLAWFLNHLHQTVQATPQELLLQSEQELEVLSVLPPGWQPDEPVVPRPFLLVPSTRVTFLAWQYRFVIELDLSPSTGIVDDSTGEILFDEVFHALSRCLGGLLRPFRVPGSCINFQPEIYVTIQAYSSIIGLQSHQVLVQGCLLDPSQREAFLQQVYEQLCLFEDKVATMLQQQYEPQGQAEDQSPESGESLGRKVGVSMVTADLGLVSMIRQGILALQLLPSNSSAGIIVITDGVTSVPDVAVCETLLNQLRSGTVACSFVQVGGVYSYDCSFGHVPNVELMKFIAMATFGSYLSTCPETEPGNLGLTVYHRAFLLYSFLRSGEALNPEYYCGSQHRLFNEHLVSASSNPALALRRKKHTEKEVPADLVSTVSVRLREGYSVREVTLAKGGSQLEVKLVLLWKHNMRIEYVAVAPWPLEPEGPRGTRVEVTMEGGYDILHDVSCALRQPIRSLYRTHVIRRFWNTLQSINQTDQMLAHLQSFSSVPEHFTLPDSTKSGVPLFYIPPGSSTPVLSLQHSGSDSSHAQFAAYWKPVLSMDANSWQRWLHMHRLVLILEHDTPLPKHLHTPGSNGRYSTIQCRISHSSLTSLLRDWSSFVLVEGYSYVKLLSSAPDQPPSSFYMVRIISKTPCMVLRLGFPIGTPAQARHKIVSGLKEEILRLRFPHRVQSKEPTPKVKRKGLGGVGGSSPSKSPPTLGPQQALSDRPCLVVLHKPLDKLLIRYEKLPLDYRAPFLLTLEPPGPLPLVSGRSASSSLASLSRYLYHRRWLWSVPSGLAPTLPLSATAQLLSVLTEVRLSEGFHFACSGEGIINMVLELPVQNEPLGQAAAEEKHTCVVQYILFPPHSTSTKDSFSTDDDNDVEVEALEGDSELNLVTEVWVEPQYGRVGPGPENWKHLQDLTYSEIPQALHPRDAACIGSLLTFEYLIQLCQSKEWGPLPPEPRLSDGLDQRGDTCVHEIPFHFDLLGLLPQCQQLQMFFLLLSREPEGVPLAEGPCPTNDMVLCLLHSCLGQELSDREIPLTPADQAAFLNEVLRRSLRDPGPEGPPVGGHAVAKDRAGNSTQASGDSTLPSQSVVIPGVLRSSISAQPPQWHCYARLLGPQHVFLTFLPATFSDVQHLTAYGLESSFQEETKPKLGDWSGAPSLKDPGATGTKATESQVPTLSVTLASDSAQDSGEPSTPSCQDLAANSGRQAPQTEGADGPRTRCPVYIYSCSLEALREQMVGLQPPQAPRDLIFRAQDLDHPSSSSAWMEPRCKEAATHCALLQEHAQRCFVRGLFRSLQQAQSVTCQDLLTAVDACEELLQEIDITSFLLALCGHTWGLPHAPPSPGPLSPGPFSSSIEEGPEPRERAILVSESSIETEDLSEPEFQSSRVSGNLDPGPEISLTDVCQLRGEAHDALHSLIQEKFLEISRLHFRTVPSNPHYFFYCPPSSRREDEGPRDTVDRKISDLEFSEAELVGEEGDTSACCVVTESDPELEVEYRESREPDLGPAGLDSASLSDADTVNPDEDSFSILGGDSPTGPDSLMHDLPPLFLHLTCSVRLRGQHSSVPVCSLPTCLGQVLSSLEGPPIGGRVPLRDLSITLDVFVLTLPLEVELPPASDPQHHRSTSESSASFPRSPGQPSSLRSDDGLGPPLPPPEEERHPGLSSLAMPHRLAIESTMNEIRWLLEDEMVGALRRGGIPQSPALHRAAAHIHSSSGRPTCLRQAPPLSFVFGPERSLTQFKEEFRRLHLPGHVLLEDPDSGFFFVAAGQQPGVLHGEPPSAAWAWHNHEDRAEDAEGEVLTASPQVPGSLEDSEGTPLISLPSLSQGGSQPGPSRGLSLMSSQGSVDSDHLGYDGGSSGSDSEGPGETLGEKALFTLRTPPGPAPPQPSLPVLPGPSLPDFWLIVRILQDRVEVYAHARSLSREDGGPGAECRHLQQFLVRRVGEICREVNQRLLLQDLHDSHVCNSLLVAESEEDLWRSETPFHSRQRAVLPSDDFAADESCAPRGYLAATMQFVPGHFSCDVVWGTVIRVHSRLKMGPSMGVSRAIQALRSVLNAFSVVNRKNMFVYQERATKAVYYLRLLETSCSDRPWEGDTLPPSLALSRSQEPISSEDSVAPRSPLDMASSRSSDAVRPVGQVDRHIQLLVHGVGQAGPEITDELVRVLRRRLDEATLDIITVMLVRNCKLTPADVEFIQPPGSLPSEVLHLVLPPSCRPCLPALAWYLRQNLLTFLHSPKYTDSNSRNHFQHPLPAQGGLPDLDIYLYNKPGGQGTGGKGVACITLAFVEEGGTPISLASWPPSSPGPPDPLREEEFEQLTQVIRCPNTLDSCSAQDGSPRLRLDVWEKGNISIVQLEEKLRAAARQALADAIMELRLLPASLCTEDIPPGSLKSGPLDTKSPACRANTFPCTPVSGEPVTPPSKAGRRSFWDMLSKTEAGDLGSPKTTDDIVLDRPEDTRGRRRHKTENVRTPGGSERAPGPDSGAQRQRRRTTQLEEGEVGTLHPVFARVIQRWMGFMVQIGCASVSRSSTHMVSRFLLPSILSEFTTLVISMAGDTSVRVFEQHLGSEPDVFSPCSPGQLGPAPRPAAQRHLLLLGRNFAQWRRPTQQAAKAVQRFESGGDGSPGRSAPRQRLLLLEVTDKKLQLLTYNWAPDLGAALGRALIRLVQWQNARAHLISCLLSQKLGLFHHCGQLDFPMRDGKEPNPFLLPTMEVETLIRNASPPLSREQGRLSGSSRGGGPLSLDTFPFDEALRDITAARPSSTGGPAPRPPDPVTYHGQQFLEIKMTERKELERQMKMENLFVTWQQRSAPASMPISAGELETLKQSSRLVHYCATALLFDPAAWLHGPPETCAPSEGQRRPCPESGSGSREVPTSCESLDVPPPGAREEPWLKELSLAFLQQYVQYLQSIGFVLVPLRPPSPARSTSRLRAMAILGTEGRGSFSCPKAKAEGSPKSTSTPVTTYHLQRALPGGIILMELTFQGCYFCVKQFALECSRIPMGQAVNSQLSLLFTEECDKVRDLMHVHSFSYDFHLRLVHQHVLGAHLALRHGYHLTTFLQHFLAHHPDGPHFGRNHIYQGTLELPTPLIAAHQLYNYVADHASSYHMKPLRMARPGGPEHNEYALVSAWHSSGSYLDSEGLRHQDDFDVSLLVCHSAAPFEEQGEAERHVLRLQFFVVLTSQRELFPRLTADMRRFRKPSRLPLEPETPGSLVGSPREASGMMLAPGPAPLFPPLAAEVGMARARLAQLVRLAGGHCRRDTLWKRLFLLEPPGPDRLRLGGRLALAELEELLEAVHAKSIADIDPQLDCFLSMTVSWYQSLIKVLLSRFPQSCRHFQSPDLGTQYLVVLNQKFTDCFVLVFLDSHLGKTSLTVVFREPFPVQPQDSESPPAQLVSTYHHLESVINTACFTLWTRLL | null | null | cellular response to amino acid starvation [GO:0034198]; cellular response to glucose starvation [GO:0042149]; central nervous system development [GO:0007417]; corpus callosum morphogenesis [GO:0021540]; negative regulation of TORC1 signaling [GO:1904262]; pigmentation [GO:0043473]; post-embryonic development [GO:0009791]; protein localization to lysosome [GO:0061462]; regulation of superoxide dismutase activity [GO:1901668]; response to nutrient levels [GO:0031667] | GATOR1 complex [GO:1990130]; GATOR2 complex [GO:0061700]; KICSTOR complex [GO:0140007]; lysosomal membrane [GO:0005765]; peroxisome [GO:0005777] | null | null | null | null | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q5T011}. Peroxisome {ECO:0000269|PubMed:20045724}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q5T011}. | null | null | null | null | null | FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids (By similarity). In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose (PubMed:28199306, PubMed:28199315). May play a role in the cellular response to oxidative stress (PubMed:20045724). {ECO:0000250|UniProtKB:Q5T011, ECO:0000269|PubMed:20045724, ECO:0000269|PubMed:28199306, ECO:0000269|PubMed:28199315}. | Mus musculus (Mouse) |
A2A9F4 | KDF1_MOUSE | MPRPGQPRPSSGPPRLGPWERPSELCLETNDERSQPPPGRRTRRPDPKDPGHHGPESITFISGSAEPANEPPTCCLLWRPWGWDWCRAAFCFRRCRDCLQRCGACVRGCSPCLSAGDPIEGSAEAAWAKEHNGVPPSPDRAPPSRRDGQRLKTSMGSSFSYPDVKLKGIPVYPYRHATSPVPDVDSCCKEPLAEPPPTRHSLPSTFTNSPRGSEEYYSFHESDLDLPEMGSGSMSSREIDVLIFKKLTELFSVHQIDELAKCTSDTVFLEKTSKISDLISSITQDYHLDEQDAEGRLVRGIIRISTRKSRSRPQTSEGRSARSTAPAAAPDSGHETMLGSGLSQDELTVQISQETTADAIARKLRPYGAPGYPASQDSSFQGTDTDSSGAPLLQVYC | null | null | developmental growth [GO:0048589]; establishment of skin barrier [GO:0061436]; keratinocyte development [GO:0003334]; keratinocyte proliferation [GO:0043616]; limb epidermis development [GO:0060887]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of stem cell proliferation [GO:2000647]; positive regulation of epidermal cell differentiation [GO:0045606]; regulation of epidermal cell division [GO:0010482]; stem cell proliferation [GO:0072089] | anchoring junction [GO:0070161]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737] | null | PF15551; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24075906}. Cell junction {ECO:0000269|PubMed:24075906}. Note=Localized at cell borders in single layered keratinocytes. Localized at cell borders in the basal and spinous layers but is more diffusely localized in the granular layer. Colocalized with actin near the cell membrane, especially in cellular protrusions. | null | null | null | null | null | FUNCTION: Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny. {ECO:0000269|PubMed:24075906}. | Mus musculus (Mouse) |
A2AA28 | MET23_MOUSE | MDSVRPRAPWAPPPDPASLDSPTCEPGLMAGTQLFRFREEPVPGGNRAVLEVRVPQVLHVQYGMYVWPCAVVLAQYLWFHRRSLPGKAVLEVGAGVSLPGILAAKCGAKVILSDSSEFPHCLDICRQSCQMNNLPQVEVVGLTWGHISKDILSLPPQDIILGSDVFFEPEDFESILATVYFLMQKNPKVQFWSTYQVRSADWSLEGLLYKWDMKCVHIPLESFDADKEDIAESTLPGRHTVEMLIISFAKDSF | 2.1.1.319 | null | cognition [GO:0050890]; epigenetic programing of male pronucleus [GO:0044727]; epigenetic programming in the zygotic pronuclei [GO:0044725]; methylation [GO:0032259]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | DNA-binding transcription factor binding [GO:0140297]; heat shock protein binding [GO:0031072]; histone H3R17 methyltransferase activity [GO:0035642]; histone methyltransferase activity [GO:0042054]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-lysine N-methyltransferase activity [GO:0016279] | PF10294; | 3.40.50.150; | Methyltransferase superfamily, METTL23 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28930672}. Cytoplasm {ECO:0000269|PubMed:28930672}. Note=Localizes in male and female zygote pronucleus and cytoplasm. {ECO:0000269|PubMed:28930672}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; Evidence={ECO:0000269|PubMed:28930672}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097; Evidence={ECO:0000269|PubMed:28930672}; | null | null | null | null | FUNCTION: Histone methyltransferase that dimethylates histone H3 at 'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling (PubMed:28930672). Maternal factor involved in epigenetic chromatin reprogramming of the paternal genome in the zygote: mediates H3R17me2a, promoting histone H3.3 incorporation in the male pronucleus, leading to TET3 recruitment and subsequent DNA demethylation (PubMed:28930672). {ECO:0000269|PubMed:28930672}. | Mus musculus (Mouse) |
A2AAE1 | BLTP1_MOUSE | MDQRKNDSIVPSITQLEDFLTEHNSNVVWLLVATILSCGWIIYLTYYNSRNVGLILTLVLNRLYKHGYIHIGSFSFSVLSGKVMVREIYYITEDMSIRIQDGFIIFRWWKMYNPKQKQHDPKAETRLYITVNDFEFHVYNRSDLYGRLQELFGLEPTIIPPKKDDDKTRENGRTRTQSKIERVKVKTESQDPTSSWRSLIPVIKVNVSTGRLAFGNHYQPQTLCINFDDAFLTYTTKPPSSHLDQFMHIVKGKLENVRVMLVPSPRYVGLQNDEPPRLMGEGFVVLQSNDVDLYYYMDEPGLVPEETEESTEGDISSEDCKLQDLPPCWGLDIVCGKGTDFNYGPWADRQRDCLWKFFFPPDYQVLKVSEIAQPGRPRQILAFELRMNIITDATIDLLFTKNRETNAVHVNVGAGSYLEINIPMTVDENGYTPAIKGQLLHVDATTSMQYRTLLEAEMLAFHINASYPRIWNMPQTWQCELEVYKATYHFIFAQKNFFTDLIQDWSSDNAPDIFSFVPYTWNFKIMFHQFEMIWAANQHNWIDCSTKQQENVYLAACGETLNIDFSLPFTDFVPATCNTRFSLRGEDVDLHLFLPDCHPSKYSLFMLVKNCHPNKMVPETGIPAECQSGQKTVKPKWRNVTQEKAGWVECWTVPSVMLTIDYTWHPIYPQKADEQLKQSLSEMEETMLSVLRPAQKTSERVVSSPSMSPRPPVDPSELPPDKLHVEMELSPDSQITLYGPLLNAFLCIKENYFGEDDMYMDFEEVISSPVLSLSTSSSSGWTAVGMDNDKRENESSAKSIHPLALRPWDITVLVNLYKVHGRLPVHGTTDGPECPTAFLERLCFEMKKGFRETMLQLVLSPLNVFVSDNYQQRPPVDEVLREGHINLSGLQLRAHAMFSAEGLPLGSDSLEYAWLIDVQAGSLTAKVTAPQLACLLEWGQTFVFHVVCREYELERPKSVIVCQHGIDRRFCESKLSCIPGPCPTSDDLKYTMTRLAIDGSDIYIVEHGCATNIKMGAVRIANCNLHNQSVGEGISAAIQDFQVRQYIEQLNNCRIGLQPAVLRRAYWLEAGSANLGLITVDIALAADHHSKHEAQRHFLETHDARTKRLWFLWPDDTLKNKRCRNKCGCLGGCRFFGGTVTGLDFFKLEELTPSSSSAFSSTSAESDMYYGQSLLQPGEWIITKEIPKTVDGNVNSMKRKEWENKSVGIEGERKTQHLSLQVPLRSHSSSSSSEENSSSSAAQPLLAGEKESPSSAADDHSVQKDLLHSARRDDGQASVPTEISGTSPVSPNTQDKSVGQSPLRSPLKRQASVCSTRLGSTKSLTAAFYGDKQPVTVGVQFSSDVSRSDENVLDSPKQRRSFGSFPYTPSADSNSFHQYRSMDSSMSMADSEAYFSAAEEFEPISSDEGPGTYPGRKKKKKQMQQIDYSRGSIYHSVEGPLAVHGEGITDPRTLPFKTHPSQASFVSALGGEDEVIEHVYIVEGEKRGESEQVTSQQPVMSCYHTYLTQFQVINWSVKHPTNKRTSKSSLHRPLDLDTPTSEESSSSFEQLCVPTFKVIKQGLTANSLLDRGMQLSGSTSNTPYTPLDKKIVDTTDDETLTEEWTLDQPVAQTKTTAIVEVKGTVDVVLTPLVAEALDRYIEAMVHRVSTRHPAAIVDDLHTKVLREAVQNSKTTFSENLSPKQDIRGTKTEHPMIGTTNQGQIQTNVTTKQDNVTIKGLQANVSIPKVNLCLLQASVEESPATVPSRSVTHVSLVALCFDRIATQVRMNRGVVEETANNVDAGKTSNFDRYVHASKMQPQSSGSLRSNAGAEKGKEIAAKLNIHRVHGQLRGLDTTDIGTCAITAIPFEKSKVLFTLEELDEFTFVDETDQQAIPDVTRIGPSQEKWGWIMFECGLENLTIKGGRQSGAVLYNSFGIMGKNSVTERGGVLTSNNSSDSPTGSGYNTDVSDDNLPCDRTSPSSDINGNSVSDEQDEGVESDDLKKDLPLMPPPPDSCSMKLTIKEIWFSFAAPTNVRSPAHAFSRQLNLLSTATPAVGAWLVPIDQLKSSLNKLETEGTLRICAVMGCIMTEALENKSVHFPLRSKYNRLTKVARFLQENPSCLLCNILHHYLHQANYSIIDDATMSDGLPALVTLKKGLVALARQWMKFIVVTPAFKGVSLHRPAQPLKPPATVDQEHEEGLGLDNGGGLQSDTSADGAEFEFDAATVSEHTMLLEGTANRPPPGSSGPVTGAEIMRKLSKTHTHSDSALKIKGIHPYHSLSYTSGDTATDSPVHVGRAGMPVKESPRKESLLSYLTGSFPSLHNLLEGTPQRSSAAVKSSSLTRTGNTVATDMLSEHPLLSEPSSVSFYNWMSNAVGNRGSVVQESPVTKSGHNSLPTGVAPNLPTIPSASDFNTVLSSDQNTLDGTHSQHSTSQDDVAGVEEANQGFPAVQLADAQVVFKPLLSHTGIQSQDTMPLCYRMYFGEHLSFSGTLDCLRADIVDSDTAKDRKGKRARRQGHVNLPPLEFKPALMLETFSISAVVMEKSVCTPQNSTSALSFHDLNKRYYNTFHCNFTISCQSISQHVDMALVRLIHQFSTMIDDIKATQTDIKLSRYTAGSASPTPTFKTRKHRDFRSSDFSRSSRGSLNGGNRVNNAKNKRANNENNKKESRNKNSLGRSERRTSKVSRKGSKDVVDHMTIHMDDSDSITVSEQSEPSAECWQNMYKLLNFYSLISDPTGILEKSSETFGPAGVRSPTEPTCRVVFENEQDNNSLTKTQRKRSLVTSEPQHVTLIVFGIGMVNRTHLEADIGGLTMESELKRIHGSFTLKEKMKDVLHQKMTETCATAHIGGVNIVLLEGITPNIQLEDFPTSPTSTAKQEFLTVVKCSIAKSQALYSAQRGLKTNNAAVFKVGAISINIPQHPATLHSMMVRSSHQLSKQISDLIRQPSTAPQPMKEDIATPLPSEKTPTSVNQTPIETNEFPQLPEGLEKKPIVLKFSAMLDGIAIGAALLPSLKAEYKMGRMRSHGMTGAQTRFTFELPNHRLRFTSKVSATDMSTIPPSASLNLPPVTMSGKYIMEEHDSYSDQVWSIDELPSKQGYYLQGNYLRCVAEVGSFEHNLTTDLLNHLVFVQKVFMKEVNEVIQKVSGGEQPIPLWNEHDGTTDGDKPKILLYSLNLQFKGIQVTATTPSMRAVRFETGLIELELSNRLQTKASPGSSSYLKLFGKCQVDLNLALGQIVKHQVYEEAGSDFHQVAYFKTRIGLRNALREEISGSSDREAVLITLNRPIVYAQPVAFDRAVLFWLNYKAAYDNWNEQRMALHKDIHMATKEVVDMLPGIQQTSAQAFGTLFLQLTVNDLGICLPITNTAQSNHTGDLDTGSALVLTIESTLITACSSESLVSKGHFKNFCIRFADGFETSWDDWKPEIRGDLVMNACVVPDGTYEVCSRTTGQAAAESSSAGTWTLNVLWKMCGIDVHMDPNIGKRLNALGNTLTTLTGEEDIDDIADLNSVNIADLSDEDEVDTMSPTIHTEAVDYRRQGTSSSQPGELRGRKIMKRLVDIRELNEQAKVIDDLKKLGASEGTINQEIQRYQQLESVAVNDIRRDVRKKLRRSSMRAASLKDKWGLGYKPSYSRSKSISASGRPPLKRMERASSRIGETDELPEIRVDAASPGPRVTFNIQDTFPEETELDLLSVTIEGPSHYSSNSEGSCSVFSSPKTTGGFSPSVPFQSEDGRRDDSLSSTSEDSEKDEKDEDRERERFYIYRKPSHTSRKKATGFAAVHQLLTERWPTTPVNRSLSGTATERNIDFELDIRVEIDSGKCVLHPTTLLQEHDDISLRRSYDRSSRSLDQDSPSKKKKFQTNYASTTHLMTGKKVPSSLQTKPSDLETTVFYIPGVDVKLHYNSKTLKTESPNASRGSSLPRTLSKESKLYGMKDSAASPSPSPLPCTVQSKTNTLLPPQPPPIPSAKGKGSGGVKTAKLYAWVALQSLPEEMVISPCLLDFLEKALETIPITPIERNYTAVSSQDEDMGHFDIPDPMEESTTSLVSSSTSAYSSFPVDVVVYVRVQPSQIKFSCLPVSRVECMLKLPSLDLVFSSNRGELETLGTTYPAETVSPGSNAPQTGAKTSASKAGMPGSSGLGSPLGRSRHSSSQSDLTGSSSSSSGLSFTACMSDFSLYVFHPYGAGKQKSTVSGLTSGSGGLGNVDEEPTSVTGRKDSLSINLEFVKVSLSRIRRSGGASFFESQSVSKSTSKMDTTLINISAVCDIGSASFKYDMRRLSEILAFPRAWYRRSIARRLFLGDQTVNLPTSGPGTPDSIEGVSQHLSPESSRKAYCRTWDQPSQSASFTHMPQSPNVFNEHMTNNTMSPGTAAQSLKSPASIRSRSVSDSSVPRRDSISKTSTPVNKSNKAASQQGTPWETLVVFAINLKQLNVQMNMSNVMGNTTWTTSGLKSQGRLSVGSNRDREISMSVGLGRSQLDSKGGVVGGTIDVNALEMVAHISEHPNQQPNHKIQITMGSTESRVDYMGSSILMGIFSNADLKLQDEWKVNLYNALDSSMTDKSEIFVHGDLKWDIFQVMISRSTTPDLIKIGMKLQEFFTQQFDTSKRALSTWGPVPYLPPKTMTNNLEKNSQEQLLDAAHHRHWPGVLKVVSGCHISLFQVPLPEDGMQFGGSMSLHGNHMTLACFHGPNFRSKSWALFHLEEPNIAFWTEAQKIWEDGSSDHSTYIVQTLDFHLGHNTMVTKPCGALESPMATITKITRRRHENPPHGVASVKEWFNYVTATRNEELNLLRNVDANNTENSTTVKNSSLLSGFRGGSSYNHETETIFALPRMQLEFKSIHVQEPQEPSLQDASLKPKVECSVVTEFTDHICVTMDAELIMFLHDLVSAYLKEKEKAIFPPRILSTRPGQKCPLIIHDDSSSDRDREDSITYTTVDWRDFMCNTWHLEPTLRLISWTGRKIDPVGVDYILQKLGFHHARTTIPKWLQRGVMDPLDKVLSVLIKKLGTALQDEKEKKGKDKEEH | null | null | adipose tissue development [GO:0060612]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; fat cell differentiation [GO:0045444]; intermembrane lipid transfer [GO:0120009]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; nucleus localization [GO:0051647]; phagocytosis [GO:0006909]; regulation of cell growth [GO:0001558]; spermatogenesis [GO:0007283]; synaptic vesicle endocytosis [GO:0048488] | endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | phosphatidylethanolamine transfer activity [GO:1904121] | PF10479;PF21677;PF20413; | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-cell membrane and some endoplasmic reticulum-mitochondria contact sites. {ECO:0000250|UniProtKB:Q12150}. | null | null | null | null | null | FUNCTION: Tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum. Plays a role in endosomal trafficking and endosome recycling. Also involved in the actin cytoskeleton and cilia structural dynamics. Acts as a regulator of phagocytosis. {ECO:0000250|UniProtKB:Q2LD37}. | Mus musculus (Mouse) |
A2AAJ9 | OBSCN_MOUSE | MDHSFSGAPRFLTRPKAFVVSVGKDATLSCQIVGNPTPHVSWEKDRQPVEAGARFRLAQDGDVYRLTILDLALGDSGQYVCRARNAIGEAFAAVGLRVDSEGTCAEQAPHFLLRPTSIRVREGADATFRCRVGGSPQPAVSWSKDGRRLGPPDAPHVRVEEHGESSALRIRSARPRDGGTYEVRAENPLGSASAAAALVVDSDAEVAGPPGTSTATLLAHLQQRREAMRAEGIPPSPPGAGTRTCTVTEGKHARLSCFVTGEPKPETVWKKDGQLVTEGRRHVVYEDEQENFVLKILFCKQSDRGLYTCTASNLVGQTYSSVLVVVREPTVPFKKRLQDLEVREKESATFQCEVAQPATEAAWFKEETRLWASAKYDIEEEGTERRLTVRNVSADDDAVYICETTEGSRTVAELSVQGNLTRKLPRKTAVRTGDTAIFWVELAVPEGPVRWLRNQEEMVAGGRVAITAEGTCHTLTIFQCTLEDMGEVAFVSGGCRTTTQFCVSAPRRPPLYPPADPVVKAKTESSVTLSWSAPPHGDRPVTIDGYVLEKRKLGAYAWSRCHEAGWLATTEFTITGVAEEGDFQFRVSAINHFGQGPYLEFPGTMHLVPMLAVKTPLKAVEAVEGGEVTFSVDLTVASSGEWFLDGEALKASSIYVIRCDRTRHMLTIREVPARLHGAQLKFVANGIETSIQMVVRAALGLPSSKLPAAAAREVLAQLHEEAQLLAELSDQAAAVTWLKDGRELSLGPKYEMQVSAGRRALLVRDVAQDDAGLYECVSRGSRTAYQLLVQDITDGYRDWGPAGPQKHMCKCAGAKIARYLGSSCYRFLQYDKGVWHWLEAALDTRQGKGTSSCSLHEKPKLVFAKGQQAHSEVKAEAGNSATLSCEVTQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKGQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKMVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVTEPKLVFAKEQQARSEVKAEVGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQARSEVKAEAGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFHLDVTEPKLVFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAEGQKLSFRLDVAEPKLVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQANSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLFFRLDVAEPKLMFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQVGKADAGEYSCEARGQKLSFRLDVADTRLMFAKEQQARTEVKAEAGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEAESQIPERPSRREPLVVKEHETIILTATIAAPSVAAVTWLKDGVEIRRSKRHEATSLGDTHTLTVRGAQVLDSAIYSCRVGKEGQDFPVQVEEVAAKFSKPLEPVEGELGGTVMLVCELSPEQAEVVWRCGNTQLRPGKRFQMTSEGPRRTLTVSGLREDDAEEYVCESRDDRTSARLTVKVPRVVKFTSGLSAMVAEEGQEATFQCVVSPSDAGVTWYKDGMQLQPSEKFVMVESGASRSLTILGLTLEDAGQVTVEAEGASSSAALRVREAPVLFKKKLEPQTVEERTSVTLEVELTRPWPEVKWTRNAAVLTPSENVEIRAEGARHCLVLRSVGFADRGFFGCETPDDKTQAKLNVEMRQVRLVRGLQEVEAKEQGTASMDVELSHAEVEGSWTRDGLRLQPGPKCHLAVQGPVHILTLSALQPQDSGLVAFRAEGVHTSARLIVTELPVSFTRVLQDVVATQKEKVTLECELSRPVDVRWLKDGVELRAGKAIGIVAQGTCRSLVIYRCETGDQGVYVCDALDAQTSASLRVQGRTYTLIFRRVLAEDAGEVKFVAENAESRAHLRVKELPVTLLRPLRDKIAMEKHRGVLECQVSRASAQVRWFKGGVELQSGPKYEVVSDGLYRKLVINDVQPEDEDTYTCDAGNVKTSAQFFVEEQSITIVRGLKDMTVMEPAPAWFECETSIPSVRPPKWLLGKTVLQAGGNVGLEQDGTVHRLTLHKTCSTMTGPVHFTIGKSRSSAQLVVSDIPVVLTRPLEPKAGRELQSVVLSCDFRPAPKAVQWYKDDTPLSPSEKFKMALEGQMAELRILRLTPADAGVYRCQAGSAQSSAEVTVEAREVTVIQPLQDAEAMEEGRVCFSCELSHKDEDIEWSLNGTPLYNDSFHEISHEGCLHTLVLKSVRQADTGTVCATSPKVSVSARLVVKGKPVVFLKALDDVSAEERGTLTLQCEVSDPEARVVWRKDGVELGPSDKYDFLHKAGARGLTVHDLSHEDAGLYTCQVGSKETQSKVSVHDLHVGITKRLKTVEVLEGESCSFECVLSHESPSDPAVWTVGGKTVGGSGHFHAVRQGRKYTLTVKDAALSDAGEVVFSVLGLTSKASLIIRERPVDITKPLEDQRTTLGEDVMLSCELSRAGTSVRWLKDGKAIRKSQKYDLLSEGTRAVLVVRKASLKDSGEYTCETEASKSTAKLCVEEKANRFTEELADLQVEEKGRAVFTCKTEHPASVVTWRKGLLELRASGKHVPSQEGLTLKLTINALERTDSDTYTCDIGQARTQARLLVHGQKVRVIEDLEDTAVQEGSSAKFCCRIAPADYGPVHWFLDKTPLHSNELNEITVQPGGYHVLTLRQLALKDSGTVYFEAGDQRTSAALRVTEKPSIFSRPLTDVTVTEGEDLTLVCETTTVDSSVRWTKDGKTLRPSARCQLSHEGCQAQLLITATTPQDGGRYKCEIGGASSSSIVRVHALPVRFRESLKDVEVPEGKAATLRCVLSSVAAPVEWRHGDDVLKSSNKYSLRQEGAVLELVIRDLQPQDSGQYSCSFGDQTTSATLTVKTSSAQFVGKLRNKEATEGTTVTLRCELTKEAPVEWKKGTETLRNGDKYSLKQDGAVCELQICSLLVADAGEYSCVCGQEKTSATLTVKALLVHFVRRLRSKEATEGDTTTLQCELSKAAPVEWRKGTETLRDGDRYSLKQDGAVCELQIRSLTIADAGEYLCTCGQEKTSATLTVRALPAKFKDSLKNEEATEGTTATLSCELSKAAPVTWKKGPKTLQSGDKYVLRQDGAVCGLQIHGLTMADAGEYSCVCGQEKTSATLTVRGLPAKFIEDLRSQEATEGATAILRCELSKAAPVEWRKGSETLKDGDRYTLRQDGAVCELQIRGLAVVDTGTYSSLPTKFTEGLRNEEATEGTMATLRCQMSKAAPVEWRKGSETLRDGDRYSLRQDGAMCELQIRGLTIEDSGEYTCVCGQEKTSATLSVKALPSRFIEDLRSQEATEGTMATLRCQMSKTAPVEWKKGSETLRDGGRYSLRQDGPVCELQICDLAVEDAGEYSCVCGQEKTSATLSIKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLGDGGRYSLRQNGAVCELQIHDLAVEDTGEYSCVCGQEKTSATLNVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLRDGGRYSLRQDGAVCELQIHDLDVEDAGQYSCVCGQEKTSAVLTVDALPPKFTEGLKKEEATEGTMVTLRCQMSKEATVEWRKGAKTLSDGGRYSLRQDGAMCELQICGLAVEDAGEYSCVCGQEKTSATLSVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLRDGDRYSLRQDGAVCELQIRDLAVEDAGEYLCVCGQEKTSATLSVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSKTLRDGDRYSLRQDGAMCELQICDLAVEDTGDYSCVCGQEKTSATLSVKALPPRFIEDLRSQEAREGTVATLRCRMSKAAPVEWRKGSETLKDGDRYSLRQEGNLCELQIRDLAVEDTEEYSCVCGQEKTSATLSVKALPAKFIEDLRSQEAPESSTVTLRCKLSKKASVVWKKGSETLRNGARYSLRQDGAVCELEIRDLTVEDTGEYSCTCGQERTSATLSIMAPQVVFQQPLQNLQAEEGSMASLRCELSVPNAAMVWSKGGLELQGDTRREARQQGCVAELLLRDLRREDAGEYSCTCGSQTTSATLMVTAAPVRFLRELQAQDVDEGATARLRCELSREAVSVEWRKGSLQLFPCAKYQMVQEGTTAELLVHGVEQEDAGEYTCDAGHTQSIARLSVRAPKPKFKTDLQSTEQEAGGTARLCCQLSEAEPGTPVQWLKEGVELHVGSKYEMRRQGAVCELLIHGLEAKDTGEYACLVGGQKTLASLRVKEPEVTIVRGLVDMEVQADEDVEFTCKVSQAGATDVQWHLQGLPLQSNEVTEVAVLADGCTHVLQLKGVTLEDAGTVSFHVGGLSSSAQLTVRVPEVTVLEPLKDVQLSEGQDAHFRCRLSRASGQEARWALGGVPLQCNEMNDITVEQGTLYLLTLHKVTLEDAGTITLQVGSCSSEAQLKVTAKNTVLRGLENVDALEGGEALFECQLSQPEVAAHTWLLDDEPVHTSEKVEVVYFENGLRHLLLLKNLKPQDSCRVTFLAGDVVTSAFLTVRGWRLEVLEPPHDASVKAGMQVRFTCILSEAVPVGEATWYINGAAIQPDDTDWTVTTDGSHHALTLSNAQPQHAGEVTFAARDAVASARLSVLALPDPPEDAEVVGRSDHSVTLSWVAPMSDGGGGLCGYRVEMKEASTGQWQLCHDLVPGPECVVDDLVPGKTYRFRVAAVGPAGAGEPVHLPQMVKIAPAPAPAPAPAPAPAPETRQAVVGEDICLELEVAADGGEVVWHKGTERIQPGGHFEVLSRGQRQMLVIKGFRTEDQGEYRCGPIQGLPSSGAATFNVVMTSGSGDEVPAQPSLPPEAAQEGDLHLLWEALARKRRMSREPTLDSISELPEEDSRVQHLRQEAEETAPDLSEGYSTADELARTGEADLSHTSSDDESRAGTPSLVTYLKKAGGPGISPLASKHEAQVTTSVKPQKQQEPVVPTCPPPGDLSAADLMDPSLDKAAVKIQAAFKGYKVRKEMKQQEGPVFSRTFGDTEAQVGDVLRLECVLATKTDMRACWLKDGIELTDGRHYHIDQLKDGTCSLLVTGLAPTDSGRYTCQVSTKSGRVSHSACVVVSGTESEAESSSGGELDDAFRRAARRLHRLFRTKSPAELSEEELFLSADEGPGEPEEPADWQTYREDENFVCIRFESLAEARQAVTCFRNMFATMGIGVEISLGEQGPRGVEMRIGKVAPTVTPAVPLAKTPGLQTSDAAPVFLTELQNQDVQDGYPMSFDCVVTGQPVPSVRWFKDGKLLEEDDHYMINEDQQGGHQLIITAVVPADMGVYRCLAENSMGVSSTKAELRVELTSTDYDTAADATETSSYFSAQGYLSSREQEGTESDEGQLPQVLEELKDLQVAPGTRLAKFQLKVKGYPAPKLYWFKDGQPLTTSDHIRMTDKKTLHTLEIVSVTREDSGQYAAYISNAVGAAYSSARLLVRGPSEPEEKPASDVHERLVPPRILEKFTPKKVKRGSSITFSVKVEGHPAPSVHWLKEEAEKGVLWIGPDTPGYTMASSSKQHSLVLLDVGRQHQGTYTCIATNPAGQALCSASLHISGLAKEEEQERVKEALISSFLQGTSQAVSAQMSESAGFADLVGQSKGESLVAEEAHSHLSLAEVGTEEFLQKLTSQITEMVSAKISQAKLQVPGGDSDEETKTPSASPRHGRSRPSSSVQESSSESEDGDSRGEIFDIYVVTADYLPLGAEQDAIILREGQYVEVLDSAHPLRWLVRTKPTKSSPSRQGWVSPAYLDKRLKLSPEWGPTEAPEFPGEAVSEDEYRTRLSSVIQELLSSEQAFVGELQFLESHHMKHLERSPRVPAAVASQKTVIFRNVQDISHFHSSFLKELQGCGTDDDVAMCFIKNQEAFEKYLEFLVGRVQAESVVVSTPVQEFYKKYAEETLSAKDPTQPPPPPLQHYLEQPVERVQKYQALLKELIRNKARNRQNCALLEQAYAVVSALPQRAENKLHVSLMENYPGTLEALGEPIRQGHFIVWEGAPGARMPWKGHNRHVFLFRNYLVICKPRRDSRTDTFSYVFRNMMKLSSIDLNDQVEGDDRAFEVWHEREDSVRKYLLQARTVIIKNSWVKEICGIQQRLAQPVWRPPEFEEELADCTAELGETVKLACRVTGTPKPIVSWYKDGKPVEVDPHHILIEDPDGSCTLILDNLTGIDSGQYMCFAASAAGNASTLGKILVQVPPRFVNKVRATPFVEGEDAQITCTVEGAPYPQIRWYKDGTLLAPGNRYRMLNEPRSGVLVLVIQAASKEDLGHYECELVNRLGSTRGGGELYMQSPALRARDQHHREQIVAAVEDTSVEGSAHSAQDGADQQAASVLWRLLGSEALGPSPGDLPNTRQSEPPAFEEAASQIPGAASGTPEVSQPGTHKGLEQETTSSGSQGWTVPIRVEGTAWPGAGTGQLLLDVHSQVIMETTQRTYVCQAPDTGVTRAPSMQVTIEDVQVQVGDMAQFDAVIEGHPPPIVTWYKGSTQLTSSARLSQRQDGTTYSLVLTDVAPHDAGVYTCVANNAGGQVLCKAELLVHGGDKLDAENQVYRRKLHSFYDVQEEIGRGVFGFVKRVQHKGNKMFCAAKFIPLRSKTRAQAYQERDILATLGHPLVTGLLDQFETRKTLILILELCSSEELLDRLFKKGVVTEAEVKVYIQQLVEGLHYLHSHGILHLDIKPPNILMVHPAREDIKICDFGFAQKITPSEPQYSKYGSPEFVSPEIIEQNPVSEGSDIWAMGVISYLSLTCSSPFAGESDRATLLNVLEGRVSWSSPTAAHLSEDAKDFIKATLQRTPRARPSTSQCLAHPWFLKSMPAEEAHFINTKQLKFLLARSRWQRSLMSYKSILVMRSIPELLQGPPDSPSLGVARHLRGEASGASSSSSSSDNELAPFARAKSLPPSPVTHSPLLHPRGFLRPSASLPEETEASMPTADAAVPASPQSAGPPASPGCVPRHSVISSLFYQQAGEGAERGNKTSGAKRHPARRRHLLKGGYIARALPGLREPLMEYSLLEEEAAREEQASLMTKTPSFETALRLPSSSVREVPGRSHSLDNPPVTTGPSPEACKEQLLFPPSTGLTHETTAKDRGHKEGFLQESVPFPPMSGDSRPGKQEGSSQDSCRGKPASSCHSELGSGSQEGCGPPSSQSLGSLPPQSLKKELSTSCGPLFSEQPQAAPFPTQVSPLLGSEKEPQDGSLSEGPVPVPSSSPGSASQVDASLDTEGLSEAGDTCDFTPPPQRPQEQATTRKFSLESRGGYAGVAGYGTFAFGGDAGGMLGQGPLWARMAWAVSQSSEEQDEAATESPQPLESLGPIAEASGVPLRTSPSLTPWEEVEQVSLVQIRDLSGDAEAADTISLDISEVDPAYLNLSDLYDIKYLPFEFMIFRRVPKPIEQPESPGSETEAGQGLADFLEEAAWPWPGELGLRAGLEITEEPEEPGDLEALLGEAAVGRKRKWSPSRGLFQFPGRCLSGEEPVELGLRQRVKASMAHISRILKGRPEGPEREGPPRKKAGLASFRLSGLKGRDQELSDEAVVLGQSVTLACQVLAQPTAQATWSKDGVLLESSGHLLISSTLKNFQLLTILVVKEEDLGTYTCCVSNPLGTAVTTGVLRKAERPSSSPRPEVGELYKDAVLLVWKPVESCGPVTYIVQCCIEGGSWTTLASDISDCCYLTGKLSRGGMYIFRTACVSKAGMGPYSSPSEQVLLGGPNHLASEEESSRGRPAQLLPSTKTFAFQMQIRRGRFSVVRQCREKASGRALAAKIVPYQPEDKTAVLREYEALKRLHHPHLAQLHAAYLSPRHLVLILELCSGPELLPSLAERESYSESDVKDYLWQMLSATQYLHAQHILHLDLRSENMMVTEYNLLKVIDLGNAQSLDQEKVPAPENFKDYLETMAPELLEGQGAVPQTDIWAIGVTAFIMLSGEYPESSEGTRDLQKGLRKGLIRLSRCYAGLSGGAVAFLQSSLCAQPWGRPCASTCLQCGWLTEEGPTGSRPTPVTFPTVRLRAFVREREKRRALLYKKHNLAQVR | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23392350}; | cell differentiation [GO:0030154]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468] | cytosol [GO:0005829]; extracellular space [GO:0005615]; intercalated disc [GO:0014704]; M band [GO:0031430]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863]; Z disc [GO:0030018] | ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; phosphatidylinositol bisphosphate binding [GO:1902936]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00041;PF07679;PF00047;PF00612;PF00169;PF00069;PF00621; | 1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Autophosphorylated by protein kinase domain 1 and 2. {ECO:0000269|PubMed:23392350}.; PTM: Two small isoforms, one probably containing protein kinase domain 2 and a partial protein kinase domain 1 and one containing only protein kinase domain 2, are glycosylated. {ECO:0000269|PubMed:23392350}. | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23392350}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:23392350}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Nucleus {ECO:0000269|PubMed:23392350}. Secreted {ECO:0000269|PubMed:23392350}. Note=Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. One or both small isoforms, one probably containing protein kinase domain 2 and partial protein kinase domain 1 and one containing only protein kinase domain 2, localize to the extracellular side of the sarcolemma. {ECO:0000269|PubMed:23392350}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:28826662}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:28826662}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23392350}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23392350}; | null | null | null | null | FUNCTION: Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (PubMed:23392350). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (By similarity). {ECO:0000250|UniProtKB:Q5VST9, ECO:0000269|PubMed:23392350}.; FUNCTION: Isoform 2 and isoform 3: bind phosphatidylinositol bisphosphates (PIP2s) via their PH domains and negatively regulate the PI3K/AKT/mTOR signaling pathway, thus contributing to the regulation of cardiomyocyte size and adhesion. {ECO:0000269|PubMed:28826662}. | Mus musculus (Mouse) |
A2AAY5 | SPD2B_MOUSE | MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGATEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGNDPTSVDPMVLEQYVVVADYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVVQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKLGPSSPAHSGALDLDGVSRHQNAMGREKELLNNQRDGRFEGRLVPDGDVKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKSLSGWWYIQMEDKEGWAPATFIDKYKKTSSASRPNFLAPLPHEMTQLRLGDAAATENNTGPEAVGPSRPLPEAPHGAVDSGMLWSKDWKGGKEAPRKASSDLSASTGYEEISDPTQEEKPSLPPRKESIIKSEEELLERERQKMEPLRGSSPKPPGMILPMIPAKHAPLARDSRKPEPKLDKSKFPLRNDMGLECGHKVLAKEVKKPNLRPISRSKAELSEEKVDPTSQNLFMKSRPQVRPKPTPSPKTEPAQSEDHVDIYNLRSKLRPAKSQEKALLDGESHHAAGSHDTALSRSFLPGEGPGHGQDRSGRQDGLSPKETPCRAPPRPAKTTDPGPKNVPVPVQEATLQQRPVVPPRRPPPPKKTSSSPLSCRPLPEVRGAQREESRVAPAAGRALLVPPKAKPFLSNSSVGQDDMRGKGGLGPRVTGKVGETREKAASFLNADGPKDSLYVAVANFEGDEDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP | null | null | adipose tissue development [GO:0060612]; bone development [GO:0060348]; cranial skeletal system development [GO:1904888]; eye development [GO:0001654]; heart development [GO:0007507]; osteoblast fate commitment [GO:0002051]; podosome assembly [GO:0071800]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of gene expression [GO:0010628]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of stress fiber assembly [GO:0051496]; protein localization to membrane [GO:0072657]; regulation of brood size [GO:0060378]; skeletal system development [GO:0001501]; skeletal system morphogenesis [GO:0048705]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801] | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; podosome [GO:0002102] | phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; SH2 domain binding [GO:0042169]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00787;PF00018;PF07653; | 3.30.1520.10;2.30.30.40; | SH3PXD2 family | PTM: Phosphorylated in SRC-transformed cells. {ECO:0000269|PubMed:19144821}. | SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. | null | null | null | null | null | FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation. {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821, ECO:0000269|PubMed:19755710}. | Mus musculus (Mouse) |
A2ABV5 | MED14_MOUSE | MAPVQLDNHQLIPPGGGGGSSGGGGSSSGSASAPAPPPPAAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPEVPWRLLKLEILVEDKETGDGRALVHSMQIDFIHQLVQSRLFADEKPLQDMYNCLHCFCLSLQLEVLHSQTLMLIRERWGDLVQVERYHAGKSLSLSVWNQQVLGRKTGTASVHKVTIKIDENDVSKPLQIFHDPPLPASDSKLVERAMKIDHLSIEKLLIDSVHARAHQRLQELKAILRSFNANESSSIETALPALIVPILEPCGNSECLHIFVDLHSGMFQLMLYGLDPATLEDMEKSLNDDMKRIIPWIQQLKFWLGQQRCKQSIKHLPTITTETLQLANYSTHPIGSLSKNKLFIKLTRLPQYYIVVEMLEVPNKPTQLSYNYYFMSVSTADREDSPVMALLLQQFKDNIQDLMSYTKTGKQTRTGTKHKLSDDPCPIDSKKAKRSGEMCAFNKVLAHFVAMCDTNMPFVGLRLELSNLEIPHQGVQVEGDGFNHAIRLLKIPPCKGISEETQKALDRSLLDCTFRLQGRNNRTWVAELVFANCPLNGTSTREQGPSRHVYLTYENLLSEPVGGRKVVEMFLNDWSSIARLYECVLEFARSLPEIPAHLNIFSEVRVYNYRKLILCYGTTKGSSISIQWNSIHQKFHIALGTVGPNSGCSNCHNTILHQLQEMFNKTPNVVQLLQVLFDTQAPLNAINKLPTVPMLGLTQRTNTAYQCFSILPQSSTHIRLAFRNMYCIDIYCRSRGVVAIRDGAYSLFDNSKLVEGFYPAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPQQQPFPKQPGTSGAYPLTSPPTSYHSTVNQSPSMMHTQSPGNLHAASSPSGALRAPSPASFVPTPPPSSHGISIGPGASFASPHGTLDPSSPYTMVSPSGRAGNWPGSPQVSGPSPATRLPGMSPANPSLHSPVPDVSHSPRAGTSSQTMPTNMPPPRKLPQRSWAASIPTILTHSALNILLLPSPTPGLVPGLAGSYLCSPLERFLGSVIMRRHLQRIIQQETLQLINSNEPGVIMFKTDALKCRVALSPKTNQTLQLKVTPENAGQWKPDELQVLEKFFETRVAGPPFKANTLIAFTKLLGAPTHILRDCVHIMKLELFPDQATQLKWNVQFCLTIPPSAPPIAPPGTPAVVLKSKMLFFLQLTQKTSVPPQEPVSIIVPIIYDMASGTTQQADIPRQQNSSVAAPMMVSNILKRFAEMNPPRQGECTIFAAVRDLMANLTLPPGGRP | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; somatic stem cell population maintenance [GO:0035019] | core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712] | PF08638; | null | Mediator complex subunit 14 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2AC93 | DNAI2_MOUSE | MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTQAEKIVCTFYGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSSSLSTLQRNEKNIASSIFERETRREKILEARHREMRLKEKGKVEGKEDDQKEEEAALDLDELVGKAEEEFFEVIFSELKRKEAEALKKKPKPRKKSSVKVEAEEEVEENVGEEEEAGGIIGIDAVEDMSEEAGEEQEDVPT | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; outer dynein arm assembly [GO:0036158] | 9+2 motile cilium [GO:0097729]; axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dynein axonemal particle [GO:0120293]; external side of plasma membrane [GO:0009897]; microtubule [GO:0005874]; outer dynein arm [GO:0036157]; sperm flagellum [GO:0036126] | dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503]; microtubule motor activity [GO:0003777] | PF00400; | 2.130.10.10; | Dynein intermediate chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9GZS0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q4QR00}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q9GZS0}. | null | null | null | null | null | FUNCTION: Part of the dynein complex of respiratory cilia. {ECO:0000250}. | Mus musculus (Mouse) |
A2AD83 | FRMD7_MOUSE | MLHLKVQFLDDSQKIFVVDQKSSGKALFNLSCGHLNLAEKEYFGLEFCSHSGNNVWLELLKPITKQVKNPKEVVFKFMVKFFPVDPGHLREELTRYLFTLQIKKDLALGRLPCSDNCTALMVSHILQSELGDFHEETVRKHLVQTQYLPSQASLESKIMQFHQQHIGRSPAESDILLLDIARKLDMYGIRPQPASDGEGMQIHLAVAHMGVLVLRGNTKINTFNWAKIRKLSFKRKHFLIKLHANILVLCKDTLEFTMASRDACKAFWKTCVEYHAFFRLSEEPKSKPKTLLCSKGSSFRYSGRTQRQLLEYGKKGRLKSLPFERKQYPSQYHERQCRSSPDILSDVSKQVEDLRLTYGSSYYRNVNGVHASESMLDSRRRNSAVEVTFAAELEHSKPEAEATSLHPSQSSSSFTFIYADPVFNTDPEPIEFFEERSPLSSFQTTSKFADSHTSKASPARQLTYTDVPYIPCTSQKVDIMPPQVFFYVDKPPQVPRRSLIMAEENMRPDSYVDHSAIKPAKRSPRNMRIKSLQQDLQELQEAMARTSGRSNINVEPEEEDPHLDDAFAYNLQEQTPKRSQSQSDMKTIRFPFGSEFRPLGPCPALTRKTDLFACTFAEQEFPTVLIDQSSAERYVASESSDSESEIIKPDYYFLYGKGTKSPRARIRLSSGSLQLEEEDETISFATPGAEDRTLLKPCNYFLA | null | null | negative regulation of stress fiber assembly [GO:0051497]; nervous system development [GO:0007399]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; regulation of neuron projection development [GO:0010975] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; growth cone [GO:0030426]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF08736;PF09380;PF00373;PF09379; | 1.20.80.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cell projection, neuron projection {ECO:0000269|PubMed:19892780}. Cell projection, growth cone {ECO:0000269|PubMed:19892780}. Note=In undifferentiated neurons, located in the actin-rich regions of the cell body. In differentiated neurons, located in the actin-rich regions of the cell body and primary neurite processes but is almost absent from secondary extensions arising from the primary neurite. Also found at the actin-rich distal end of growth cones. {ECO:0000269|PubMed:19892780}. | null | null | null | null | null | FUNCTION: Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability. {ECO:0000250|UniProtKB:Q6ZUT3, ECO:0000269|PubMed:19892780}. | Mus musculus (Mouse) |
A2AF47 | DOC11_MOUSE | MAEVRKFTKRLSKPGTAAELRQSVSEAVRGSVVLEKAKLVEPLDYENVITQRKTQIYSDPLRDLLMFPMEDISISVIGRQRRTVQSTVPEDAEKRAQSLFVKECIKTYSTDWHVVNYKYEDFSGDFRMLPCKSLRPEKIPNHVFEIDEDCEKDEDSSSLCSQKGGVIKQGWLHKANVNSTITVTMKVFKRRYFYLTQLPDGSYILNSYKDEKNSKESKGCIYLDACIDVVQCPKMRRHAFELKMLDKYSHYLAAETEQEMEEWLIMLKKIIQINTDSLVQEKKDTVEAIQEEETSSQGKAENIMASLERSMHPELMKYGRETEQLNKLSRGDGRQNLFSFDSEVQRLDFSGIEPDVKPFEEKCNKRFMVNCHDLTFNILGHIGDNAKGPPTNVEPFFINLALFDVKNNCKISADFHVDLNPPSVREMLWGTSTQLSNDGNAKGFSPESLIHGIAESQLCYIKQGIFSVTNPHPEIFLVVRIEKVLQGNITHCAEPYIKNSDPIKTAQKVHRTAKQVCSRLGQYRMPFAWAARPIFKDVQGSLDLDGRFSPLYKQDSSKLSNEDILKLLSEYKKPEKTKLQIIPGQLSITVECVPVDLPNCITSSYVPLKPFEKNCQNITVEVEEFVPEMTKYCYPFTIYKNHLYVYPLQLKYDSQKSFAKARNIAVCVEFRDSDESDASALKCIYGKPAGSVFTTNAYAVVSHHNQNPEFYDEIKIELPIHLHQKHHLLFTFYHVSCEINTKGTTKKQDTVETPVGFAWVPLLKDGRVITLEQQLPVSANLPPGYLNVNDAESRRQSNADIKWVDGAKPLLKIKTHLESTIYTQDLHVHKFFHHCQLIQSGSKEVPGELIKYLKCLHAMEIQVMIQFLPVILMQLFRVLTNMTHEDDVPINCTMVLLHIVSKCHEEGLESYLRSFIKYSFRPEKPSTLQAQLIHETLATTMIAILKQSADFLAINKLLKYSWFFFEIIAKSMATYLLEENKIKLPRGQRFPEAYHHVLHSLLLAIIPHVTIRYAEIPDESRNGNYSLASFLKRCLTLMDRGFVFNLINDYISGFSPKDPKVLAEYKFEFLQTICNHEHYIPLNLPMAFAKPKLQRVQDSNLEYSLSDEYCKHHFLVGLLLRETSIALQDNYEIRYTAISVIKNLLIKHAFDTRYQHKNQQAKIAQLYLPFVGLLLENIQRLAGRDTLYSCAAMPSSASRDEFPCGFVSPTNRGSLASDKDTAYGSFQNGHGIKREDSRGSLIPEGATGFPDPGSTSENTRQSSSRSSVSQYNRLDQYEIRNLLMCYLYIVKMISEDTLLTYWNKVSPQELINILVLLEVCLFHFRYMGKRNIARVHDAWLSKHFGIDRKSQTMPALRNRSGVMQARLQHLSSLESSFTLNHSSATTEADIFHQALLEGNTATEVSLTVLDTISFFTQCFKNQLLNNDGHNPLMKKVFDIHLAFLKNGQSEVSLKHVFASLRSFISKFPSAFFKGRVNMCAAFCYEVLKCCTSKISSTRNEASALLYLLMRNNFEYTKRKTFLRTHLQIIIAVSQLIADVALSGGSRFQESLFIINNFANSDRPMKATAFPTEVKDLTKRIRTVLMATAQMKEHEKDPEMLIDLQYSLAKSYASTPELRKTWLDSMAKIHIKNGDFSEAAMCYVHVAALVAEFLHRKKLFPSGCSAFKKITPNIDEEGAMKEDAGMMDVHYSEEVLLELLEQCVDGLWKAERYEVISEISKLIIPIYEKRREFEKLTQVYRTLHGAYTKILEVMHTKKRLLGTFFRVAFYGQSFFEEEDGKEYIYKEPKLTGLSEISLRLVKLYGEKFGTENVKIIQDSDKVNAKELDPKFAHIQVTYVKPYFDDKELTERKTEFERNHNINRFVFEAPYTLSGKKQGCIEEQCKRRTILTTSNSFPYVKKRIPINCEQQVNLKPIDVATDEIKDKTAELHKLCSSVDVDMIQLQLKLQGCVSVQVNAGPLAYARAFLNESQANKYPPKKVNELKDMFRKFIQACSIALELNERLIKEDQIEYHEGLKSNFRDMVKELSDIIHEQILQEDTMHSPWMNNTLHVFCAISGTSSNRGYGSPRYAEV | null | null | B cell homeostasis [GO:0001782]; marginal zone B cell differentiation [GO:0002315]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; small GTPase-mediated signal transduction [GO:0007264] | null | guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF06920;PF20422;PF20421;PF14429;PF11878;PF00169; | 1.20.58.740;1.25.40.410;2.60.40.150;2.30.29.30; | DOCK family | null | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP (PubMed:15710388, PubMed:16968698, PubMed:25851601). Required for marginal zone (MZ) B-cell development, is associated with early bone marrow B-cell development, MZ B-cell formation, MZ B-cell number and marginal metallophilic macrophages morphology (PubMed:25729399). Facilitates filopodia formation through the activation of CDC42 (PubMed:22494997). {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}. | Mus musculus (Mouse) |
A2AG06 | MEIOC_MOUSE | MEVSGGDTCRPRHPQGLREGPEPKVAAAAAAFRGSANRCWNLSVDTSNRLSDVFNSMMLTGSAPFYDCYKSQNEDNVDLRQTCTPLSSSTEYASSIDSSLFYAPWSTYGDDIKQPPSSQISVKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFVDHHDLLTEPKRPVDTSISQQAFYSGESVSAVEKQYLHNSSLTPQQKIDELYHGYTGLDLEEQWLYLSRSDHSNCYNSQANDTVKATFQEYPFVKNCFTPQTGLSDIMKESGIDTYAYGREKICTKGLETPLQHKRAEIFLSQFNRYNENADYCRYPEYAHPNKAKLNKCSNFSVQDGKKLANGTPETPTVEADAYTKLFQVKPANQKKMEETIPDQQNFAFPKTTPHLTEKQFAKEAAFTADFGLKSEYGLKPHTACPTNNDFANVSEKQQFAKPDPLNSEYFKSVNLFSNSATSSGGISLNRPTWMNVQTKNNLPIPYRNQGNLMKLNSHLSAASKGSNHSSDFPQLSSTNLTSNSNLFQKYCQENPSAFSSFDFSYNGAERIQSVNHMEGLTKTGEDNLFESVTEKKIKQPNGFCDSYSASQYGIIENVNKHNFQAKPQSGHYDPEDIPKHFDGLPQNTYQDLLESQGHFNSHRQGSGDNNINSRVNRTQASCFSNNYMMGDLRHNQGFQQLGSNGFPLRSTHPFGHSVVPLLDSYDLFSYDDLSHLYPYFNDMMYGDNSFSGFVPTFGFQRPIKTRSGPASELHIRLEECYEQWRALEKERKKTELALAKNYPGKKVSSTNNTPIPRLTSNPSRVDRLIVDELREQARVVTLLGKMERLRSSPLHANISTALDRHLESIHIVQSRRKDEIVNASNRQRQGVPRCQDDRDVFALATAIKEMCVATRKARTTLWCALQMTLPKTASTAGQADMEKAFQDLVNCEEKVHESINSSNPMNQRGETSKH | null | null | chromosome organization involved in meiotic cell cycle [GO:0070192]; double-strand break repair [GO:0006302]; female meiosis I [GO:0007144]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; male meiosis I [GO:0007141]; metaphase chromosome alignment [GO:0051310]; mRNA stabilization [GO:0048255]; oocyte development [GO:0048599]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF15189; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. Nucleus {ECO:0000269|PubMed:28380054}. Note=at late pachytene a fraction is nuclear. {ECO:0000269|PubMed:28380054}. | null | null | null | null | null | FUNCTION: Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic prophase I by properly promoting the transition from a mitotic to a meiotic cell cycle program by binding transcripts through its interaction with YTHDC2 that regulate the mitotic cell cycle (PubMed:28380054). {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. | Mus musculus (Mouse) |
A2AGH6 | MED12_MOUSE | MAAFGILSYEHRPLKRLRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVNFNPAKISSNFSSIIAEKLRCNTLSDTGRRKSLMNQKDNFWLVTARSQSAINTWFTDLAGTKPLTHLAKKVPIFSKKEEVFGYLAKYTVPVMRAAWLIKMTCAYYAAMSETKVKKKNTADPFTEWTQIITKYLWEQLQKMAEYYRPGPAGSGGCGSTIGPLPHDVEMAIRQWDYNEKLALFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLKLLLPLLLRYSGEFVQSAYLSRRLAYFCTRRLALQLDGVSSHSSHVIAAQSTSSLPTTPAPQPPTSSTPSTPFSDLLMCPQHRPLVFGLSCILQTILLCCPSALVWHYSLTDSRIKTGSPLDHLPIAPSNLPMPEGNSAFTQQVRAKLREIEQQIKERGQAVEVRWSFDKCQEATAGFTIGRVLHTLEVLDSHSFERSDFSNSLDSLCNRIFGLGPSKDGHEISSDDDAVVSLLCEWAVSCKRSGRHRAMVVAKLLEKRQAEIEAERCGESEAADEKGSVASGSLSAPSAPIFQDVLLQFLDTQAPMLTDPRSESERVEFFNLVLLFCELIRHDVFSHNMYTCTLISRGDLAFGAPGPRPPSPFDDPTDDPERKEAEGSSSSKLEDPGLSESMDIDPSSSVLFEDMEKPDFSLFSPTMPCEGKGSPSPEKPDVEKEVKPPAKEKIEGTLGILYDQPRHVQYATHFPIPQEESCSHECNQRLVVLFGVGKQRDDARHAIKKITKDILKVLNRKGTAETDQLAPIVPLNPGDLTFLGGEDGQKRRRNRPEAFPTAEDIFAKFQHLSHYDQHQVTAQVSRNVLEQITSFALGMSYHLPLVQHVQFIFDLMEYSLSISGLIDFAIQLLNELSVVEAELLLKSSDLVGSYTTSLCLCIVAVLRHYHACLILNQDQMAQVFEGLCGVVKHGMNRSDGSSAERCILAYLYDLYTSCSHLKSKFGELFSDFCSKVKNTIYCNVEPSESNMRWAPEFMIDTLENPAAHTFTYTGLGKSLSENPANRYSFVCNALMHVCVGHHDPDRVNDIAILCAELTGYCKSLSAEWLGVLKALCCSSNNGTCGFNDLLCNVDVSDLSFHDSLATFVAILIARQCLLLEDLIRCAAIPSLLNAACSEQDSEPGARLTCRILLHLFKTPQLNPCQSDGNKPTVGIRSSCDRHLLAASQNRIVDGAVFAVLKAVFVLGDAELKGSGFTVPGGTEELPEEEGGGGSSGRRQGGRNISVETASLDVYAKYVLRSICQQEWVGERCLKSLCEDSNDLQDPVLSSAQAQRLMQLICYPHRLLDNEDGENPQRQRIKRILKNLDQWTMRQSSLELQLMIKQTPNTEMNSLLENIAKATIEVFQQSAETGSSSGSTASNMPSSSKTKPVLSSLERSGVWLVAPLIAKLPTSVQGHVLKAAGEELEKGQHLGSSSRKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLASLHSQVHQIVINWRENQYLDDCKPKQLMHEALKLRLNLVGGMFDTVQRSTQQTTEWAQLLLEIIISGTVDMQSNNELFTTVLDMLSVLINGTLAADMSSISQGSMEENKRAYMNLVKKLQKDLGERQSDSLEKVHQLLPLPKQNRDVITCEPQGSLIDTKGNKIAGFDSIFKKEGLQVSTKQKISPWELFEGLKPSTAPLSWAWFGTVRVDRRVARGEEQQRLLLYHTHLRPRPRAYYLEPLPLPPEDEEPPAPALLEPEKKAPEPPKTDKPGAAPPSTEERKKKSTKGKKRSQPATKNEDYGMGPGRSGPYGVTVPPDLLHHANPGSISHLSYRQSSMGLYTQNQPLPAGGPRVDPYRPVRLPMQKLPTRPTYPGVLPTTMSTVMGLEPSSYKTSVYRQQQPTVPQGQRLRQQLQAKIQSQGMLGQSSVHQMTPSSSYGLQTSQGYTSYVSHVGLQQHTGPAGTMVPPSYSSQPYQSTHPSTNPTLVDPTRHLQQRPSGYVHQQAPTYGHGLTSTQRFSHQTLQQTPMMGTMTPLSAQGVQAGVRSTSILPEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQYHIRQQQQQQQMLRQQQQQQQQQQQQQQQQQQQQQQQQQQQPHQQQQQAAPPQPQPQSQPQFQRQGLQQTQQQQQTAALVRQLQQQLSNTQPQPSTNIFGRY | null | null | axis elongation involved in somitogenesis [GO:0090245]; embryonic brain development [GO:1990403]; embryonic neurocranium morphogenesis [GO:0048702]; embryonic organ development [GO:0048568]; endoderm development [GO:0007492]; heart development [GO:0007507]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; oligodendrocyte development [GO:0014003]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; post-anal tail morphogenesis [GO:0036342]; protein ubiquitination [GO:0016567]; Schwann cell development [GO:0014044]; somatic stem cell population maintenance [GO:0035019]; somitogenesis [GO:0001756]; spinal cord development [GO:0021510]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071] | CKM complex [GO:1990508]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; ubiquitin ligase complex [GO:0000151] | beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; nuclear thyroid hormone receptor binding [GO:0046966]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630] | PF09497;PF12145;PF12144; | null | Mediator complex subunit 12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2AGL3 | RYR3_MOUSE | MAEAGEGGEDEIQFLRTEDEVVLQCIANIHKEQRKFCLAAEGLGNRLCFLEPTSEAKYIPPDLCVCNFVLEQSLSVRALQEMLANTVENGGEGAAQGGGHRTLLYGHAILLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEKVRIGDDLILVSVSSERYLHLSISNGSIQVDASFMQTLWNVHPTCSGSSIEEGYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRVFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALTEDQGLLLQDRGKSDTKSTAFSFRASKEIKEKLDSSHKRDMEGMGVPEIKYGDSVCFVQHVASGLWVTYKAQDAKTSRLGPLKRKVILHQEGHMDDGLTLQRCQQEESQAARIIRNTTALFSQFVSGNNRTTAPVALPTEEVLQTLQDLIAYFQPPEDEMQHEDKQNKLRSLKNRQNLFKEEGMLALVLNCIDRLNIYNSVAHFAGIVREESGMAWKEILNLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILIESPEALNLIAEGHIKSIISLLDKHGRNHKVLDVLCSLCLCNGVAVRANQNLICDNLLPRRNLLLQTRLINDVTSIRPNIFLGVAEGSPQYKKWYFELIIDQVEPFLTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLWSGRIPRAVASINQHLLKSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMGGRHGEFKFLPPSGYAPCYEALLPKEKMRLEPVKEYKRDADGVRDLLGTTQFLSQASFIPCPIDTSQVVLPLHLEKIRDRLAENIHELWGMNKIELGWTYGKVRDDNKRQHPCLVEFSKLPETEKNYNLQMSTETLKTLLALGCHIAHVNPAAEEDLKKVKLPKNYMMSNGYKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVRTFVGYGYNIEPSDQELADPTVEKVSIDKIRFFRVERSYAVKSGKWYFEFEVVTGGDMRVGWARPGCRPDIELGADDQAFVFEGSRGQRWHQGSGYFGRTWQPGDVVGCMINLDDASMVFTLNGELLITNKGSELAFADYEIENGFVPICSLGLSQIGRMNLGTDASTFKFYTMCGLQEGFEPFAVNMNRDVAVWFSKRLPTFVNVPKDHPHIEVVRIDGTMDSPPCLKVTHKTFGTQNSNANMIYCRLSMPVECHSSFSHSPCLDSEAFQKRKQMQEILSHTTTQCYYAIRIFAGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQRSSRSNVDLEIGCLLDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELGKLKNAMPLSAAIFKSEEKNPTPQCPPRLDVQTIQPVLWSRMPSSFLKVETERVSERHGWVVQCLEPLQMMALHIPEENRCVDILELCEQEDLMQFHYHTLRLYSAVCALGNSRVASALCSHVDLSQLFYAIDNKYLPGLLRSGFYDLLISIHLANAKERKLMMKNEYIIPITSATRNIRLYPDESKRHGLPGVGLRTCLKPGFRFSTPCFVVTSEDHQKQSPEIPLQILKTKALSMLTEAVHCSGAHIRDPVGGSVEFQFVPVLKLIGTLLVMGVFDDDDVRQILLLIDPSVFGEHSGETEEGVEKEVTHAEEKAVEAGEKACKEAPVKGLLQTRLPESVKLQMCELLSYLCDCELQHRVEAIVAFGDIYVSKLQANQKFRYNELMQALNMSAALTARKTREFRSPPQEQINMLLNFHLGENCPCPEEIREELYDFHEDLLVHCGVPLEEEEEEEEDTSWTGKLCALVYKIKGPPKPEKEQPTEEEKPYPTTLKELVSQTMIRWAQENQIQDAELVRMMFNLLRRQYDSIGELLQALRKTYTISQASVNDTINLLAALGQIRSLLSVRMGREEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMVNVLGTEKSQIAFPKMVASCCRFLCYFCRISRQNQKAMFEHLSYLLENSSVGLASPSMRGSTPLDVAASSVMDNNELALGLEEPDLEKVVTYLAGCGLQSCPMLLARGYPDVGWNPIEGERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALRGEGGNGLLAAMQGAIKISENPALDLPSQGYKTEVTQDDGEEEEIVHMGNAIMSFYSALIDLLGRCAPEMHLIQTGKGEAIRIRSILRSLVPTEDLVGIISIPLKLPSLNKDGSVSEPDMAANFCPDHKAPMVLFLDRVYGIKDQTFLLHLLEVGFLPDLRASASLDTVSLSTTEAALALNRYLCSAVLPLLTRCAPLFSGTEHCTSLIDSTLQTIYRLSKGRSLTKAQRDTIEECLLAICNHLRPSMLQQLLRRLVFDVPQLSEYCKMPLKLLTNHYEQCWKYYCLPSGWGSYGLAVEEELHLTEKLFWGIFDSLSHKKYDLDLFRMALPCLSAIAGALPPDYLDTRITATLEKQVSVDADGNFDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSHSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLKTMLAVGWTVERTKEGEALVQQRENEKLRCVSQTNQGNSYSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGGSHPLLVPYDTLTAKEKFRDREKAQDLFKFLQVNGILVSRGMKDLELDASSMEKRFAYKFLKKILKYVDAAQEFIAHLEAIVSSGKTEKSPHDQEIKFFAKVLLPLVDQYFTNHRLYFLSSPLKPLSSSGYASHKEKEMVASLFCKLAALVRHRISLFGSDSTTMVSCLHILAQTLDTRTVMKSGSELVKAGLRAFFENAAEDLEKTSENLKLGKFTHSRTQIKGVSQNINYTTVALLPILTSIFEHIAQHQFGVDLLLSDVQVSCYHILCSLYSLGTGKNIYVERQRPALGECLASLAAAIPVAFLEPSLNRHNPLSVFNTKTPRERSILGMPDKVEDMCPDIPQLEGLMKEINDLAESGARYTEMPHVIEVILPMLCNYLSYWWERGPENLPPSTGPCCTKVTSEHLSLILGNILKIINNNLGIDEASWMKRIAVYAQPIISKARPDLLRSHFIPTLEKLKKKAVKTVQEEEQLKTDGKGDTQEAELLILDEFAVLCRDLYAFYPMLIRYVDNNRSNWLKSPDPDSDQLFRMVAEVFILWCKSHNFKREEQNFVIQNEINNLAFLTGDSKSKMSKSGGQDQERKKTKRRGDLYSIQTSLIVAALKKMLPIGLNMCTPGDQELISLAKSRYSCRDTDEEVKEHLRNNLHLQEKSDDPAVKWQLNLYKDVLRNDEPSNPEKTVERVQSISAALFHLEQVEQPLRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRSINLFLHGYQRFWIETEAHFFEEKLVQDLAKSPRVEDEEEEETERQPDPLHQIILHFSRNALTERSKLEDDPLYTSYSSMMAKSCQSGEDEEEEEDKEKTFEEKEMEKQKTLYQQARLHERGAAEMVLQMISASKGEMSPMVVETLKLGIAILNGGNAGVQQKMLDYLKEKKDAGFFQSLSGLMQSCSVLDLNAFERQNKAEGLGMVTEEGTLIVRERGEKVLQNDEFTQDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNIIISTVDYLLRLQESISDFYWYYSGKDIIDESGQHNFSKALAVTKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFLHVFANMQMKLSQDSSQIELLKELLDLLQDMVVMLLSLLEGNVVNGTIGKQMVDTLVESSTNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGIISRKEFQKAMEGLKQYTQSEIDFLLSCTEADENDMFNYVDFVERFHEPAKDIGFNVAVLLTNLSEHMPNDSRLKSLLDPAESVLNYFEPYLGRIEIMGGAKKIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEQEKMELFVNFCEDTIFEMQLASQISESDSTDRPEEEEEEDEDSAYSIETEGEEEEKSFESASAFTMACVSVKRNVTKFLKRATLKNLRKQYRNVKKMSAKELVKVFFSFFWMLFVGLFQLLFTIFGGIFQILWNTVFGGGLVEGAKNIRVTKILGDMPDPTQFGIHDDVIETDRAEVTEPGVTTELVHFVKGEAGDTDIMSDLFGIHSKKEGGLKQGPEVGLGDLSEIIGKDEPPTLESTVRKKRKAQAAEMKAVHEAEGKAESEKADMEDREKEDKIKEEGQTDYLWADVTVKKTRRRGQKAEKPEAFMANFFKGLEIYQTKLLHYLARNFYNLRFLALFVAFAINFILLFYKVTEEPLEEETEDVANLWNSFNDDDEEEAMVFFVLQESTGYMAPTLRALAIVHTIISLVCVVGYYCLKVPLVVFKREKEIARKLEFDGLYITEQPSEDDIKGQWDRLVINTPSFPNNYWDKFVKRKVINKYGDLYGAERIAELLGLDKNALDFSPVEEAKAEAASLVSWLSSIDMKYHIWKLGVVFTDNSFLYLAWYTTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDDDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVREDMETKCFICGIGNDYFDTTPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLG | null | null | calcium ion transmembrane transport [GO:0070588]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; cellular response to magnesium ion [GO:0071286]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; protein homotetramerization [GO:0051289]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; striated muscle contraction [GO:0006941] | calcium channel complex [GO:0034704]; cytoplasmic side of plasma membrane [GO:0009898]; junctional membrane complex [GO:0030314]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; ryanodine-sensitive calcium-release channel activity [GO:0005219] | PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.10.238.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR3 subfamily | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:9582272}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8702664, ECO:0000269|PubMed:9582272}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Plays a role in cellular calcium signaling. Contributes to cellular calcium ion homeostasis. Isoform 2 lacks a predicted transmembrane segment and does not form functional calcium channels by itself; however, it can form tetramers with isoforms that contain the full complement of transmembrane segments and modulate their activity. {ECO:0000269|PubMed:11500519, ECO:0000269|PubMed:11717163, ECO:0000269|PubMed:17596299, ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:8702664, ECO:0000269|PubMed:9582272}. | Mus musculus (Mouse) |
A2AGT5 | CKAP5_MOUSE | MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKYLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYVEIEKGESVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIISLKPIIKVLPKLFESRDKAVRDEAKLFAIEIYRWNRDAVKHTLQNINSVQLKELEEEWVKLPTGAPKPSRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQVDAYELLDAVEILSKLPKDFYDKIEAKKWQERKEALEAVEVLVKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTSSTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKSVNPFLADVDKLKLDRIKECSEKVELVHGKKSGLATEKKESKPLPGRAAASGAAGDKDTKDVSGPKPGPLKKTPTAKAGGPSKKGKTTAPGGSASAGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMERTEMPCQALVKMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQIVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVMSMAFSQKNPKNQSETLNWLSNAIKEFGFSELNVKAFISNVKTALAATNPAVRTSAITLLGVMYLYVGPSLRMIFEDEKPALLSQIDAEFQKMQGQSPPAPTRGIAKHSTSATDEGEDGEEPGEGGNDVVDLLPRIEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINEAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGANIRQHVKNLGIPVITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLKDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKANMPSKPAAPAKAMSKPMGGSAPAKTQPIPAPVEDSVSSTIEAKPDLKKAKAPGVSSKAKSVQGKKVPSKTTLKEDDDKSGPIFIVVPNGKEQRMRDEKGLKVLKWNFTTPRDEYIEQLKTQMSTCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKDGVISCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLILKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLIESYGMNVCQPTPGKALKEIAIHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPVKQAEEKPQRTQNINSNANMLRKGPAEDMSSKLNQARSLSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYSTHMADEKLDKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDTDIEPFLKNSSQFFQSYVERGLRVIEMERESKGRIPTSTGISPQMEVTCVPTPTSTVSSLGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAIPPVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSAGTMTSSSSTTNIDDLKKRLERIKSSRK | null | null | cell division [GO:0051301]; central nervous system myelin formation [GO:0032289]; centrosome cycle [GO:0007098]; centrosome duplication [GO:0051298]; cytoplasmic translation [GO:0002181]; dendritic spine maintenance [GO:0097062]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; excitatory postsynaptic potential [GO:0060079]; habituation [GO:0046959]; locomotory behavior [GO:0007626]; long-term synaptic potentiation [GO:0060291]; microtubule polymerization [GO:0046785]; mitotic spindle organization [GO:0007052]; mRNA localization resulting in post-transcriptional regulation of gene expression [GO:0010609]; positive regulation of endocytosis [GO:0045807]; protein-RNA complex assembly [GO:0022618]; RNA transport [GO:0050658]; visual learning [GO:0008542] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; kinetochore [GO:0000776]; microtubule plus-end [GO:0035371]; neuronal ribonucleoprotein granule [GO:0071598]; perikaryon [GO:0043204]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; spindle pole [GO:0000922] | microtubule binding [GO:0008017]; microtubule plus end polymerase [GO:0061863]; microtubule plus-end binding [GO:0051010]; ribonucleoprotein complex binding [GO:0043021] | PF12348;PF21041; | 1.25.10.10; | TOG/XMAP215 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14008}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q14008}. Note=Detected on centrosomes and kinetochores during interphase and mitosis independently from TACC3 and clathrin. Located to spindle poles and microtubules during mitosis. In complex with TACC3 localized to microtubule plus-ends in mitosis and interphase. In complex with TACC3 and clathrin localized to inter-microtubule bridges in mitotic spindles. Accumulation sites at microtubule plus ends protruded approximately 100 nm from MAPRE1/EB1 sites in interphase cells. {ECO:0000250|UniProtKB:Q14008}. | null | null | null | null | null | FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments. {ECO:0000250|UniProtKB:Q14008}. | Mus musculus (Mouse) |
A2AH22 | AMRA1_MOUSE | MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTTVECCQHPGILCLCSRCAGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGSIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHLPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPSSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLSETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGAASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLPSEPGQLAERALSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDGSNRGEAAGPSGEPQNR | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to starvation [GO:0009267]; mitophagy [GO:0000423]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; neural tube development [GO:0021915]; positive regulation of autophagy [GO:0010508]; positive regulation of free ubiquitin chain polymerization [GO:1904544]; positive regulation of mitophagy [GO:1901526]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of regulatory T cell differentiation [GO:0045591]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of transcription by RNA polymerase II [GO:0006357]; response to mitochondrial depolarisation [GO:0098780] | autophagosome [GO:0005776]; axoneme [GO:0005930]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335] | GTPase binding [GO:0051020]; protein phosphatase binding [GO:0019903]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625] | PF00400; | 2.130.10.10; | WD repeat AMBRA1 family | PTM: Phosphorylation at Ser-52 by MTOR inhibits its ability to regulate autophagy and mediate ubiquitination of ULK1. Phosphorylation by ULK1 in response to autophagy induction abolishes interaction with DYNLL1 and DYNLL2, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation. Phosphorylation by MTOR inhibits interaction with PPP2CA and subsequent dephosphorylation of MYC. Phosphorylation at Ser-1044 by CHUK/IKKA promotes its interaction with ATG8 family proteins GABARAP and MAP1LC3B and its mitophagic activity. {ECO:0000250|UniProtKB:Q9C0C7}.; PTM: Ubiquitinated by RNF2 via 'Lys-48'-linkage in unstressed cells, leading to its degradation by the proteasome (PubMed:24980959). Induction of autophagy promotes stabilization via interaction with CUL4 (CUL4A or CUL4B) and DDB1. Upon prolonged starvation, ubiquitinated and degraded, terminating the autophagy response (By similarity). {ECO:0000250|UniProtKB:Q9C0C7, ECO:0000269|PubMed:24980959}.; PTM: Undergoes proteolytic processing by caspase-6 (CASP6), caspase-7 (CASP7) and caspase-8 (CASP8) during apoptosis, resulting in the dismantling of the autophagic machinery and the accomplishment of the programmed cell death program. Also cleaved by calpains during apoptosis, which mediate a complete proteolytic degradation. {ECO:0000250|UniProtKB:Q9C0C7}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasmic vesicle, autophagosome {ECO:0000305|PubMed:17589504, ECO:0000305|PubMed:24089209, ECO:0000305|PubMed:28362576, ECO:0000305|PubMed:32616651}. Mitochondrion {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasm, cytosol {ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:24980959}. Nucleus {ECO:0000269|PubMed:24980959, ECO:0000269|PubMed:28362576, ECO:0000269|PubMed:32616651}. Cell junction, focal adhesion {ECO:0000269|PubMed:28362576}. Note=Localizes to the cytoskeleton in absence of autophagy induction. Upon autophagy induction, AMBRA1 relocalizes to the endoplasmic reticulum to enable autophagosome nucleation (By similarity). Partially localizes at mitochondria in normal conditions (By similarity). Localizes also to discrete punctae along the ciliary axoneme (PubMed:24089209). {ECO:0000250|UniProtKB:Q9C0C7, ECO:0000269|PubMed:24089209}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854235, ECO:0000269|PubMed:33854239}. | null | null | FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy (PubMed:17589504, PubMed:33854232, PubMed:33854235, PubMed:33854239). The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins such as BECN1, CCND1, CCND2, CCND3, ELOC and ULK1 (PubMed:23974797, PubMed:33854232, PubMed:33854235, PubMed:33854239). Acts as an upstream master regulator of the transition from G1 to S cell phase: AMBRA1 specifically recognizes and binds phosphorylated cyclin-D (CCND1, CCND2 and CCND3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation (PubMed:33854232, PubMed:33854235, PubMed:33854239). By controlling the transition from G1 to S phase and cyclin-D degradation, AMBRA1 acts as a tumor suppressor that promotes genomic integrity during DNA replication and counteracts developmental abnormalities and tumor growth (PubMed:33854232, PubMed:33854235, PubMed:33854239). AMBRA1 also regulates the cell cycle by promoting MYC dephosphorylation and degradation independently of the DCX(AMBRA1) complex: acts via interaction with the catalytic subunit of protein phosphatase 2A (PPP2CA), which enhances interaction between PPP2CA and MYC, leading to MYC dephosphorylation and degradation (PubMed:25438055). Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (By similarity). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation (PubMed:17589504). In normal conditions, AMBRA1 is tethered to the cytoskeleton via interaction with dyneins DYNLL1 and DYNLL2 (By similarity). Upon autophagy induction, AMBRA1 is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (By similarity). The DCX(AMBRA1) complex mediates 'Lys-63'-linked ubiquitination of BECN1, increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (PubMed:23974797). In collaboration with TRAF6, AMBRA1 mediates 'Lys-63'-linked ubiquitination of ULK1 following autophagy induction, promoting ULK1 stability and kinase activity (By similarity). Also activates ULK1 via interaction with TRIM32: TRIM32 stimulates ULK1 through unanchored 'Lys-63'-linked polyubiquitin chains (By similarity). Also acts as an activator of mitophagy via interaction with PRKN and LC3 proteins (MAP1LC3A, MAP1LC3B or MAP1LC3C); possibly by bringing damaged mitochondria onto autophagosomes (PubMed:21753002, PubMed:25215947). Also activates mitophagy by acting as a cofactor for HUWE1; acts by promoting HUWE1-mediated ubiquitination of MFN2 (By similarity). AMBRA1 is also involved in regulatory T-cells (Treg) differentiation by promoting FOXO3 dephosphorylation independently of the DCX(AMBRA1) complex: acts via interaction with PPP2CA, which enhances interaction between PPP2CA and FOXO3, leading to FOXO3 dephosphorylation and stabilization (PubMed:28789945, PubMed:30513302). May act as a regulator of intracellular trafficking, regulating the localization of active PTK2/FAK and SRC (PubMed:28362576). Also involved in transcription regulation by acting as a scaffold for protein complexes at chromatin (PubMed:32616651). {ECO:0000250|UniProtKB:Q9C0C7, ECO:0000269|PubMed:17589504, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:25215947, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:28362576, ECO:0000269|PubMed:28789945, ECO:0000269|PubMed:30513302, ECO:0000269|PubMed:32616651, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854235, ECO:0000269|PubMed:33854239}. | Mus musculus (Mouse) |
A2AHC3 | CAMP1_MOUSE | MVDAGGRCAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQVATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCFYLTLEDMLYAPLVLKPNVMVFIAELFWWFENVKPDFVQPRDIQELKDAKTVLQQKSSRPPVPISNATKRSFLGSPAAMSPADQPPSTQPLAEGSHRYHLHSEEPECLGKGASTFSPSHPLLPLRQKQQKVSQTEEIPDQRHRSNSLTRVDGQPRGAIGAWPDKKNRPVSQPTSFALHHAASCDVDPSSGDSVSLARSISKDSLASNIIHLTPQNQPHPSAGKSNGKSLLSNVNIEDEDEELVAIIRTDVSPPSPQMPRTSPQAPGLVASIRSPQRQADTLESKPDSFYLEPLMPAVLRPAKEKQITTKEDERGEGRPRTIMAKRPSEGSQPMVRKKVSGGHGSRDLNRTFTPIPCSEFAASIDLAEVGPQSAEATGEGQPLALGRFDTLPQGQAADGFFLHVGRAEEDEGRWYVGSQSPSSHDSEPWTILRQDSDSDVVDVEDTEQDFIGEDHPVVIPRYAGEEESAKLQEDMKVKEHEDKDDASGRSSPCLSTTSQLSSMSMASGSVKMTSFAERKLQRLNSCETKSSTSSSQKTTPDASESCPAPLTTWRQKREQSPGRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKKGKADGAPQPLRPEHFTKEFTQHNGEDLDDGTCKTEGFLVKEEQRDLSDAQDVAFVQLHKPRDPAALHDGEKHRMISTALLEDSVGEVDVNECDLSIEKLNETISTLQQAILKISQQQEQLLMKSPTVPTPGTKNNCQDQKIKAPVHFVEPLSPTGVPGHRKPPRLGQGRNSRSGRPAELKVPKDRQQGCSRSKTPTPSVETLPQSRSLPPSTHPRSPSDPGGELPEKCLFDSYRLHDESNHRTFVLSSCKDANIVSEQVNFKEGLDTSVKEAGLSSSTITGKEHTPVEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSVELGGDSDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQGLGKPKSKPKKPRPKSVHREESYSDSGTKCSSTHNLSQTHSGSSLSLASAATTEPESVYSGGTPSHRVESLEALPILSRNPSRSTDRDWETASAASSLASVAEYTGPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTGPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPTVPKKTQTRK | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; neuron projection development [GO:0031175]; regulation of cell morphogenesis [GO:0022604]; regulation of microtubule polymerization [GO:0031113] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules. Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization. In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation. Through interaction with spectrin may regulate neurite outgrowth. {ECO:0000250|UniProtKB:Q5T5Y3}. | Mus musculus (Mouse) |
A2AHL1 | ANO3_MOUSE | MVHHSGSIQSFKQQKGMNISKSEITTEASLKPSRRSLPCLAQSYAHSKSLSQSASLFQSTESESQAPTSVTFLSADKPEHVTSEESRKDSTLKCSFADLSDFCLALGKDKDYLDESEHANYDRSRLLNDFVTKDKPASKTKLSKNDMSYIASSGLLFKDGKKRIDYILVYRKTNIQYDKRNTFEKNLRAEGLMLEKEPAIANPDIMFIKIHIPWDTLCKYAERLNIRVPFRKKCYYTDQKNKSKSRVQNYFKRIKKWMSQNPMVLDKSAFPELEESDCYTGPFSRARIHHFIINNKDTFFSNATRSRIVYHMLERTKYENGISKVGIRKLITNGSYIAAFPPHEGAYKSSLPIKTHGPQNNRHLLYERWARWGMWYKHQPLDLIRMYFGEKIGLYFAWLGWYTGMLIPAAVVGLCVFFYGLVTMNESQVSQEICKATEVFMCPLCDKNCSLQRLNDSCIYAKVTYLFDNGGTVFFAIFMAIWATVFLEFWKRRRSILTYTWDLIEWEEEEETLRPQFEAKYYRMEVINPITGKPEPHQPSSDKVTRLLVSVSGIFFMISLVITAVFAVVVYRLVVMEQFASFKWNFVKQHWQFATSGAAVCINFIIIMLLNLAYEKIAYLLTNLEYPRTESEWENSFALKMFLFQFVNLNSSIFYIAFFLGRFVGHPGKYNKLFERWRLEECHPSGCLIDLCLQMGVIMFLKQIWNNFMELGYPLIQNWWSRHKIKRGIQDASIPQWENDWNLQPMNIHGLMDEYLEMVLQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLPARATDIGIWLGILEGIGILAVITNAFVIAITSDYIPRFVYEYKYGPCANHVKQNENCLKGYVNNSLSFFDLSELGMGKSGYCRYRDYRGPPWSSKPYEFTLQYWHILAARLAFIIVFEHLVFGIKSFIAYLIPDIPKGLRERIRREKYLVQEMMYEAELEHLQQQRRKSGQPIHHEWP | null | null | calcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; chloride transmembrane transport [GO:1902476]; detection of mechanical stimulus [GO:0050982]; detection of temperature stimulus [GO:0016048]; establishment of localization in cell [GO:0051649] | plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; phospholipid scramblase activity [GO:0017128]; protein dimerization activity [GO:0046983] | PF16178;PF04547; | null | Anoctamin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Shows an intracellular localization. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:23532839}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; Evidence={ECO:0000305|PubMed:23532839}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in); Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390; Evidence={ECO:0000269|PubMed:23532839}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900; Evidence={ECO:0000305|PubMed:23532839}; | null | null | null | null | FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide (PubMed:23532839). Does not exhibit calcium-activated chloride channel (CaCC) activity (PubMed:23532839). Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity (PubMed:23872594). {ECO:0000269|PubMed:23532839, ECO:0000269|PubMed:23872594}. | Mus musculus (Mouse) |
A2AI05 | NDOR1_MOUSE | MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRKSLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVPLDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDVSEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA | 1.18.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; | electron transport chain [GO:0022900]; iron-sulfur cluster assembly [GO:0016226] | cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471] | electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADPH binding [GO:0070402]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor [GO:0016731]; oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor [GO:0016653] | PF00667;PF00258;PF00175; | 3.40.50.360;3.40.50.80;2.40.30.10; | NADPH-dependent diflavin oxidoreductase NDOR1 family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; | null | null | null | null | FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (By similarity). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP-Rule:MF_03178}. | Mus musculus (Mouse) |
A2AI08 | TPRN_MOUSE | MAGLGRLDPGPRTVMPAWKREILERRRAKLAALSGGQGSGAAPDGPNERLVLAESLGPLSQNPFMRLESERRRGTRPAQQLLELYCRVPGVRTIRADNILIIESAPGFPPAVPPAAGIRAAEVVVYEAPQPGRVSRLLEKFDSPAAPCRRGSPERFRPALPQLPVASASAATRTPTNRSLAPASPVRLSQPAPPISPVPVAQRAGQRSACCEPAHPDGTAGPGARRSDFLQKTGSNSFTVHPRGLPRSAVNRSLSNGPMTQESPTGPANGLSGSPPVPGKWKPKVESKEPSLHPPPSPGTPSATSVGPPAFPAPSPASATPSQRQWVSSATSANDSFEIRPSSKPDMETIPIGDLQARALANLRVNSRNSFVLIPKRKAPGNYPLAGRQFEEPKGEVGWASQSQGLGSQLVSTVDGAPALEKSPLAAEMQWAVRKGACPRPAISDTDKCVRWQRPASPPPFLPATAEAEPAEGLGVPGLAKNGQEPVRPGLPVTFIDEVDSEEEAFQEAKLPSSAVGVPSQYHLHPARPGHTSELLNRGSNTFTVVPKRKPGTLQEPHLSQTNGQSQQGAEEQDAESLSGPHTTLENTLKKRYPTVHEIEVIGGYLALQKSCLIKAGSSRKKMKISFNDKSLHTTFEYPSESSLAQEEAEEEEEEEGEEDGEEEEVGPDSEKPFTVFLPRATFVSSVGPESSSGLSSYTPKHSMAFSKWQEQTLVQTPTDVELPPKEVMLTPASQNDLSDFRSEPALYF | null | null | auditory receptor cell stereocilium organization [GO:0060088]; sensory perception of sound [GO:0007605]; stereocilium maintenance [GO:0120045] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; microvillus [GO:0005902]; nucleoplasm [GO:0005654]; stereocilium [GO:0032420]; stereocilium base [GO:0120044] | actin binding [GO:0003779]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase inhibitor activity [GO:0004865] | PF13914;PF13916; | null | Taperin family | null | SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:20170899, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:30159668, ECO:0000269|PubMed:30380417, ECO:0000269|PubMed:35752427, ECO:0000269|PubMed:37952086}. Cell projection, microvillus {ECO:0000269|PubMed:24285636}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4KMQ1}. Cytoplasm {ECO:0000250|UniProtKB:Q4KMQ1}. Note=Localized prominently at the basal taper region of hair cell stereocilia (PubMed:20170899, PubMed:30159668, PubMed:30380417, PubMed:37952086). Forms organized ring-like structures with diameters ranging from 150 to 200 nm in the stereocilium taper region (PubMed:37952086). Detected in microvilli of inner hair cell supporting cells (PubMed:24285636). Predominantly nuclear in non-stereocilium cells but can shuttle between the nucleus and the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q4KMQ1, ECO:0000269|PubMed:20170899, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:30159668, ECO:0000269|PubMed:30380417, ECO:0000269|PubMed:37952086}. | null | null | null | null | null | FUNCTION: Essential for hearing (PubMed:30380417, PubMed:35752427, PubMed:37952086). Required for maintenance of stereocilia on both inner and outer hair cells (PubMed:27693694). Necessary for the integrity of the stereociliary rootlet (PubMed:30159668). May act as an actin cytoskeleton regulator involved in the regulation of actin dynamics at the pointed end in hair cells (PubMed:30380417). Forms rings at the base of stereocilia and binds actin filaments in the stereocilia which may stabilize the stereocilia (PubMed:37952086). Acts as a strong inhibitor of PPP1CA phosphatase activity (By similarity). Recruited to sites of DNA damage and may play a role in DNA damage repair (By similarity). {ECO:0000250|UniProtKB:Q4KMQ1, ECO:0000269|PubMed:27693694, ECO:0000269|PubMed:30159668, ECO:0000269|PubMed:30380417, ECO:0000269|PubMed:35752427, ECO:0000269|PubMed:37952086}. | Mus musculus (Mouse) |
A2AIR5 | NMD3A_MOUSE | MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTTAPRAASRAQDGGRAGAQRDEPESGTWRPPAPSQGARWLGSALHGRGPPGSRKLGEGAGTETLWPRDALLFAVENLNRVEGLLPYNLSLEVVMAIEAGLGDLPLMPFSSPSSPWSSDPFSFLQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSSVLHIPVLSIVRHEFPRESQNPLHLQLSLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTENNSKFHLESIINITANLSSTKDLLSFLQVQLENIRNSTPTMVMFGCDMGSIRQIFEMSTQFGLSPPDLHWVLGDSQNVEELRTEGLPLGLIAHGKTTQSVFEYYVQDAMELVARAVATATMIQPELALLPSTMNCMDVKTTNLTSGQYLSRFLANTTFRGLSGSIKVKGSTIVSSENNFFIWNLQYDPMGKPMWTRLGSWQGGRIVMDSGIWPEQAQRHKTHFHHPNKLHLRVVTLIEHPFVFTREVDDEGLCPAGQLCLDPMTNDSSILDSLFSSLHSSNDTVPIKFKKCCYGYCIDLLEQLAEDMNFDFDLYIVGDGKYGAWKNGHWTGLVGDLLSGTANMAVTSFSINTARSQVIDFTSPFFSTSLGILVRTRDTAAPIGAFMWPLHWTMWLGIFVALHITAIFLTLYEWKSPFGMTPKGRNRNKVFSFSSALNVCYALLFGRTAAIKPPKCWTGRFLMNLWAIFCMFCLSTYTANLAAVMVGEKIYEELSGIHDPKLHHPSQGFRFGTVRESSAEDYVRQSFPEMHEYMRRYNVPATPDGVQYLKNDPEKLDAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPPNSPLTSNISELISQYKSHGFMDVLHDKWYKVVPCGKRSFAVTETLQMGIKHFSGLFVLLCIGFGLSILTTIGEHIVYRLLLPRIKNKSKLQYWLHTSQRFHRALNTSFVEEKQPCSKTKRVEKSRWRRWTCKTEGDSELSLFPRSNMGPQQLMVWNTSNLSHDNQRKYIFNDEEGQNQLGTQTHQDIPLPPRRRELPASLTTNGKADSLNVARNSVMQELSELEKQIQVIRQELQLAVSRKTELEEYQRTNRTCES | null | null | calcium ion transport [GO:0006816]; dendrite development [GO:0016358]; ionotropic glutamate receptor signaling pathway [GO:0035235]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of dendritic spine development [GO:0061000]; prepulse inhibition [GO:0060134]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; response to ethanol [GO:0045471]; rhythmic process [GO:0048511]; synaptic transmission, glutamatergic [GO:0035249] | cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793] | calcium channel activity [GO:0005262]; glutamate receptor activity [GO:0008066]; glutamate-gated receptor activity [GO:0004970]; glycine binding [GO:0016594]; identical protein binding [GO:0042802]; NMDA glutamate receptor activity [GO:0004972]; protein phosphatase 2A binding [GO:0051721]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF00060;PF10613;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, NR3A/GRIN3A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1M7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic density {ECO:0000250|UniProtKB:Q9R1M7}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities. Requires the presence of GRIN1 to be targeted at the plasma membrane. {ECO:0000250|UniProtKB:Q9R1M7}. | null | null | null | null | null | FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. During the development of neural circuits, plays a role in the synaptic refinement period, restricting spine maturation and growth (By similarity). By competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting signaling and limiting the maturation and growth of inactive synapses (PubMed:24297929). May also play a role in PPP2CB-NMDAR mediated signaling mechanism (By similarity). {ECO:0000250|UniProtKB:Q9R1M7, ECO:0000269|PubMed:24297929}. | Mus musculus (Mouse) |
A2AIV2 | VIR_MOUSE | MAVDSSMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSGLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPTLKRNLKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPMSLPVSGDKEEDVPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEPQEEGEDDEDDVDVEEEEDEDEDDCHTVDSIPDDEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPNFDVEYTPEDLASVPPMTYDPYDRELAPLLYFSCPYKTTFEIEISRMKDQGPDKENSGAVEASVKLTELLDLYQEDRGAKWVTALEEIPSLIIKGLSYLQLKNTEQDSLGQLVDWTMQALNLQVAFRQPIALNVRQLKAGTKLVTSLAECGAPGVTELLQAGVINVLFDLLFADHVSSSLKLNAFKALDSVISMTEGMEAFLRSTQNEKSGYQRLLELILLDQTVRVVTAGSAILQKCHFYEILSEIKRLGDHIAEKTSAVPNHSEPDQDTDAVLERANPDYENEVEASMDMDLLESSIISEGEIEKLTNLLEEVFHVMETAPHTMTQPPVKSFPTIARITGPPERDDPYPVLFRYLHSHHFLELVTLLLSIPITSAHQGVLQATKDVLKFLAQSQKGLLFFMSEYEATNLLIRALCHLYDQDEEEGLQSDGADDAFALWLQDSTQTLQCITELFSHFQRCTASEETDHSDLLGTLHNLYLITFNPVGRSAVGHVFSLDKNLQSLITLMEYYSKEALGDSKSKKSVAYNYACVLTLVVAQSSSGVQMLEQHAASLLKLCKADENNAKLQELGKWLEPLKNLRFEINCIPNLIEYVKQNIDNLMTAEGVGLTTALRVLCNVACPPPPVEGQQKDLKWNLAVIQLFSAEGMDTFIRVLQKLNSILTQPWRLHVNMGTTLHRVTTISMARCTLTLLKTMLTELLRGGSFEFKDMRVPSALVTLHMLLCSIPLSGRLDSDEQKIQNDIIDILLTFTQGVNEKLTISEETLANNTWSLMLKEVLSSILKVPEGFFSGLILLSELLPLPLPMQTTQVIEPHDISVALNTRKLWSMHLHVQAKLLQEIVRSFSGTTCQPIQHMLRRICVQLCDLASPTALLIMRTVLDLIVEDLQSTSEDKEKQYTSQTTRLLALLDALASHKACKLAILHLINGTIKGDERYAEIFQDLLALVRSPGDSVTRQQCVEYVTSILQSLCDQDIALILPSPSEGPASELEQLSNSLPSKELMTAICDCLLATLANSESSYNCLLTCVRTMMFLAEHDYGLFHLKSSLRKNSSALHSLLKRVVSTFSKDTGELASASLDFMRQILNADAMGCCGDDSGLMEVEGAHPPRTMSLNAAELKQLLQSKEESPESLFLELEKLVLEHSKDDDSLESLLDNVIGLKQMLESSGEPLPLSDQDVEPVLSAPESLQNLFNNRTAYVLADVMDDQLKSMWFTPFQAEEIDTDLDLVKVDLIELSEKCCSDFDLHSELERSFLSEPSSPGRSKTTKGFKLGKHKHETFITSSGKSEYIEPAKRAHVVPPPRGRGRGGFGQGIRPHDIFRQRKQNTSRPPSMHVDDFVAAESKEVVPQDGIPPPKRPLKVSQKISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRGNYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASTNSGSGGSRGKFVSGGSGRGRHVRSFTR | null | null | mRNA alternative polyadenylation [GO:0110104]; mRNA methylation [GO:0080009]; RNA splicing [GO:0008380] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396] | RNA binding [GO:0003723] | PF15912; | null | Vir family | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q69YN4}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}. | null | null | null | null | null | FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites. Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA). {ECO:0000250|UniProtKB:Q69YN4}. | Mus musculus (Mouse) |
A2AIV8 | CARD9_MOUSE | MSDYENDDECWSTLESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYELAMCLAHLSEEKGAALMRNRDLQLEVDRLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKDLLQARVQELQVSVQEGKLDRNSPYIQVLEEDWRQALQEHQKQVSTIFSLRKDLRQAETLRARCTEEKEMFELQCLALRKDAKMYKDRIEAILLQMEEVSIERDQAMASREELHAQCTQSFQDKDKLRKLVRELGEKADELQLQLFQTESRLLAAEGRLKQQQLDMLILSSDLEDSSPRNSQELSLPQDLEEDAQLSDKGVLADRESPEQPFMALNKEHLSLTHGMGPSSSEPPEKERRRLKESFENYRRKRALRKMQNSWRQGEGDRGNTTGSDNTDTEGS | null | null | antifungal innate immune response [GO:0061760]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; host-mediated regulation of intestinal microbiota composition [GO:0048874]; immunoglobulin mediated immune response [GO:0016064]; JNK cascade [GO:0007254]; neutrophil mediated immunity [GO:0002446]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production [GO:0001819]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of innate immune response [GO:0045089]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of JNK cascade [GO:0046330]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of T-helper 17 type immune response [GO:2000318]; positive regulation of tumor necrosis factor production [GO:0032760]; protein homooligomerization [GO:0051260]; regulation of apoptotic process [GO:0042981]; regulation of interleukin-2 production [GO:0032663]; regulation of interleukin-6 production [GO:0032675]; regulation of tumor necrosis factor production [GO:0032680]; response to aldosterone [GO:1904044]; response to exogenous dsRNA [GO:0043330]; response to fungus [GO:0009620]; response to muramyl dipeptide [GO:0032495]; response to peptidoglycan [GO:0032494]; response to xenobiotic stimulus [GO:0009410]; stress-activated MAPK cascade [GO:0051403] | CBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | CARD domain binding [GO:0050700]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621] | PF00619; | 1.10.533.10; | null | PTM: Phosphorylated at Thr-231 by PRKCD downstream of C-type lectin receptors activation: phosphorylation promotes interaction with BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:22265677). Phosphorylated at Thr-531 and Thr-531 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B (By similarity). {ECO:0000250|UniProtKB:Q9EPY0, ECO:0000269|PubMed:22265677}.; PTM: Ubiquitinated at Lys-125 via 'Lys-27'-linked ubiquitin by TRIM62 downstream of C-type lectin receptors activation; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). Deubiquitinated at Lys-125 by USP15, inhibiting CARD9 (By similarity). {ECO:0000250|UniProtKB:Q9H257}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H257}. | null | null | null | null | null | FUNCTION: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors (PubMed:16862125, PubMed:20538615, PubMed:26679537, PubMed:29080677). CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota (PubMed:16862125, PubMed:20538615, PubMed:24470469, PubMed:25621893, PubMed:26679537, PubMed:29080677, PubMed:32548948). Transduces signals in myeloid cells downstream of C-type lectin receptors CLEC7A (dectin-1), CLEC6A (dectin-2) and CLEC4E (Mincle), which detect pathogen-associated molecular pattern metabolites (PAMPs), such as fungal carbohydrates, and trigger CARD9 activation (PubMed:16862125, PubMed:20538615). Upon activation, CARD9 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:16862125, PubMed:20538615, PubMed:22265677, PubMed:29080677). CARD9 signaling in antigen-presenting cells links innate sensing of fungi to the activation of adaptive immunity and provides a cytokine milieu that induces the development and subsequent of interleukin 17-producing T helper (Th17) cells (PubMed:17450144, PubMed:24470469, PubMed:32358020). Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (PubMed:17486093). CARD9 can also be engaged independently of BCL10: forms a complex with RASGRF1 downstream of C-type lectin receptors, which recruits and activates HRAS, leading to ERK activation and the production of cytokines (PubMed:25267792). Acts as an important regulator of the intestinal commensal fungi (mycobiota) component of the gut microbiota (PubMed:27158904, PubMed:33548172). Plays an essential role in antifungal immunity against dissemination of gut fungi: acts by promoting induction of antifungal IgG antibodies response in CX3CR1(+) macrophages to confer protection against disseminated C.albicans or C.auris infection (PubMed:33548172). Also mediates immunity against other pathogens, such as certain bacteria, viruses and parasites; CARD9 signaling is however redundant with other innate immune responses (PubMed:17187069, PubMed:26679537, PubMed:29080677). In response to L.monocytogenes infection, required for the production of inflammatory cytokines activated by intracellular peptidoglycan: acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B (PubMed:17187069). {ECO:0000269|PubMed:16862125, ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:17450144, ECO:0000269|PubMed:17486093, ECO:0000269|PubMed:20538615, ECO:0000269|PubMed:22265677, ECO:0000269|PubMed:24470469, ECO:0000269|PubMed:25267792, ECO:0000269|PubMed:25621893, ECO:0000269|PubMed:26679537, ECO:0000269|PubMed:27158904, ECO:0000269|PubMed:29080677, ECO:0000269|PubMed:32358020, ECO:0000269|PubMed:32548948, ECO:0000269|PubMed:33548172}. | Mus musculus (Mouse) |
A2AIW0 | ENTR1_MOUSE | MSGYARRQGAPPLSRTRSLVVPDAPAFYERRSCLPQLDCERPHGGDLHPHLFGFRPTFMCYVPSPVLASVGDTGFGYGKGKCTNQGPSGAPETRFGGDKLEDLEEANPFSFKEFLKTKNLSLSKEDTTTSRIYPKEASRHPLGLEHSSPASQLMGYGLESQQPFFEDPTRASNLEEDEDDGWNITYLPSAVDQTHSSRDTQDSPPCDTYLSFFSNSSELACPESLPPWTLSDTDSRISPASPAGSPNADFAAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGASLSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLVAEILKSIDRISEVKDEVDS | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell projection organization [GO:0030030]; endocytic recycling [GO:0032456]; positive regulation of cilium assembly [GO:0045724]; positive regulation of protein localization to cilium [GO:1903566]; protein transport [GO:0015031]; regulation of cytokinesis [GO:0032465] | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; early endosome [GO:0005769]; midbody [GO:0030496]; recycling endosome [GO:0055037]; retromer complex [GO:0030904] | null | null | null | ENTR1 family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q96C92}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16332174}. Early endosome {ECO:0000250|UniProtKB:Q96C92}. Endosome {ECO:0000250|UniProtKB:Q96C92}. Recycling endosome {ECO:0000250|UniProtKB:Q96C92}. Midbody {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q96C92}. Note=Colocalizes in a WASHC2-dependent manner with the retromer CSC complex at endosomes. During cytokinesis colocalized with PTPN13 at the midbody. Colocalizes with IFT88 and gamma-tubulin at the basal body of primary cilia. Colocalizes with IFT88 and pericentrin at the centrosome. {ECO:0000250|UniProtKB:Q96C92}. | null | null | null | null | null | FUNCTION: May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (PubMed:16332174). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1 (By similarity). {ECO:0000250|UniProtKB:Q96C92, ECO:0000269|PubMed:16332174}.; FUNCTION: Endosome-associated protein that plays a role in membrane receptor sorting, cytokinesis and ciliogenesis. Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1. Plays a role in the formation of cilia. Involved in cargo protein localization, such as PKD2, at primary cilia (By similarity). Involved in the presentation of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell surface, and hence in the modulation of the TNF-induced apoptosis (PubMed:16332174). {ECO:0000250|UniProtKB:Q96C92, ECO:0000269|PubMed:16332174}. | Mus musculus (Mouse) |
A2AJ15 | MA1B1_MOUSE | MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLSLDSCVFNTEAHPLPIWAPA | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; | carbohydrate metabolic process [GO:0005975]; ERAD pathway [GO:0036503]; mannoprotein catabolic process [GO:0006058]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; endosome [GO:0005768]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2AJ76 | HMCN2_MOUSE | MTPGAQLLPLLVAISTAVAAVVTSDAPTKTLSPATGDATLAFVFDVTGSMWDDLMQVIDGASRILERSLSSRSRVIANYALVPFHDPDIGPVTLTADPVVFQRELRELYVQGGGDCPEMSVGAIKAAVEVANPGSFIYVFSDARAKDYHKKKELLQLLQLKQSQVVFVLTGDCGDRTHPGYLVFEEIASTSSGQVFQLDKQQVSEVLKWVESAIQASKVHLLSADHEEEGEHTWRIPFDPSLKEVTIALSGPGPEIEVRDPLGRVLQTDEGLNVLLNIPDSAKVVAFKPEHPGLWAIKVYSSGRHSVRISGISNINFRAGFSMQPSLDLNHTIEWPLQGVPISLVINSTGLQAPGHLESVELSHSSGRSLLTLPTQLLSNGSTHQLWAGPPFHVPKERFYLKVKGKDHEGNPLLRVSGVSYSAVAPGVPLVSMAPKIHGYLQQPLLVSCSVYSTLPFQLQLQRDGERLGEERYFQESGNSSWEIPRASKAEEGTYQCIAVSRAGSGRASAQIVITDPPPQLVPGPNVTVSPGETAILSCQVLGETPYNLTWVRDWRALPATTGRISQLSDLSLEVRSIIPTDGGQYQCVASNPNGVTRATTWLLVREAPQVSINARSQRFSQGVEVRVSCSASGYPTPHISWSREGLALPEDSRIHVDAQGTLIIQGLAPEDAGNYSCQATNEVGTDEETVTLYYTDPPSVSAVNAVVLTAVGEEAVLLCAASGVPPPRVIWYRGGLEVILAPGDSRSGTLRIPEAQERDAGLYTCKAVNELGDASAEIQLVVGNAPRLTDPPQDVTVELGKSVFLTCRATGRPPPIVTWRRGDGQALEPGRGSRTGQRDSGVLVFERVSLEDQAPYVCEARNVFGKAQAEARLVVTGHAPPQIANSASVVRVLEGQPVSLTCVILAGRPLPERRWLKAGSPLPPGNRHAVRADGSLHLDRALQEDAGRYSCVATNVAGSQHRDVELVVQVPPRIHPTSTHHVTNEGVPASLPCIASGVPTPKITWTKETNALTTSGHYSVSRNGTLVIVQPSPQDAGAYVCTATNSVGFSSQEMWLSVNTKPMIKMNGSQAVDVPLRVTVKAGEEVTLDCEAQGSPTPLLTWTKDANPLLPVTNRYELLPSGSLRLAQAQVGDNGLYGCTASNPAGATSRRYVLRVQVPPQVQPGPRVLKVLAGEALDLNCVAEGNPQPQLNWFKDGMALMGEGAQGSVHFAAVKTSDAGLYRCEASNSAGTDTWKLELLVLEPPHWGTDETKSLLERVAGENASLPCPAQGTPKPRITWRRGPSSEPLNGRPDVAVLDEGSLFLSSVSLADSGEYECQATNEVGSASRRAKLVVYVPPSIREEGHITNVSGLAGQPLTLECDINGFPAPEVAWLKDGQLVGDSGGGWDGEEASGHRLLDGSRSLHFPRIQESHSGLYSCQAENQAGSAQRDFNLAVFIPPSLLGAGAAQEVLGLAGADVTLECQTSGVPTPQVEWTKDGQPILPGDPHILLQEDGQVLRIISSHLGDEGQYQCVAFSPAGQQAKDFQLSIHSPPTIWGSNETGEVTVLEGHTAQLLCEARGMPSPAITWYKDGTLLAPSSEVVYSKGGRQLQLVKAQPSDAGLYTCQASNPAGITKKSTSLEVYVPPTIEGADGGPYLVQAVAGRPVALECVARGHPPPTISWQHEGLPVVDSNGTWLEAGGALQLENPGEASGGLYSCVASSPAGEAVLQYSVEMQVPPQLLVAEGMGQVTATVGQSLDLPCQASGSPVPTIQWLQNGRPAEELAGVQLASQGTILHISHVELNHSGLFACQATNEAGTAGAEVEVSVHGKQVSVNLGASFSAHHWWGEPHSPFPATCNPPVCRHWSAYPKPSLVERWRGRGNLRGQPSGTVREPGLTLLSQIEKADLRDEGVYTCSATNLAGESKKDVTLKVLVPPNIEPGPVNKVVLENASVTLECLASGVPPPDVSWFKGRQPISTQRRVIVSADGRVLHIERVQLSDAGSYRCVATNVAGSAGLKYGLRVNVPPRITLPPNLPGPVLLGTPFRLTCNATGTPRPTLIWLKDGNPVSPEGIPGLKVFPGGQVLTVASARASDSGSYSCVAVSAVGEDRRDVILQVHMPPSILGEELNMSVVVNESVTLECQSHAVPPPVLRWQKDGRPLEPHPGIRLSADKALLEVDRAAVWDAGHYTCEAINQAGRSEKHFNLHVWVPPAFPSKEPYTLTVTEGQTARLSCDCQGIPFPKISWRKDGQPLPGEGDSLEQVLAVGRLLYLGQAQSAQEGTYTCECSNAAGTSSQEQSLEVLVPPQVTGLWEPLTTVSVIQDGNTTLACNATGKPLPVVTWQRDGQPVSVEPGLRLQNQNHSLHVERAQASHAGGYSCVAENTAGRAERRFALSVLAPPHLTGDSDSLTNVTATLHGSFTLLCEAAGVPAPTVQWFQEGQPISPREGTYLLAGGWMLKMTQAQEQDRGLYSCLASNEAGEARRNFSVEVLVPPSIENEDLEEVIKVPEGQTAQLECNATGHPPPKVTWFKDGQSLTVEDPYEMSPDGAFLWIPQANLSNAGHYSCIASNAVGEKTKHTQLSVLVVPTILGVPEKNANEEVTVTINNPISLICEALAFPSPNITWMKDGSPFEASKNIQLLPGTHGLQILNAQKEDAGQYTCVVTNELGEATKNYHVEVLIPPSISKDDPLGEVSVKEVKTKVNSSLTLECECWATPPPSISWYKDGRPVTPSHRLSVLGEGRLLQIQPTQVSDSGRYLCVATNVAGEDDQDFNVLIQVPPMFQKMGDVDAGFEPLPHEEEAQGRVTEYREIVENNPAYLYCDTNAIPPPELTWYREGQPLSAADGVSVLQGGRILQLPLVQAEDAGRYSCKAANEVGEDWLHYELLVLTPPVIPGDTQELVEEVTVNASSAVSLECPALGNPAPAVSWFQNGLPVSPSPRLQVLEEGQVLKVATAEVADAASYMCVAENQAGSAEKLFTLKVQVPPQISDWTTSQLTATLNSSVSLPCEVYAHPNPEVTWYKDGQPLSLGQEAFLLPGTHTLRLARAQPADSGTYLCEALNAAGRDQKMVQLNVLVPPSFKQAPGGPQEAIQVRAGDKAILSCETDSLPEPAVTWFKDQQPLALGQRIQGLQGGQTLEILDSQASDKGVYSCKVSNTAGEAIRTFVLAIQVPPTFEKPERETVNQVAGRTLVLACDVSGIPAPTVTWLKDRLPVESSVVHGVVSRGGRLQLSHLQPAQAGTYTCVAENAQAEARKDFVVSVLVPPQIQDSGMAQEHNVLEKQEIRLHCEAEGQPPPDITWLKDGGLLDQHVGPHLRFYLDGSTLVLKGLRTADSGAYTCVAHNPAGEDARLHTVNVLVPPTIKQQAGDTGTLVSRTGELVTMVCPVQGSPPIHVSWLKDGLPLPLSQRTLLHSSGRTLRISQVQLADSGVFTCVAASPAGVADRNFTLLVLVPPILEPVEFQNNVMAAQGSEVVLPCEARGSPLPLVSWMKDGEPLLPQSLEQGPGLKLESVSVGDAGTYSCTAASEAGEARRHFQLTVMDPPHIEESGETSELSLTPGAHLELLCEARGIPPPNITWHKDGQALRRTENDSQAGRVLRVDNAGLYTCLAESPAGEVEKSFRVRVQAPPNVVGPRGPRSVVGLAPGQLILECSVEAEPAPEIEWHRGGVLLQADAHTHFPEQGRFLKLQALSTADGGDYSCTARNRAGSTSVAFRVEIHTAPTIQSGPNTVNVSVNRTTLLPCQTHGVPTPLVSWRKDGIPLHPGSPRLEFLPEGSLRIHPVLAQDAGHYLCLASNSAGSDRKGLDLRVFEPPAIAPGPSNLTLTAYSPASLPCEARGSPKPLVTWWKDGQKLDLRLQQGAYRLLPSNALFLTAPSPQDSAQFECVVSNEVGESRRRYQVTVHVPPTIADDQTHFTVTRMAPVILTCHSTGSPTPAVSWSKAGTQLGARGSGYRILPSGALEIERALPLHAGRYTCTARNSAGVARKHMVLTVQASPVVKPLPSVVQVVASEEVLLPCEASGIPQPMVIWQKEGLSIPEGAHMQVLPSGQLRIMHASPEDAGNYFCIAQNSVGSAMAKTRLVVQVPPVIENGLPDLSTIEGSHALLPCTAKGSPEPAITWEKDGHLVSGAEGKFTLQPSGELLVKNSEGQDAGTYICTAENAVGRARRRVHLTILTLPVLTTLPGDRSLRLGDRLWLRCVARGSPTPRIGWTINDQPVTEGVSEQDGGSTLQRAAVTREDSGTYTCWAENRVGRVQAVSFVHVKEAPVLQGEAFSYLVEPVGGSIQLHCVVRGDPAPDIHWTKDGLPLPISRLHFQLQNGSLTILRTKMDDAGRYQCLAVNEMGTVKKVVTVVLQSAPVFQVEPQDVTVRSGVDVELRCRATGEPVPTIEWLRAGRPLQAGRKLRALPDGSLWLEHVEAGDAGVYECVAHNHLGSVTAKALLAVRGEPRGSRGSMTGVINGQEFGMATLNISVLQQGSSEAPTIWSSISQVPASVGPLMRVLVVTIAPIYWALARESGEALNGYSLTGGSFQQESQMEFSTGELLTMTQVARGLDPDGLLLVDMKINGMIPESLADGDLRVQDFQEHYVQTGPGQLFAGSTQRFLHDSLPASLRCNHSIQYDETRGLQPQLVQHLRASSISSAFDPEAEALNFQLTTALQTEENEVGCPEGFEPDVQGAFCVDKDECSGGPSPCSHTCRNAPGHFSCSCPTGFSLAWDHRNCRDVDECAGNTHLCQEEQRCVNLLGSYNCLASCRPGFRVTADGSNCEDVDECLEQLDECHYNQLCENTPGGHHCGCPRGYRQQGHSLPCLDINECLQLPTPCVYQCQNLQGSYRCLCPPGQTLLRDGRTCIPLERNRQNITIVSHRSPFGPWLRSRVPRPSSSYHTWVSLRPGSGALNSVGRAWCPPGFIRQDGVCADLDECRVRSLCQHACQNTEGSYYCLCPSGYRLLPSGKNCQDINECEEDGIECGPGQMCFNTRGSFQCVDTPCPTTYRQGSSPGTCFRRCSQDCSASGPSTLQYRLLPLPLGVRAHHDVARLAAFSEAGIPANRTELTVLEPDPRSPFALRQLRAGQGAVYTRRALTRAGLYRLTVRAAAPRHQSVYILLIAVSPYPY | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; response to stimulus [GO:0050896]; synapse organization [GO:0050808] | axon [GO:0030424]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cleavage furrow [GO:0032154]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046]; calcium ion binding [GO:0005509] | PF12662;PF07645;PF07474;PF07679;PF13927; | 2.40.155.10;2.60.40.10;2.10.25.10;3.40.50.410; | null | PTM: Reported to be phosphorylated; however as this position is extracellular, the in vivo relevance is unsure. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17015624}. Cleavage furrow {ECO:0000269|PubMed:21215633}. Note=The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633}. | null | null | null | null | null | null | Mus musculus (Mouse) |
A2AJ77 | PRD12_MOUSE | MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLLEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPVEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEEQKKNKHEDFHPADSATGTAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKSARHRPPSTALQAHSPALPAPHAHAPALAAAAAAAAAAHHLPAMVL | 2.1.1.- | null | detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neurogenesis [GO:0022008]; neuron projection development [GO:0031175]; regulation of gene expression [GO:0010468]; sensory perception of pain [GO:0019233] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; histone chaperone activity [GO:0140713]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168] | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Q4}. | null | null | null | null | null | FUNCTION: Involved in the positive regulation of histone H3-K9 dimethylation. {ECO:0000269|PubMed:26005867}. | Mus musculus (Mouse) |
A2AJ88 | PLPL7_MOUSE | MQNEEDACLEAGYCLGTTLSSWRLHFMEEQSQSTMLMGIGIGALLTLAFVGITFFFVYRRVRRLRRAEPTPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTSAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSLRPSEFSSSDHGSSCVTVSGPLLKRSCSVPLPSNHGEVDELRQSQGSGSNTSAFQESHEGATSDLGMAYNRARILPHSDEQLGNSLASKSKKSVVAETPSAIFHYSENFRDETGACGKTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVKRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSATGHQLGFNTASSKWDLGNPPGNLSTVAALPASEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADGTLTPWTQRCIRQADCILIVGLGEQEPAVGELEQMLESTAVRAQKQLILLHKEDGPVPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRVFQRPPDRHSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGMTSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQDQQGTSKRKDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSEYEPSMLQGPPSLTSPEQSQDSFPWLPNQDDQGPRLEHPS | 3.1.1.-; 3.1.1.5 | null | phosphatidylcholine catabolic process [GO:0034638] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811] | lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545] | PF00027;PF01734; | 3.40.1090.10;2.60.120.10; | NTE family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; Single-pass type III membrane protein {ECO:0000269|PubMed:28887301}. Lipid droplet {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823; Evidence={ECO:0000269|PubMed:28887301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000269|PubMed:28887301}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:28887301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000269|PubMed:28887301}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000269|PubMed:28887301}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000269|PubMed:28887301}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:18086666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000269|PubMed:18086666}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:18086666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000269|PubMed:18086666}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18086666}; | null | FUNCTION: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine (PubMed:18086666, PubMed:28887301). Can also deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0) (PubMed:18086666, PubMed:22326266, PubMed:28887301). {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266, ECO:0000269|PubMed:28887301}.; FUNCTION: [Isoform 2]: Lysophospholipase. {ECO:0000269|PubMed:22326266}.; FUNCTION: [Isoform 3]: Lacks lysophospholipase activity. {ECO:0000269|PubMed:22326266}. | Mus musculus (Mouse) |
A2AJB7 | LCN5_MOUSE | MCSVARHMESIMLFTLLGLCVGLAAGTEAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKHDLTCVNALQSGQI | null | null | retinoic acid metabolic process [GO:0042573] | extracellular space [GO:0005615] | retinoid binding [GO:0005501]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | PTM: 2 different forms with differently processed N-termini exist. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. Note=Synthesized by the mid and distal caput of the epididymis and secreted into the epididymal lumen. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. | null | null | null | null | null | FUNCTION: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:1591333}. | Mus musculus (Mouse) |
A2AJK6 | CHD7_MOUSE | MADPGMMSLFGEDGSLFSEGLEGLGECGYPENPVNPMGQQMPIDQGFPSLQPSLHHPSPNQNQTKLTHFDHYSQYEQKMHLMDQPNRMMGSAPGNGLASPHSQYHTPPVPQVPHGGGGGGQMGVYPGIQNERHGQSFVDGGSMWGPRAVQVPDQIRAPYQQQQPQPAPSGPPAQGHPQHMQQMGSYLARGDFSMQQHGQPQQRMGQFSQGQEGLSQGSPFIATSGPGHLSHMPQQSPSMAPSLRHPVQQQFHHHPAALHGESVAHSPRFSPNPPQQGAVRPQTLNFSSRNQTVPSPTVNNSGQYSRYPYSNLNQGLVNSTGMNQNLGLTNSTPMNQSVPRYPNAVGFPSNSGQGLVHQQPIHSSGSLNQMNTQTMHPSQPQGTYASPPPMSPMKAMSNPAGTPPPQVRPGSAGMPMEVGSYPNMPHPQPSHQPPGAMGIGQRNMGPRNMQQPRSFMGMSSAPRELTGHMRPNGCPGVGLADPQAIQERLIPGQQHPGQQPSFQQLPTCPPLQPHPGLHQSSPPHPHHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLEKPVPDMTQVSAQNAQLVKSDDYLPSIEQQPQQKKKKKKNNHIAAGDSSKGFGKDDFPGGVENQELRRNSLDVSQEEKKKKKRPKVKKDPKESKEPKEKKEPKTPKAPKIPKEPKEKKAKTVTPKPKSSKKSSNKKPDSEASALKKKVNKGKTEGSENSDLDKTPPPSPAPEEDEDPGVQKRRSSRQVKRKRYTEDLEFKISDEEADDADAAGRDSPSNTSQSEQQESVDAEGPVVEKIMSSRLVKKQKESGEEVEVEEFYVKYKNFSYLHCQWASVEDLEKDKRIQQKIKRFKSKQGQSKFLSEIEDDLFNPDYVEVDRIMDFARSTDDRGEPVIHYLVKWCSLPYEDSTWELKQDIDQTKIEEFEKLMSREPETERVERPPADDWKKSESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPKEETIIEVELTNIQKKYYRAILEKNFTFLSKGGGQANVPNLLNTMMELRKCCNHPYLINGAEEKILEEFKETHNAESPDFQLQAMIQAAGKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRENATNGVQQLSKKEIEDLLRKGAYGALMDEEDEGSKFCEEDIDQILLRRTHTITIESEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKKAELDIDALNGRNNLVIDTPRVRKQTRLYSAVKEDELMEFSDLESDSEEKPCAKPRRPQDKSQGYARSECFRVEKNLLVYGWGRWTDILSHGRYKRQLTEQDVETICRAILVYCLNHYRGDENIKSFIWDLITPTADGQTRALLNHSGLSAPVPRGRKGKKVKAQSTQPVVHDAHWLASCNPDALFQEDSYKKHLKHHCNKVLLRVRMLYYLRQEVIGDQAEKILEGADSSEADVWIPEPFHAEVPTDWWDREADKSLLIGVFKHGYEKYNSMRADPALCFLERVGMPDAKAIAAEQRGTDMLADGGDGGEFDREDEDPEYKPTRAPFKDEIDEFANSPAEDKEESMEVHSSGKHSESNAELGQLYWPNTSTLTTRLRRLITAYQRSYKRQQMRQEALMKTDRRRRRPREEVRALEAEREAIISEKRQKWTRREEADFYRVVSTFGVIFDPVKQQFDWNQFRAFARLDKKSDESLGKYFSCFVAMCRRVCRMPAKPEDEPPDLASLIEPITEERASRTLYRIELLRKIREQVLHHPQLSDRLKLCQPSLDLPEWWECGRHDRDLLVGAAKHGVSRTDYHILNDPELSFLDAHKSFAQNRGASTVPPLNTLAMGFGQTPPVISSAHVHEEKAMEQAEGKAEECEHSPAKERSDGKEEEEEAGGAKDGKQECEVEASSVKGELKGVEGSADPGSKSVSEKGSEEDEEEKLEDDDKSEESSQPEAGAVSRGKTFDEESNASLSTARDETRDGFYMEDGDASVAQLLHERTFAFSFWPKDRVMINRLDNICEAVLKGKWPVNRRQMFDFQGLVPGYPPSAVDSPLQKRSFAELSMVSQASISASEDITTSPQLSKDDALNLSVPRQRRRRRRKVEIEAERAAKRRNLMEMVAQLRESQVVSENGQEKVVDLSKASREATSSTSNFSSLTSKFILPNVSTPVSDAFKSQMELLQAGLSRTPTRHMLNGSLVDGEPPMKRRRGRRKNVEGLDLLFMSHKRTPLSAEDAEVTKAFEEDIETPPIRNIPSPGQLDPDTRIPVINLEDGTRLVGEDAPKNKDLVDWLKLHPTYTVDMPSYVPKNTDVLFSSFQKPKQKRHRCRNPNKLDINTLTGEERVPVVNKRNGKKMGGAMAPPMKDLPRWLEENPEFAVAPDWTDIVKQSGFVPESMFDRLLTGPVVRGEGASRRGRRPKSEIARAAAAAAAVASTSGINPLLVNSLFAGMDLTSLQNLQNLQSLQLAGLMGFPPGLATAATAGGDAKSPAAVLPLMLPGMAGLPNVFGLGGLLNNPLSAATGNTTTASSQGEPEDGTSKAEEKGNDNEDENRDSEKSTDTVSAADSANGSVGAATAPAALPSNPLAFNPFLLSTMAPGLFYPSMFLPPGLGGLTLPGFPALAGLQNAVGTSEEKAADKAEGGPCKDGETLEGSDAEENLDKTVESSILEDEVAQGEELDSLEGGDEIENTGNDE | 3.6.4.12 | null | adult heart development [GO:0007512]; adult walking behavior [GO:0007628]; aorta development [GO:0035904]; aorta morphogenesis [GO:0035909]; artery morphogenesis [GO:0048844]; atrioventricular canal development [GO:0036302]; blood circulation [GO:0008015]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; camera-type eye development [GO:0043010]; cardiac septum morphogenesis [GO:0060411]; central nervous system development [GO:0007417]; chordate embryonic development [GO:0043009]; chromatin remodeling [GO:0006338]; cognition [GO:0050890]; cranial nerve development [GO:0021545]; ear morphogenesis [GO:0042471]; embryonic hindlimb morphogenesis [GO:0035116]; epithelium development [GO:0060429]; face development [GO:0060324]; female genitalia development [GO:0030540]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; inner ear morphogenesis [GO:0042472]; innervation [GO:0060384]; locomotory behavior [GO:0007626]; nose development [GO:0043584]; olfactory behavior [GO:0042048]; olfactory bulb development [GO:0021772]; olfactory nerve development [GO:0021553]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of growth hormone secretion [GO:0060123]; regulation of neurogenesis [GO:0050767]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; response to bacterium [GO:0009617]; retina development in camera-type eye [GO:0060041]; right ventricular compact myocardium morphogenesis [GO:0003226]; roof of mouth development [GO:0060021]; rRNA processing [GO:0006364]; secondary palate development [GO:0062009]; semicircular canal morphogenesis [GO:0048752]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; T cell differentiation [GO:0030217]; tissue remodeling [GO:0048771]; transcription by RNA polymerase II [GO:0006366]; ventricular trabecula myocardium morphogenesis [GO:0003222] | chromatin [GO:0000785]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF07533;PF00385;PF00271;PF00176; | 2.40.50.40;3.40.5.120;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P2D1}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2AJN7 | S4A11_MOUSE | MSQNEHCQDSGEYFSAGTQGYFKNNMEDNLEVREDSLGDEVFDTVNSSIVSGESIRFFVNVNLEVQPSKSDLEAATGGCVLLHTSRKYLKLKNFEEEVRAHRDLDGFLAQASIILNETATSLDDVLRTMLNRFALDPNHAEPDCDLDLLMAKLFTDAGAPMESKVHLLSDTIQGVTATVRGVQYEQSWLCIICTMKTLQKRHVCISRLVRPQNWGENSCEVRFVILVLAPPKMKSTKTAMEVARTFATMFSDITFRQKLLKTRTEEEFKEALVHQRQLLTMMMPRAAGHSMSSLHTHRHPQPPKCKDFFPFGKGIWMDIMRRFPVYPMDFTDGIIGKSKSVGKYVTTTLFLYFACLLPTIAFGSLNDENTNGAIDVQKTIAGQSIGGLLYALFSGQPLVILLTTAPLAIYTQVIRVICDDYNLDFNAFYAWTGLWNSFFLALYAFLNLSLLMNLFKRSTEEIIALFISITFVLDAVKGMVKIFGKYYYGHHYHTKRTSSLVSLLGIGRSPNSSLHTALNASLLASPVEMATTSSPGSTHSGQATAVLSLLIMLGTLWLGYTLYQFKKSPYLHPCVRETLSDCALPIAVLSFSLIGSYGFQEIEMSKFRYNPSESLFEVAQIHSLSFKAIGSAMGLGFLLSLLFFIEQNLVAALVNAPENRLVKGTAYHWDLLLLAIINTGLSLFGLPWIHAAYPHSPLHVRALALVEERVENGHIYETIVDVKETRLTALGASVLVGLSLLLLPFPLQWIPKPVLYGLFLYIALTSLDGNQLFSRVALLLKEQTSYPPTHYIRRVPQRKIHYFTGLQILQLLLLCAFGMSSLPYMKMVFPLIMIAMIPIRYNLLPRIIEAKYLDVMDAEHRP | null | null | cellular hypotonic response [GO:0071476]; cellular response to oxidative stress [GO:0034599]; fluid transport [GO:0042044]; intracellular monoatomic cation homeostasis [GO:0030003]; monoatomic anion transport [GO:0006820]; monoatomic ion homeostasis [GO:0050801]; regulation of mesenchymal stem cell differentiation [GO:2000739]; regulation of mitochondrial membrane potential [GO:0051881]; transmembrane transport [GO:0055085] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506] | active borate transmembrane transporter activity [GO:0046715]; bicarbonate transmembrane transporter activity [GO:0015106]; borate efflux transmembrane transporter activity [GO:0080139]; protein dimerization activity [GO:0046983]; proton channel activity [GO:0015252]; proton transmembrane transporter activity [GO:0015078]; sodium channel activity [GO:0005272]; solute:inorganic anion antiporter activity [GO:0005452]; symporter activity [GO:0015293]; transmembrane transporter activity [GO:0022857]; water transmembrane transporter activity [GO:0005372] | PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBS3}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NBS3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NBS3}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 Na(+)(in) + tetrahydroxoborate(in) = 2 Na(+)(out) + tetrahydroxoborate(out); Xref=Rhea:RHEA:66816, ChEBI:CHEBI:29101, ChEBI:CHEBI:41132; Evidence={ECO:0000250|UniProtKB:Q8NBS3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66817; Evidence={ECO:0000250|UniProtKB:Q8NBS3}; | null | null | null | null | FUNCTION: Multifunctional transporter with an impact in cell morphology and differentiation (PubMed:20185830). In the presence of borate B(OH)4(-), acts as a voltage-dependent electrogenic Na(+)-coupled B(OH)4(-) cotransporter controlling boron homeostasis (By similarity). At early stages of stem cell differentiation, participates in synergy with ITGA5-ITGB1 and ITGAV-ITGB3 integrins and BMPR1A to promote cell adhesion and contractility that drives differentiation toward osteogenic commitment while inhibiting adipogenesis (PubMed:33247189). In the absence of B(OH)4(-), acts as a Na(+)-coupled OH(-) or H(+) permeable channel with implications in cellular redox balance. Regulates the oxidative stress response in corneal endothelium by enhancing antioxidant defenses and protecting cells from reactive oxygen species. In response to hypo-osmotic challenge, also acts as water permeable channel at the basolateral cell membrane of corneal endothelial cells and facilitates transendothelial fluid reabsorption in the aqueous humor. In the presence of ammonia, acts as an electrogenic NH3/H(+) cotransporter and may play a role in ammonia transport and reabsorption in renal Henle's loop epithelium (By similarity). {ECO:0000250|UniProtKB:Q8NBS3, ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:33247189}. | Mus musculus (Mouse) |
A2AJX4 | MALR1_MOUSE | MFLPKAAVSAFSMHGSLCFLWTVCLSISPLSQQGVQAFQCSNGVSLPSDYVCDFTDHCGDNSEEQQCWSYGRCNFEDRLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYNFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQFQVIFQAQMLATHGQEEVIAIDDISFSSGCLPADVCQTCGFDLDTCGLATEASAGRTSWMCTKVREIPSLDSVPWQDQRGHDEGSFVWMRAGHASVSRLVESSAYLNSSVCHCMDGNCRLQFNYTMENSILRVRLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLSQKSFIGIDQLLVYNFGQTHSQKLCSVNEYTPASRQCLTHSSVCDSGMDHSNGIDEDSEACASLLTWDFESGFCGWEPFPTEDSHWEVVRGLSNGEHLFLEAGHTVSRNQGSFIYFGPQKSTAVARLGSPILTKSLTTFTPCQVRFWYHLSEHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEESTLPFQLVLEATILSSNATVAVDDISISHECEISYKSLRSTSIQNKVADCDFEANSCGWFEASGGDHFDWVWSSQSNLSADLEQQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGCTMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHFENCALPPPVESCDEPDHFWCRQTKACIGRHQLCDLVDDCGDYTDETGCAPGLQCNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPMKDHTLGTAKGHYLYIETSGPQGFQDKAVLLSPILNATEAKVCTFRLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSITSRKPFQILIMASVGDGFTGDIAIDDLSFMDCTLYPDNLPMDIPSPPETSVPVTLPPNNCTDDQFVCRSNGHCVGNIQKCDFRYDCIDKSDESSCVLEVCTFEERKLCKWYQPIPANSLHDSNTFRWGLGNGISIHHGEENHRPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVISLMGPRCTLVFWTYMNGATVGSLQVLIKMGNTISKVWAQSGQQGPQWKKAEVFLGIHSHVEIVFRAKRGVSYIGDVAVDDVSFQNCSPLLSTNRKCTTDEFMCANKHCIEKDKLCDFVNDCADNSDETTFICGTSSGRCDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPAVDHTLGNSSGHYIILKSFFPQQPVKTGRISSPVISKRSKDCKIIFNYHMYGSGIAALLLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSSDEDFRVKFEGRVGEGIRGNIALDDIVLTKSCLPSHHSTREEPAFPLPTGFCPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENECGGSCTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPVGLHGDKAHFKSATWQESSAACTMSFWYFISAKATGSIQILIKTDKGLWEVWQQSKPDPGNHWRRATILLGKLRNFEVIFQGIRTRDLGGGAAIDDIEFNNCTTVGETTDICSEETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHCGYYTSTAGSCNFETTSGDWTVECGLTQDPEDDLDWSIGSIIPTEGLSRDSDHTPGSGRHFLYVNTSLAEEGSTARIITSHFFPASLGICTVRFWFYMVDPHIVGILKVYLIEKSGLNILMWSMMRNKNTGWTYAHVPLSSNSPFKVAFEADLGGKEDIFIALDDITFTPTCASGGPALPQPPLCEEGQFACIYALQCVSASEKCDGQEDCIDGSDEMNCSLGPSPQPCSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSCVNQSCPSGALACNSSGLCIPAHQRCDGTAHCKDIQVDESSCSECPIHYCRNGGTCVIENIGPTCRCVQGWTGNRCHIRSNLSTEGSVHTQNYIWTLLGIGLGFLLTHIAVAILCSLGIRRRPMRKSEGVGNHSFINPVYRNCINQEKTQSSIYSFPNPFYGAASGSLETVSHHLKS | null | null | cholesterol homeostasis [GO:0042632]; negative regulation of bile acid biosynthetic process [GO:0070858] | cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794] | null | PF00057;PF00629; | 2.60.120.200;2.10.25.10;4.10.400.10; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23747249}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Enhances production and/or transport of FGF15 and thus has a role in regulation of bile acid synthesis. {ECO:0000269|PubMed:23747249}. | Mus musculus (Mouse) |
A2AKK5 | ACNT1_MOUSE | MMIKLIATPSNALVDEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAFHRLMKKDVMNSPFCICLDLYDSVNWLETVRIPSKASQRVQRWFVGPGVKREQIQEGRVRGALFLPPGKGPFPGIIDLFGVIGGLVEFRASLLASHGFAVLALAYFAYKDLPEKLQEVDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQVIATVCINGATTTTAVPLRYQDLVVTPIQQALERMEVHVSGAVCFRHTTQYLQNKNILPVEKAQGKILFIVGENDELLDSKLHAQRAMDRLRRHGRSSGRMLAYPGAGHLIEPPYSPLCFASWQPVLGRPMCFGGDLMAHAAAQEHSWREIQKFFRKHLLQSGSKL | 2.3.1.- | null | acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631] | peroxisome [GO:0005777] | fatty acyl-CoA hydrolase activity [GO:0047617]; N-acyltransferase activity [GO:0016410] | PF08840;PF04775; | 2.60.40.2240;3.40.50.1820; | C/M/P thioester hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17116739}. | CATALYTIC ACTIVITY: Reaction=taurine + tetracosanoyl-CoA = CoA + H(+) + N-tetracosanoyl-taurine; Xref=Rhea:RHEA:50120, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:132049, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + taurine = CoA + H(+) + N-eicosanoyl-taurine; Xref=Rhea:RHEA:50116, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:132048, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=octadecanoyl-CoA + taurine = CoA + H(+) + N-octadecanoyl-taurine; Xref=Rhea:RHEA:50112, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:132047, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + taurine = CoA + H(+) + N-hexadecanoyl-taurine; Xref=Rhea:RHEA:50108, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:132045, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=taurine + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoyl-taurine; Xref=Rhea:RHEA:50104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:132043, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + taurine = CoA + H(+) + N-dodecanoyl-taurine; Xref=Rhea:RHEA:50100, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:132042, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for C16:0-coenzyme A {ECO:0000269|PubMed:17116739}; Vmax=159.5 nmol/min/mg enzyme {ECO:0000269|PubMed:17116739}; | null | null | null | FUNCTION: Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine (PubMed:17116739). Shows no conjugation activity in the presence of glycine (PubMed:17116739). {ECO:0000269|PubMed:17116739}. | Mus musculus (Mouse) |
A2AKQ0 | S35D1_MOUSE | MAEVHRRQHAPVKGEAPAKSSTHRDEEELGMAPAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKTLRVVKFPDFDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGALLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYVFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAMEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNISIAGSLVYSYITFTEEQLSKQSEASNKLDTKGKGAV | null | null | chondroitin sulfate biosynthetic process [GO:0030206]; embryonic skeletal system development [GO:0048706]; pyrimidine nucleotide-sugar transmembrane transport [GO:0090481] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794] | antiporter activity [GO:0015297]; GDP-fucose transmembrane transporter activity [GO:0005457]; pyrimidine nucleotide-sugar transmembrane transporter activity [GO:0015165]; UDP-glucuronic acid transmembrane transporter activity [GO:0005461]; UDP-N-acetylgalactosamine transmembrane transporter activity [GO:0005463]; UDP-N-acetylglucosamine transmembrane transporter activity [GO:0005462] | PF03151; | null | TPT transporter family, SLC35D subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17952091}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D-glucosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D-glucosamine(out); Xref=Rhea:RHEA:73703, ChEBI:CHEBI:57705, ChEBI:CHEBI:58052; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73704; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D-galactosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D-galactosamine(out); Xref=Rhea:RHEA:74835, ChEBI:CHEBI:58052, ChEBI:CHEBI:67138; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74836; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N-acetyl-alpha-D-glucosamine(out) + UMP(in); Xref=Rhea:RHEA:72695, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-N-acetyl-alpha-D-galactosamine(in) + UMP(out) = UDP-N-acetyl-alpha-D-galactosamine(out) + UMP(in); Xref=Rhea:RHEA:72735, ChEBI:CHEBI:57865, ChEBI:CHEBI:67138; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucuronate(in) + UMP(out) = UDP-alpha-D-glucuronate(out) + UMP(in); Xref=Rhea:RHEA:72727, ChEBI:CHEBI:57865, ChEBI:CHEBI:58052; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-galactose(in) + UMP(out) = UDP-alpha-D-galactose(out) + UMP(in); Xref=Rhea:RHEA:72703, ChEBI:CHEBI:57865, ChEBI:CHEBI:66914; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose(in) + UMP(out) = UDP-alpha-D-glucose(out) + UMP(in); Xref=Rhea:RHEA:72731, ChEBI:CHEBI:57865, ChEBI:CHEBI:58885; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-xylose(in) + UMP(out) = UDP-alpha-D-xylose(out) + UMP(in); Xref=Rhea:RHEA:72723, ChEBI:CHEBI:57632, ChEBI:CHEBI:57865; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinopyranose(in) + UMP(out) = UDP-beta-L-arabinopyranose(out) + UMP(in); Xref=Rhea:RHEA:74671, ChEBI:CHEBI:57865, ChEBI:CHEBI:61457; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinofuranose(in) + UMP(out) = UDP-beta-L-arabinofuranose(out) + UMP(in); Xref=Rhea:RHEA:74679, ChEBI:CHEBI:57865, ChEBI:CHEBI:61463; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; | null | null | null | null | FUNCTION: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (By similarity). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D-glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (By similarity). May couple UDP-GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (By similarity). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development. {ECO:0000250|UniProtKB:Q9NTN3, ECO:0000269|PubMed:17952091}. | Mus musculus (Mouse) |
A2AKX3 | SETX_MOUSE | MSTCCWCTPGGSSTIDVLKRYASSTGSSEFQTADEDLCYCLECVAEYHRARDEVPFLHEVLWELETLRLVSHFEKSMKAEAEDDDDLYIVDNNGEEQLFDCSGQDFENKLRVPLFEILKYPYLLLHERVNELCVEALCRMEQNNCSFQVFDKYPGIYLFLVHPNEMVRRWAILTARNLGKVDRDDYYDLQEVLTCLFKVIELGLLESPDIYTSSVLEKGKLILLPAHMYDTTNYKNYWLGICMLLTILEEQAMDSLLLGSDKQNDFMQSILHTMEKQSDDDSMDPFWPALHCFMVILDRLGSKVWGQLIDPIEAFQTIINNESYNREIQNIRNSSIRTKLEPEPHFDDMVTCSQIVYNFNPEKTKKDSGWRSAICPDYCPNMYEEMETLANVLQSDIGQDMRVHNSTFLWFIPFVQSLMDLKDLGVAYIVEVIHHLYSEVKDVLNQTDAVCDKVTEFFILILISVIELHRNKKCLHLLWVSSQQWVEAVVKCAKLPTTAFVRSCEKSPGSTSRGAAIMSSLALHSVQSNSVQLACVQLIRGLLKEGYQLGQQTLCKRFWDKLNLFLRGNLSLGWQLTGQETHELQMCLKQIIRNIKFKMPQYSTFGDSTSTFKTPPSFKEESDKIDRKHKKNIYCLENCSPVSSKEPMKADTHRVLMKVNTTEEENFKQHYIDLNEEEQEPLPAELCLKQKSEALFSESAQEQVKISAEKSGKESSSYAPSNSTSRNGPEWGCDRGVIMSAHSLTDSSSDFMEQVSTSNEDVSLKDGSVGKTSKPSFKLQKDEICAKLSHVIKKQIRKSTLVDNIIDLEENTAISDLENCSGTDGGALKEDSIGHNVPSDPVLDDKHEEQKSQNSSLFKKEIKSEELDNSSSDDEDKLQIQEGRADDDLVSFTEVTDTLVKAPCEGHVKMVVESRDKEMRESTALTSNLVEGQVPHDSSKPLVAGRQIDLCNITLISQTTVIQFPSGLSKQNSFQLQKGDKRCLTANQNSAATCRGQVIVISDSDEEEDEDEDERSSSEENIKQSKACIGKDCSEHRSLAVNASVEKQLVKEEERYPVEFEDSESQVFEFESSSEVFSVWQDHKIDSKNSLQGEQKSYVTHVADSTNNNLGCGDSVSEEVVRNKAEGVKEHAGPHSSVSAEEFCKTGVKKPKRKRYDKVTAEDPQRPSSSVGTDQLPDRRDLTESDLKSADMGMATPSSSVERDSTILQKSTKSRTHSKPVRKVPASKATKKTHSDTRRGQSKSSCYISCRTSPAIVPPKKLRQCPEPTSTVEKLGLKKAPRKAFELSQRSLECIVQLRDHGKTVGVVDAPKKAKLISPQTLSIKNNKKLLTSQDLQFQRLMRSRSHKKRDFDYKNTDTVRVSRIVQGSDVLEADSDEPDDHRVSEPLAISNEKQLAKCMLSKTEVAEASSDPWVTGITCLVNQCESRVLSGGVPTDVVMVSASEDPVDGGAVTVQVGEVASVKAAEPASSSDTDDDDNLFLTQHDPQDMDLCSQLENKTIIVAHKKDTVQREDSLSRPQLESLSITKCKYKDCVETTKNQGEYCPRHSEAKAADDGLFRKPGLPLSVARPLRPTTTKIFSSSSASRTANLSKSLESTTLQQSALKNKSSGAQPNLKVTPPSSMGSQKPVAEVKSLCNIFHFQTPSSSSKQSCKLTFSENRPTSAASPVNILLPSQSIFDTFIKEVLKWKYQMFLNFDKCGAPTSLCQSISRPVPVRFQDCAEYFNVFLPLIILNAFETVAQEWLSSPNKENFYQLQLRKFPADYKKYWEFLIYLNESELAKQLHPKENDLVFLAPEKSYMDRHGMQDCSHYYCGYVHKFRRTSVMRSGKAECSLCIQTQDTLPASVKNLTRCIVISSLVTTQRKLKAMSLLSSRNQLARAVLNPNPMDFCTKDLLTTTSERIVAYLKDFNEDQKKAIETAYAMVKHSPSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSDENFNAKIKQNRVLVCAPSNAAVDELMKKIILEFKEKCKDKKNPLGNCGDINLVRLGPEKSINTEVLKFSLDSQVNHRMKKDLPSHIQEMLRRKEILDAQLDELSRQRALCRGGREMQRQELDEHIAIVSKERQELASKIKEVQGRPQRAQNTIILESHVICCTLSTSGGLLLESAFRGQGGVPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLLEENVEQNMIGRLPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCSSEWPFQPYLVFDVGDGSERRDNDSYINVQEIKLVMEIIKLIKEKRKDISFRNIGIITHYKAQKTMIQKDLEKEFDKKGPAEVDTVDAFQGRQKDCIIVTCVRASAVQGSIGFLASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDAQKRGAIIKTSDPNYRHDAMKILKLKPVLQRSLTHPPATAPEAPRPQGGLPSNRLDSGLATTSFAASLYHTPSDTVTSKGPERPLLQDRLRDPRLLRRLDAEAKGTFLKDPQPVSPQLPGVVHLLGEPGFPVVFQDLGFVVPPSTAIVAPLGSHRSPMQAEPPPAHPAAAASTSKRKYSDPDAGLSHKREPRAFSGEQGRHGSVTHHVLRSTDWDRRRLDDSSAKRRQFL | 3.6.4.- | null | cell differentiation [GO:0030154]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; circadian rhythm [GO:0007623]; DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; DNA-templated transcription termination [GO:0006353]; double-strand break repair [GO:0006302]; fibroblast growth factor receptor signaling pathway [GO:0008543]; MAPK cascade [GO:0000165]; mRNA splice site recognition [GO:0006376]; negative regulation of apoptotic process [GO:0043066]; nervous system development [GO:0007399]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of DNA-templated transcription initiation [GO:2000144]; positive regulation of neuron projection development [GO:0010976]; positive regulation of RNA splicing [GO:0033120]; positive regulation of termination of DNA-templated transcription [GO:0060566]; positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled [GO:2000806]; positive regulation of transcription by RNA polymerase II [GO:0045944]; spermatogenesis [GO:0007283]; termination of RNA polymerase II transcription [GO:0006369] | axon [GO:0030424]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; intercellular bridge [GO:0045171]; nuclear body [GO:0016604]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; transcription termination site sequence-specific DNA binding [GO:0001147] | PF13086;PF13087; | 3.40.50.300; | DNA2/NAM7 helicase family | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q7Z333}.; PTM: Sumoylated preferentially with SUMO2 or SUMO3. {ECO:0000250|UniProtKB:Q7Z333}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z333}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16644229}. Nucleus, nucleolus {ECO:0000269|PubMed:16644229}. Cytoplasm {ECO:0000269|PubMed:16644229}. Chromosome {ECO:0000269|PubMed:23593030}. Chromosome, telomere {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, axon {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7Z333}. Note=Most abundant in the nucleus (By similarity). Detected in granules (By similarity). Colocalized in cycling cells with FBL in the nucleolus. Localizes with telomeric DNA in a transcription-dependent manner. Under replication stress, colocalizes with a variety of DNA damage signaling and repair response proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells in a transcription- and RNA/DNA hybrid-dependent manner. Localizes at limited number of nuclear foci. Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity). At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (PubMed:23593030). May be detected in the nucleolus only in cycling cells (PubMed:16644229). {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:16644229, ECO:0000269|PubMed:23593030}. | null | null | null | null | null | FUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription. Contributes to the mRNA splicing efficiency and splice site selection. Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (By similarity). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (PubMed:22767893). Involved in DNA double-strand breaks damage response generated by oxidative stress. In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (By similarity). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (PubMed:23593030). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis. May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (By similarity). {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23593030}. | Mus musculus (Mouse) |
A2AL36 | CNTRL_MOUSE | MKKGSERRLSKAKMPLSSHFPGPSSLRSSMRSRSLSPLIGSETQPLHPGGQWPAQAELTDESTVPLEPQQRKGAESYVGVRYITEALIKKLTKQDNLALVKSLNLSLSKDGGKKFRYIENLEKCVKLEVLNLSYNLIVKIEKVDKLLRLRELNLSYNKISKIEGLENMCNLQKLNLAGNEIEHIPVWFAKKLKSLRVLNLKGNKISSLQDVSKLKPLQDLTSLVLIDNPVVALPHYLQFIIFHLRSLESLEGQPVTTQDRQEAFERFSLEEIERLEKDLEKKTVETEELKNKQTKFLEEIKNQDKLNKSLKEEAMLQKQSCEELESDLSTKKELLKQKTVELTRACQKQYELEQELAFYKIDAKFEPLNYYPSEYAEIDKYPDESPYIGKSRYKRNMFATETYIVSDAQAVQIRKMVPEGGQLRHEHTPPRVQAPPDLQLEDTEKKISAAQTRLSELHHEIETAEQKVLRATQEFKQLEEAIQQKKISEAEKDLLLKQLSGRLQHLNRLRQEALDLEIQMEKQRKEIAEKHEEINTVQLATDSLDPKDPKHSHMKAQKRGKEQQLDIMNRQYTQLESRLDEILCRIAKETEEIKDLEQQLTDGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLQDEKETLLQRLTEVQQEKEELELIAMDAENMRKELAELESALQEQHEVNASLQQAQGDLSAYETELETQLKLKDAETSQLKQELEKLLRRTQLEQSVLQTELEKERESLRDALGKAQSSEEKQQENNELRTQLKQLQDDNSLLKKQLKEFQNHLNHVVDGLIHPEEVAARVDELRKRLKLGAGEMRIHSPSDVLGKSLADLQKQFSEILARSQWEKEEAQVRERKLHEEMALQQEKLANGQEEFRQACERALEARIKFDKRQHNARIQQLENEIHYLQENLKSMEKIQGLTDLQLQEADEEKERILAQLQELEKKKKREDARSQEQFLGLDEELKSLKKAVAASDKLAAAELTIAKDQLKSLHGTVVRINQERAEELQEAERFSREAMQAAKDLSRAEAEIELLQHLLREREGQFRDEMENADLGAKGANSQLLEIEALNEAMAKQRAEITRLRDVLNLTGAGTKGGIENVLEEIAELRHAVSAQNEYISSMADPFRRQGWWYFMPPAPSSKVSSHSSQATKDSGLGLKYTASTPLRKPQPGQQEEKDSSGPLPASGYWVYSPIRSTLHKSFSKREDADSGGDSQEESGLDDQEEPPFVPPPGYIMYTVLPDGSPVPQGVALYAPSPPLPNSSHPLTPGTVVYGPPPAGAPIIYGPPPANFAVPLVPAGVQHCNIPEHHNLENEVSRLEDIMQHLKSKQREERRQKASTQHSEEEVDGLHRDIDDLLQEKKELELEVEELHRTIERHQQRKDFIDGHVENLMTELEIEKSLKHHEDIVDEIECLEKTLLKRRSELREADRLLAEAENELACTKEKTKSAVEKFTDAKRNLLQTESDAEALEKRAQETALNLVKAEQQLRLLQADAEDLEQHKIKQEEILKEINKVVAAKDADFQCLNEKKEKLTEELQSLQRDIKAAQHSEDHHLQVLRESETLLQAKRAELETLKSQVTSQQQELAVLDSELGHRREELLLLQDSLAQAKADLQEALTLGETEVAEKCSHIREVKSLLEELSFQKGELNVHISEKKTQLALIQQEMEKEEKNLQVVLQQLSRHKTELKNVADILQLETSELQGLKLQHDQKVVELEKAQVDVLEEKLELENLQQATQQQRRELERQRQLLERDRRETERVRAESQALQSCVECLSKEKEDLQGQCESWEKKSSHAQRVLAATEESNKMEQSNLGKLELSVRKLRQELEQLSQDKLALHSEVAEVQQQLQGKQEAINSLQEELDSTQDHLDLAKQDLIHTTKCQNELLNEQTQLQEDISKWMARLESCQKETETKEQQVQQLQDEIRESKLRLDQQEMMFQKLQKEREREEQKFEAGKVTLEQQQRQLEKELTDQKSRLKQLLTDVSAAEGRLGTLQEEERRIEGLERMLSQAKQQLSEREQQLMAKSGELLALQKEADDMRADFSLLRNQFLTERKKAEKQVAGLKEALKIQRSQLEKNLLEQKQENSCMQKEMATIELVAQDNHERARRLMKELSQMQQEYLELKKQVANQKDLERRQMEVSDAMRTLKSEVKDEIRTSLRNLNQFLPELPADLASILERNENLRELESLKENFPFTTKERIFEEKSNFPQVHIMDEHWRGEALRQRLRRHEDQLKAQLRHCMSKQAEVLIKGKQQTEGTLHSLRRQVDALGELVTSTSTDSASSPSLPSLVEDSQHGHSQSSFQVLQVPLEEPNSYRH | null | null | aorta development [GO:0035904]; axoneme assembly [GO:0035082]; cardiac septum development [GO:0003279]; cell cycle [GO:0007049]; coronary vasculature development [GO:0060976]; female germ-line stem cell asymmetric division [GO:0048132]; kidney development [GO:0001822]; ventricular septum development [GO:0003281] | axoneme [GO:0005930]; centriolar satellite [GO:0034451]; centriolar subdistal appendage [GO:0120103]; centrosome [GO:0005813]; cytosol [GO:0005829]; Flemming body [GO:0090543]; meiotic spindle [GO:0072687]; meiotic spindle pole [GO:0090619]; mitotic spindle pole [GO:0097431]; perinuclear region of cytoplasm [GO:0048471] | dynein complex binding [GO:0070840] | PF14580; | 3.80.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q7Z7A1}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q7Z7A1}. | null | null | null | null | null | FUNCTION: Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2ALS5 | RPGP1_MOUSE | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSLPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTHHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDDDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFTPNNPDLAKAAGISLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRVESAAQRTEVLQGFSRSSSSASSFTSVVEETEGVDGDDTGLESVSSSGTPHKRDSFLYSTWLDDSVSTTSGGSSPGLTRSPHPDVGKSGDPACPEIKIQLETSEQHTPQMGC | null | null | cell-cell adhesion [GO:0098609]; cellular response to glial cell derived neurotrophic factor [GO:1990792]; establishment of localization in cell [GO:0051649]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of thyroid gland epithelial cell proliferation [GO:1904442]; phagocytosis [GO:0006909]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of phagocytosis [GO:0050766]; regulation of small GTPase mediated signal transduction [GO:0051056] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; neuronal cell body [GO:0043025] | GTPase activator activity [GO:0005096] | PF02188;PF21022;PF02145; | 6.10.140.210;3.40.50.11210; | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000250}. | Mus musculus (Mouse) |
A2ALU4 | SHRM2_MOUSE | MEGAEPRARPERLAEAEAPATDGVRLVEVQLSGGAPWGFTLKGGREHGEPLVITKIEEGSKAAAVDKLLAGDEIVAINDVSLSGFRQEAICLVKGSHKTLKLVVKRKSDPSWRPHSWHATKYFDVHPEPAASLFLNTSGSPSWKSQHQASSSSHDLSGSWEHTSLQRTSDHFSSMGSIDSLDHSSQLYPSGHLSSAKSNSSIDHLGGHSKRDSAYGSFSTCSSTPDHTLPKADASSTENILYKVGLWEASRPGSSRQSQSTGDPQGLQDRPSCFIPRVPGNSSKSPRPEDNVEPKIATHGRSNFGPVWYVPDKKKAPSPPPLGLPLRSDSFSVAARGHEKARGPPFSDLASMQHFITLPHVQPRGDHRMETTDRQWKLTHLSSGKEIGNVGYQSEGHLDCRWLCSDDRAGRPSGPPGRLQFSDVHFLKSYHGSQHQQQCSDESPRAPSSPRELLHITPGGGLQEPPEPSQDDNPTQVRWPGSAHQKLDDRGRSHYFPGSLRQPVQGSAQVVIPRGDYWHSDTTPVDLEYPLLRPVGQRTYLQQHEETPASHEKEGYHQLNAGIEGCCSGIQEPPRASRTVRTGLQCPSNDFKLVDGESGRISRQRTPMLHSLTQDGTWRPGNSKDCGNDKPPLFDAQVGKPTRRSDRFATTLRNEIQMRRAKLQKSKSTVTLAGDSEAEDCAGDWRADVGAVPEGSFPSTYKEHLKEAQTRVLKATSFQRRDLDPTPADQYSGPSEHRTFDHSASSSLSSFPGEPDSAPRFCETGLAKAPSSGVGVPHVLRIGGRKRFTAEQKLKSYSEPEKINEVGLSGDHRPHPTVRTPEDTVGTFADRWKFFEETSKSLLQKAGHRQVHCGLPREKAERPQTGHHECESTEPWFQKRSLATSCGEILSDRKVEKASEKLNPPRRLGTFAEYQASWKEQKKPLEARSSGRYHSADDILDAGLDQQQRPQYIHERSRSSPSTDHYSQEVPVEPNRQAEDSGDHKEAILCTLQAEEGCSAPSAQPQDSQHVNEDTTFPQPETQLSSKCQHLQTSAMETSRSPSPQFAPQKLTDKPPLLIHEDNSARIERVMDNNTTVKMVPIKIVHSESQPEKESRQSLACPAELPPLPSGLERDQIKTLSTSEQCYSRFCVYTRQEVEAPHRARPPEPRPPSTPAPPVRDSCSSPPSLNYGKAKEKTMDDLKSEELAREIVGKDKSLADILDPSVKIKTTMDLMEGIFPKDEYLLEEAQQRRKLLPKVPLPRVTEDKKQDPGMPGVVSLATNSTYYSTSAPKAELLIKMKDLQEPEEYSAGDLDHDLSVKKQELIDSISRKLQVLREARESLLEDIQANNALGDEVEAIVKDVCKPNEFDKFRMFIGDLDKVVNLLLSLSGRLARVENALNNLDDNPSPGDRQSLLEKQRVLTQQHEDAKELKENLDRRERIVFDILATYLSEENLADYEHFVKMKSALIIEQRELEDKIHLGEEQLKCLFDSLQPERSK | null | null | actin filament organization [GO:0007015]; apical protein localization [GO:0045176]; brain development [GO:0007420]; camera-type eye development [GO:0043010]; camera-type eye morphogenesis [GO:0048593]; cell migration [GO:0016477]; cell-cell junction maintenance [GO:0045217]; cellular pigment accumulation [GO:0043482]; ear development [GO:0043583]; establishment of melanosome localization [GO:0032401]; eye pigment granule organization [GO:0008057]; lens morphogenesis in camera-type eye [GO:0002089]; melanosome organization [GO:0032438]; negative regulation of actin filament depolymerization [GO:0030835] | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell cortex [GO:0005938]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; beta-catenin binding [GO:0008013]; protein domain specific binding [GO:0019904] | PF08688;PF08687;PF00595; | 2.30.42.10;6.10.250.3120; | Shroom family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16684770}. Cell junction, tight junction {ECO:0000269|PubMed:16684770}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770}. Note=Associates with cortical F-actin. | null | null | null | null | null | FUNCTION: May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution. {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:16987870}. | Mus musculus (Mouse) |
A2ALV5 | SHOC1_MOUSE | MALNGRTMFPAFKYYAIDYLQEDIIKERLYRDALLLQIPSCLNQDKNIIDDKYRTPWTRAIPVQEMEDNSVLEQWRTRFCVEGVPEKKTVTGVMINGTFEEIVPSSNPNSPPGIENDKLFPSKDYVDDFIPVKCSLYYPGVKAEHQGLLIDEEMIFMNKAMDNHLPTVNGLLSRLKLYLVKDPFLDFKEELSGKDNFTEYFSVQECSEPFVRDFHMAEETFCKKKLPSVFPSGFKSLISTNPKQEILILPPSKLKKPLNSIPKIMDSVDESECFKGDITSKHEFDTEDIKCNSTENLTFASLCEPECSEPGDLEMPPTHLILPRQHSAVSSLHMGFQTFPFSATCKINLLSAGESANKYCMLWQLGGCRNSWVSFLLTVPRFQEPSSQYSLADMRNIFSVKGDSLVINPAKAKGWRQARLHPIMAETLAHLKAYLCHNGLSSQETKLEIFLPTKVFQLESWLELKSRPLPIVPISEKSTDVHQLHPQKRPIPSSEKEVPHLCLSGESISVKKSKVEANPKNDQEPEARIMQKPENSCVGLGCSSQVPSAESASSSQIQASYDKKQDDLDLLSEFIILRSKHQTFPSEADVDVKSHDHDQNNEFQDKEKYSLTLQEESLVASNSKAPEERCEERTDGVIEIPASDTQCQAYCLLEATANPILKELVCLCTYPAANWKFATVNFDQTRFFLKEQEKKINDATHPDKNDDRKMTFRHAALLHLLITIRDVLLTCNLDTALGYLSNAKDIYKSVLDSRLDNIWRQLKILQFIKEKRPKSNYKIQELQCQILSRLQNQQQMKVLIIIRMDSDGEKHLLIKTLKKIEGLTMTVLRSNDRKKILETTSILKGTNACVVVHNHSIGADFPWSSFSLVVEYNHVGHSCWAEHCQLLDIPFLAFKVAVPDTALQRDALLDGFGGFLLKIPIPYVFFASEGLLNTPEILRLLESNYNITLVERCCCGSLKLFGSTECYVVVTVDEHTAIVVQDLEELHHEKASDNIIMRLMALSFQYSCCWIILYSKETLNSQYHLTEETLRHLAQVYAALVSSGLKSEELDVKLIIAPGVEETALIIRQIADHNLMTSTRDPHEWLDKSWVEVSPSKEEMSLLDFPCINPLVAQLMLHRAPSLHWLLIATPAELQELLPQVPGKVLKHFCSITSLFKISSPSMTKSSQISSLQEDMNQTDLFISQSSAPIIQEQEEYYPYEDSEGTSSSPVELRATPCMLPSAAPHSQRGCWEDPSCGPDPVQNNPSLMNAESKKVTWPSVPSWSDSESDVFSLARTQVSCEPIMTLTDSQRRGTNGFVNCPEAKGPRNMQVSTPVFLPENSQSHLHWDFKKNSCRKQIYSFNPSCGTEQTTYNKWYSWKDDFSSNQPECLWDEMEDVTYRNANAGTRETFWRELPAVPSWDSPCASDSNANQRGFKGLDFCQRAGNYLGQRSLPVSSSNWGDYKTPTDLMYSQVPQPKKRRLMYEKVPGRVDGQTRLKFL | 3.6.-.- | null | reciprocal meiotic recombination [GO:0007131]; resolution of meiotic recombination intermediates [GO:0000712]; synaptonemal complex assembly [GO:0007130] | chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794] | ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697] | PF17825; | null | XPF family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. Note=Localizes to meiotic chromosomes; associates with mid-stage meiotic recombination intermediates (PubMed:29742103). Localization requires meiotic double-strand breaks (DSBs) recombination intermediates catalyzed by DMC1 (PubMed:29742103). {ECO:0000269|PubMed:29742103}. | null | null | null | null | null | FUNCTION: ATPase required during meiosis for the formation of crossover recombination intermediates (PubMed:29742103). Binds DNA: preferentially binds to single-stranded DNA and DNA branched structures (By similarity). Does not show nuclease activity in vitro, but shows ATPase activity, which is stimulated by the presence of single-stranded DNA (By similarity). Plays a key role in homologous recombination and crossing-over in meiotic prophase I in male and female germ cells (PubMed:30272023). Required for proper synaptonemal complex assembly and homologous chromosome pairing (PubMed:35485979). Required for recruitment of TEX11 and MSH4 to recombination intermediates (PubMed:30272023). {ECO:0000250|UniProtKB:Q5VXU9, ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:35485979}. | Mus musculus (Mouse) |
A2AM29 | AF9_MOUSE | MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPKKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKDSSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKADSNLLTVTSGQQDKKAPSKRPPASDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSMLPPFDDIVDPNDSDVEENMSSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEAEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS | null | null | anterior/posterior pattern specification [GO:0009952]; gene expression [GO:0010467]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; regulation of chromatin organization [GO:1902275]; regulation of stem cell division [GO:2000035]; segment specification [GO:0007379] | chromosome [GO:0005694]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription elongation factor complex [GO:0008023] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; modification-dependent protein binding [GO:0140030] | PF17793;PF03366; | 1.20.1270.290;2.60.40.1970; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:11439343}. Chromosome {ECO:0000250|UniProtKB:P42568}. Note=Colocalizes with acylated histone H3. H3 Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr). {ECO:0000250|UniProtKB:P42568}. | null | null | null | null | null | FUNCTION: Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr). Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3. In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones. Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me). Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than conferring, HSC stemness. Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L. {ECO:0000250|UniProtKB:P42568}. | Mus musculus (Mouse) |
A2AMM0 | CAVN4_MOUSE | MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVASVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDIPCPASLSVVKDRSLPENQEEAEEVFDPPIELSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSRENMQKTRQTLDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISSAAPSKEAFKIRSLRKAKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDEFSETEKEVTKGGYSPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS | null | null | cardiac myofibril assembly [GO:0055003]; muscle organ development [GO:0007517]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; Rho protein signal transduction [GO:0007266] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | GTPase activator activity [GO:0005096] | PF15237; | null | CAVIN family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18332105}. Cytoplasm {ECO:0000269|PubMed:18332105}. Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:24567387}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19546242}. Cell membrane {ECO:0000269|PubMed:26497963}. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm (PubMed:18332105). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}. | null | null | null | null | null | FUNCTION: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation (PubMed:24567387). Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes (PubMed:26497963). Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway (PubMed:18332105). {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:26497963}. | Mus musculus (Mouse) |
A2AMT1 | BFSP1_MOUSE | MYRRSYVFQARQERYERAQPAGPAAQPGGTAPGLAALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQPGPEDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSRLSSVFIETPISLITPSHGAPLSLGSSVKDLARAVQDITAAKPRQKALPKSLPKRKEIIAQDKVEETLEDAPLKPPQEPKALQVERKAEGGSQPGAGGGHGVSPTQEGGPEDVPDGGQISKAFGKLCKVVKERVSGHKEPEPEPPTDLFTKGRHVLVTGESSFVDPEFYSSSIPARGGVVISIEEDSMHHDGHVEPSPGQPMPPVENGQGVPQGREGDHSNHQQGTDKNGLRAKEPKDLEEKDDDGKKEAEGSRRPCPVIIPGPDEPSTSHSQTSGSNQGGPVGPASKSSSLLAKGPSKALSIKKVEVVESIEKISTESIQTYEETSVIVETLIGKSKGNKKLGEKSLPDTRA | null | null | cell maturation [GO:0048469]; intermediate filament organization [GO:0045109]; lens fiber cell development [GO:0070307] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | structural constituent of eye lens [GO:0005212] | PF00038; | 1.20.5.170;1.20.5.1160; | Intermediate filament family | PTM: Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases. {ECO:0000250|UniProtKB:Q06002}.; PTM: [Filensin C-terminal fragment]: Myristoylated at Gly-432 following proteolytic cleavage at Asp-431. {ECO:0000250|UniProtKB:Q06002}.; PTM: [Filensin N-terminal fragment]: Acetylated at Ala-35 following proteolytic cleavage at Leu-34. {ECO:0000250|UniProtKB:Q06002}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19029034}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm {ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q06002}. | null | null | null | null | null | FUNCTION: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:27559293). Involved in altering the calcium regulation of MIP water permeability (By similarity). {ECO:0000250|UniProtKB:Q12934, ECO:0000269|PubMed:27559293}. | Mus musculus (Mouse) |
A2AN08 | UBR4_MOUSE | MATSGGEEAAAAAPAPGAPATGQDTTPGWEVAVRPLLSASYSAFEMKELPQLVASVIESESEILHHEKQYEPFYSSFVALSTHYITTVCSLIPRNQLQSVAAACKVLIEFSLLRLENPDEACAVSQKHLILLIKGLCTGCSRLDRTEIITFTAMMKSAKLPQTVKTLSDVEDQKELASPVSPELRQKEVQMNFLNQLTSVFNPRTVPSPPISPQALVEGENDEQSSPDQVSAAKTKSVFIAQNVASLQELGGSEKLLRVCLNLPYFLRYINRFQDAVVANSFFIMPATVADATAVRNGFHSLVIDVTMALDTLSLPVLEPLNPSRLQDVTVLSLSCLYAGVSVATCMAILHVGSAQQVRTGSTSSKEDDYESDAATIVQKCLEIYDMIGQAISSSRRAGGEHFQNFQLLGAWCLLNSLFLILNLSPTALADKGKEKDPLAALRVRDILSRTKEGVGSPKLGPGKGHQGFGVLSVILANHAIKLLASLFQDLQVEALHKGWETDGPPAVLSIMAQSTSTQRIQRLIDSVPLTNLLLTLLSTSYRKACVLQRQRKGSMSSDASASTDSNTYYEDDFSSTEEDSSQDDDSEPILGQWFEETISPSKEKAAPPPPPPPPPLESSPRVKSPNKQASGEKGNILASRKDPELFSGLASNILNFITTSMLNSRNSFIRSYLSASLSEHHMATLASIIKEVDKDGLKGSSDEDFAAALYHFNHSLVTSDLQSPNLQNTLLQQLGVAPFSEGPWPLYIHPQGLSVLSRLLLIWQHKAGAQGDPDVPECLKVWDRFLTTMKQNALQGVVPSETEDLNVEHLQLLLLIFHSFSEKGRRAILTMLVQSIQELSVNMEVQMRTAPLILARLLLIFDYLLHQYSKAPVYLFEQVQHNLLSPPFGWASGSQDSSSRRANTPLYHGFKEVEENWSKHFSSDAAPQPRFYCVLSTEASEEDLNRLDSEACEVLFSKPVKYDELYSSLTTLLAAGSQLDTTRRKEKKNVTALEACALQYYFLILWRILGILPPSKTYMNQLAMNSPEMSECDILHTLRWSSRLRISSYVSWIKDHLIKQGMKPEHAGSLIELAASKCSSVKYDVEIVEEYFARQISSFCSIDCTAVLQLHEIPSLQSIYTLDAAVSKVQVSLDEHFSKMAAETDPHKSSEITKNLLPATLQLIDTYASFTRAYLLQNLNEEGSTEKPSQEKLHGFAAVLAIGSSRCKANTLGPTLVQNLPSSVQSVCESWNNINTNEFPNIGSWRNAFANDTIPSESYISAVQAAHLGTLCGQSLPLAASLKHTLLSLVRLTGDLIVWSDEMNPAQVIRTLLPLLLESSTESAAEISSNSLERILGPAESDEFLARVYEKLITGCYNILANHADPNSGLDESILEECLQYLEKQLESSQARKAMEEFFSDGGELVQIMMATANEDLSAKFCNRVLKFFTKLFQLTEKSPNPSLLHLCGSLAQLACVEPVRLQAWLTRMTTSPPKDSDQLEVIQENRQLLQLLTTYIVRENSQVGEGVCAVLLGTLTPMATDMLANGDGTGFPELMVVMATLASAGQGAGHLQLHNAAVDWLGRCKKYLSQKNVVEKLNANVMHGKHVMVLECTCHIMSYLADVTNALSQSNGQGPSHLSVDGEERAIEVDSDWVEELAVEEEDSQAEDSDEDSLCNKLCTFTITQKEFMNQHWYHCHTCKMVDGVGVCTVCAKVCHKDHEISYAKYGSFFCDCGAKEDGSCLALVKRTPSSGMSSTMKESAFQSEPRVSESLVRHASTSPADKAKVTISDGKVTDEEKPKKSSLCRTVEGCREELQNQANFSFAPLVLDMLSFLMDAIQTNFQQASAVGSSSRAQQALSELHTVDKGVEMTDQLMVPTLGSQEGAFENVRMNYSGDQGQTIRQLISAHVLRRVAMCVLSSPHGRRQHLAVSHEKGKITVLQLSALLKQADSSKRKLTLTRLASAPVPFTVLSLTGNPCKEDYLAVCGLKDCHVLTFSSSGSVSDHLVLHPQLATGNFIIKAVWLPGSQTELAIVTADFVKIYDLSIDALSPTFYFLLPSSKIRDVTFLFNEEGKNIIVIMSSAGYMYTQLMEEASSAQQGPFYVTNVLEINHEDLKDSNSQVAGGGVSVYYSHVLQMLFFSYSQGRSFAATVSRSTLEVLQLFPINIKSSNGGSKTSPALCQWSEVMNHPGLVCCVQQTTGVPLVVMVKPGTFLIQEIKTLPAKAKIQDMVAIRHTACNEQQRTTMILLCEDGSLRIYMANVENTSYWLQPSLQPSSVISIMKPVRKRKTATITARTSSQVTFPIDFFEHNQQLTDVEFGGNDLLQVYNAQQIKHRLNSTGMYVANTKPGGFTIEISNNSSTMVMTGMRIQIGTQAIERAPSYIEIFGRTMQLNLSRSRWFDFPFTREEALQADRKLSLFIGASVDPAGVTMIDAVKIYGKTKEQFGWPDEPPEDFPSASVSNICPPNLNQSNGTGESDSAAPATTSGTVLERLVVSSLEALESCFAVGPIIEKERNKHAAQELATLLLSLPAPASVQQQSKSLLASLHSSRSAYHSHKDQALLSKAVQCLNTSSKEGKDLDPEVFQRLVITARSIAVTRPNNLVHFTESKLPQMETEGADEGKEPQKQEGDGCSFITQLVNHFWKLHASKPKNAFLAPACLPGLTHIEATVNALVDIIHGYCTCELDCINTASKIYMQMLLCPDPAVSFSCKQALIRVLRPRNKRRHVTLPSSPRSNTPMGDKDDDDDDDADEKMQSSGIPDGGHIRQESQEQSEVDHGDFEMVSESMVLETAENVNNGNPSPLEALLAGAEGFPPMLDIPPDADDETMVELAIALSLQQDQQGSSSSALGLQSLGLSGQAPSSSSLDAGTLSDTTASAPASDDEGSTAATDGSTLRTSPADHGGSVGSESGGSAVDSVAGEHSVSGRSSAYGDATAEGHPAGPGSVSSSTGAISTATGHQEGDGSEGEGEGEAEGDVHTSNRLHMVRLMLLERLLQTLPQLRNVGGVRAIPYMQVILMLTTDLDGEDEKDKGALDNLLAQLIAELGMDKKDVSKKNERSALNEVHLVVMRLLSVFMSRTKSGSKSSICESSSLISSATAAALLSSGAVDYCLHVLKSLLEYWKSQQSDEEPVAASQLLKPHTTSSPPDMSPFFLRQYVKGHAADVFEAYTQLLTEMVLRLPYQIKKIADTSSRIPPPVFDHSWFYFLSEYLMIQQTPFVRRQVRKLLLFICGSKEKYRQLRDLHTLDSHVRGIKKLLEEQGIFLRASVVTASSGSALQYDTLISLMEHLKACAEIAAQRTINWQKFCIKDDSVLYFLLQVSFLVDEGVSPVLLQLLSCALCGSKVLAALAASTGSSSVASSSAPPAASSGQATTQSKSSTKKSKKEEKEKEKEGESSGSQEDQLCTALVNQLNRFADKETLIQFLRCFLLESNSSSVRWQAHCLTLHIYRNSNKAQQELLLDLMWSIWPELPAYGRKAAQFVDLLGYFSLKTAQTEKKLKEYSQKAVEILRTQNHILTNHPNSNIYNTLSGLVEFDGYYLESDPCLVCNNPEVPFCYIKLSSIKVDTRYTTTQQVVKLIGSHTISKVTVKIGDLKRTKMVRTINLYYNNRTVQAIVELKNKPARWHKAKKVQLTPGQTEVKIDLPLPIVASNLMIEFADFYENYQASTETLQCPRCSASVPANPGVCGNCGENVYQCHKCRSINYDEKDPFLCNACGFCKYARFDFMLYAKPCCAVDPIENEEDRKKAVSNINTLLDKADRVYHQLMGHRPQLENLLCKVNEAAPEKPQEDSGTAGGISSTSASVNRYILQLAQEYCGDCKNSFDELSKIIQKVFASRKELLEYDLQQREAATKSSRTSVQPTFTASQYRALSVLGCGHTSSTKCYGCASAVTEHCITLLRALATNPALRHILVSQGLIRELFDYNLRRGAAAIREEVRQLMCLLTRDNPEATQQMNDLIIGKVSTALKGHWANPDLASSLQYEMLLLTDSISKEDSCWELRLRCALSLFLMAVNIKTPVVVENITLMCLRILQKLIKPPAPTSKKNKDVPVEALTTVKPYCNEIHAQAQLWLKRDPKASYEAWKKCLPIRGVDGNGKSPSKSELHRLYLTEKYVWRWKQFLSRRGKRTTPLDLKLGHNNWLRQVLFTPATQAARQAACTIVEALATVPSRKQQVLDLLTSYLDELSVAGECAAEYLALYQKLIASCHWKVYLAARGVLPYVGNLITKEIARLLALEEATLSTDLQQGYALKSLTGLLSSFVEVESIKRHFKSRLVGTVLNGYLCLRKLVLQRTKLIDETQDMLLEMLEDMTTGTESETKAFMAVCIETAKRYNLDDYRTPVFIFERLCSIIYPEENEVTEFFVTLEKDPQQEDFLQGRMPGNPYSSNEPGIGPLMRDIKNKICQDCDLVALLEDDSGMELLVNNKIISLDLPVAEVYKKVWCATNEGEPMRIVYRMRGLLGDATEEFIESLDSTTDEEEDEEEVYRMAGVMAQCGGLQCMLNRLAGVKDFKQGRHLLTVLLKLFSYCVKVKVNRQQLVKLETNTLNVMLGTLNLALVAEQESKDSGGAAVAEQVLSIMEIILDESNAEPLSEDKGNLLLTGDKDQLVMLLDQINSTFVRSNPSVLQGLLRIIPYLSFGEVEKMQILVERFKPYCSFEKYDEDHSGDDKVFLDCFCKIAAGIKNNSNGHQLKDLILQKGITQNALDYMKKHIPSAKNLDADIWKKFLSRPALPFILRLLRGLAMQHPATQVLIGTDSITSLHKLEQVSSDEGIGTLAENLLEALREHPDVNKKIDAARRETRAEKKRMAMAMRQKALGTLGMTTNEKGQVVTKTALLKQMEELIEEPGLTCCICREGYKFQPTKVLGIYTFTKRVALEEMENKPRKQQGYSTVSHFNIVHYDCHLAAVRLARGREEWESAALQNANTKCNGLLPVWGPHVPESAFATCLARHNTYLQECTGQREPTYQLNIHDIKLLFLRFAMEQSFSADTGGGGRESNIHLIPYIIHTVLYVLNTTRATSREEKNLQGFLEQPKEKWTESAFDVDGPHYFTILALHVLPPEQWKAIRVEILRRLLVASHARAVAPGGATRLTDKAVKDYSAYRSSLLFWALVDLIYNMFKKVPTSNTEGGWSCSLAEYIRHNDMPIYEAADKALKTFQEEFMPVETFSEFLDAAGLLSEITDPESFLKDLLNSVP | 2.3.2.27 | null | negative regulation of fatty acid biosynthetic process [GO:0045717]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | calmodulin binding [GO:0005516]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF13764;PF19423;PF02207; | null | UBR4 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrates at the leading edge of membrane structures involved in actin motility. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradation. {ECO:0000269|PubMed:16055722}. | Mus musculus (Mouse) |
A2ANU3 | SYNG1_MOUSE | MDGIIEQKSVLVHSKISDAGKRNGLINTRNFMAESRDGLVSVYPAPQYQSHRLVASAAPGSLEGGRSEPVQQLLDPNTLQQSVESHYRPNIILYSDGVLRSWGDGVATDCCETTFIEDRSPTKDSLEYPDGKFIDLSGDDIKIHTLSYDVEEEEELQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASTSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL | null | null | intracellular protein transport [GO:0006886]; positive regulation of synapse assembly [GO:0051965]; synaptic vesicle clustering [GO:0097091] | cell body [GO:0044297]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; early endosome membrane [GO:0031901]; excitatory synapse [GO:0060076]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; synaptic vesicle membrane [GO:0030672] | glutamate receptor binding [GO:0035254]; protein homodimerization activity [GO:0042803] | PF04505; | null | CD225/Dispanin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Early endosome membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Postsynaptic density membrane {ECO:0000269|PubMed:20152115}. Synapse {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Shuttles between the cell surface and early endosome membrane. | null | null | null | null | null | FUNCTION: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation. {ECO:0000250}. | Mus musculus (Mouse) |
A2AP18 | PLCH2_MOUSE | MGGLAWGPSRAAGSSWVNASGTWEQPLRGFSGLQGGRRRGRGEKGIPEEPLCQLTPQLGLSLRVPFGLGDYGLDMPGPQPSAASQTTGAVACLAEVLLWVGGSVVVSPRWQLSLVVERCMSAMQEGTQMVKLRGSSKGLVRFYYLDEHRSCLRWRPSRKNEKAKISIDSIQEVSEGRQSEIFQRYPDSSFDPNCCFSIYHGSHRESLDLVSPSSEEARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSISEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDASDLQRFLEVEQKMNGVTLESCQNIIEQFEPCLENKSKGMLGIDGFTNYTRSPAGDIFNPEHNRVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIENHCSVVQQKKMAQYLTDILGDKLDLSSVSSEDATMLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEMEDDCKLLNGDASTNRKRVENIAKKKLDSLIKESKIRDCEDPNDFSVSTLSPSGKLGRKAEAKKGQSKVEEDVEAGEDSGVSRQNSRLFMSSFSKRKKKGSKIKKVASVEEGDETLDSPGSQSRGTARQKKTMKLSRALSDLVKYTKSVGTHDVEIEVVSSWQVSSFSETKAHQILQQKPTQYLRFNQHQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGDCGYVLKPQCMCQGVFNPNSEDPLPGQLKKQLALRIISGQQLPKPRDSVLGDRGEIIDPFVEVEVIGLPVDCSKEQTRVVDDNGFNPMWEETLVFTVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSIMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQTLGLKGLFLRGTKPGSLDSHAAGQPLPRPSVSQRLLRRTASAPTKSQKPSRKGFPELALGTQDAGSEGAADDVAPSSPNPALEAPTQERSGSSSPRDTRLFPLQRPISPLCSLEPIAEEPALGPGLPLQAAAPTGPSQEGSQCPVGLGAKVTSSQQTSLGAFGTLQLRIGGGRENEEPPLRPHNGGISSGPREGTSGRQTDSKSRSRVPGHLPVVRRAKSEGQVLSELSPTPAVYSDATGTDRLWQRLEPGSHRDSVSSSSSMSSNDTVIDLSLPSLGLCRSRESIPGVSLGRLTSRPCLASAARPDLPPVTKSKSNPNLRVAGGLPTAPDELQPRPLAPRLTGHHPRPPWHHLTLVGLRDCPVSAKSKSLGDLTADDFAPSFQGSTSSLSCGLGSLGVAHQVLEPGIRRDALTEQLRWLTGFQQAGDITSPTSLGPAGDGSVGGPSFLRRSSSRSQSRVRAIASRARQAQERQQRLRGQDSRGPPEEERGTPEGACSVGHEGCVDVPMPAKGAPEQVCGAADGQLLLRL | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; release of sequestered calcium ion into cytosol [GO:0051209] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629] | PF00168;PF09279;PF16457;PF00388;PF00387; | 2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899900}. Cell membrane {ECO:0000269|PubMed:15899900}. Note=Localized predominantly at the plasma membrane. {ECO:0000269|PubMed:15899900}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000269|PubMed:15899900}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000305|PubMed:15899900}; | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain. {ECO:0000269|PubMed:15899900, ECO:0000269|PubMed:16107206}. | Mus musculus (Mouse) |
A2APB8 | TPX2_MOUSE | MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFDEAASTYVPIAQQVEAFHKRTPNRYHLRNKKDESLLPSKSVNKIARDPQTPILQTKYRTRAVTCKSTAEQEAEELEKLQQYKFKARELDPRIFESGPILPKRAPVKPPTQPVGFDLEIEKRIHERESKKKTEDEQFEFHSRPCPTKILEDVVGVPEKKVIPATVPKSPVFALKNRIRVPIKDEEEEKPVVIKAQPVPHYGVPYKPHIAEARNVEVCPFSFDTRDKERQLQKEKKIKEMQKGEVPKFKALPVPHFDTINLPEKKVKNVTQAEPFSLETDKRGAYKAEMWKHQLEEEQKQQKDAACFKARPNTVIFQEPFVPKKEKKSLAENPSGSLVQEPFQLATERRAKERQELEKKMAEVEAWKLQQLEEVRQQEEEQQKEELARLRKELVHKANPIRKYAAVEVKSSELPLTVPVSPKFSTRFQ | null | null | activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; cell division [GO:0051301]; microtubule nucleation [GO:0007020]; mitotic spindle assembly [GO:0090307]; negative regulation of microtubule depolymerization [GO:0007026]; regulation of mitotic spindle organization [GO:0060236]; spindle assembly [GO:0051225] | aster [GO:0005818]; axon hillock [GO:0043203]; cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686]; nuclear microtubule [GO:0005880]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle pole [GO:0000922] | importin-alpha family protein binding [GO:0061676]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901] | PF09041;PF06886;PF12214; | null | TPX2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27753540}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9ULW0}. Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucleus. Is released from the nucleus in apoptotic cells and is detected on apoptotic microtubules. {ECO:0000250|UniProtKB:Q9ULW0}. | null | null | null | null | null | FUNCTION: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation. {ECO:0000250|UniProtKB:Q9ULW0, ECO:0000269|PubMed:18663142}. | Mus musculus (Mouse) |
A2APC3 | TTLL9_MOUSE | MSRQKNQNSKGHGVSKGKEREQRTLIRFKTTLMNTLMDVLRHRPGWVEVKDEGEWDFYWCDVSWLRENFDHTYMDEHVRISHFRNHYELTRKNYMVKNLKRFRKYLERESGKTEAAKCDFFPKTFEMPCEYHLFVEEFRKNPGITWIMKPVARSQGKGIFLFRRLKDIMDWRKGTSGKKPTGVETQPARANMNPSGSHDTRSSDDQKDDLPVENYVAQRYVENPYLIGGRKFDLRVYVLVMSYIPLRAWLYRDGFARFSNTRFTLNSIDDHYVHLTNVAVQKTSPDYHLKKGCKWMLQRFRQYLASKHGPKAVETLFSDMDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLEDTLHVVDMEARLTGKEKRVGGFDLMWNDGPVSREDGPSDLSGMGNFVTNTHLGCVNDRKEQLRQLFRSLQAQRKAPS | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | flagellated sperm motility [GO:0030317]; microtubule cytoskeleton organization [GO:0000226]; protein modification process [GO:0036211] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; motile cilium [GO:0031514] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.1490.20;3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:27257088}. | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:27257088}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000305|PubMed:27257088}; | null | null | null | null | FUNCTION: Probable tubulin polyglutamylase that generates side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of target proteins (PubMed:27257088). Similar to TTLL1, may acquire enzymatic activity only in complex with other proteins as it is most likely lacking domains important for autonomous activity (Probable). Mediates tubulin polyglutamylation which induces establishment of microtubule heterogeneity in sperm flagella, thereby playing a role in normal motile flagella axoneme structure and sperm flagella beating pattern (PubMed:27257088). {ECO:0000269|PubMed:27257088, ECO:0000305|PubMed:17499049}. | Mus musculus (Mouse) |
A2APF3 | CTCFL_MOUSE | MAAAEVPVPSGYFTQIKEQKLKPGDLEEEKEEDGVQRVEAQEGVVKEVEAENSCLLLEARAPVESDRRILTLQTVHLESQDVHLQGLGWLSVPHSEELSGTVPEAEGILQLPSVLWLDPEPQLSLQHCVTVSIPEELYPPEELQRIHFHLLRENVLMAEENPELTPDLDESTALKKPEEDEKDQLPPQGETDKREERLLLLEMKPKEGKDDEIVLTISHLSLEEQQDPPAANQTSVPGAKAAKPKRRRQTKGKPQSFQCDTCPFTSSKLSTFNRHIKIHSNERPHLCHLCLKAFRTVTLLRNHVNTHTGTRPHKCRDCDMAFVTSGELVRHRRYKHTYEKPFKCSLCKYASVEASKMKRHIRSHTGERPFQCCQCAYASRDSYKLKRHMRTHSGEKPYECPTCHVRFTQSGTMKIHIAQKHGENVPKYECPHCATIIARKSDLRVHLRNLHSQSPEEMKCRYCPAGFHERYALIQHQRTHKNEKKFKCKQCDYACKQERCLKAHMRMHTGEKPFSCLACNKHFRQKQLLTVHLRKYHDPNFVPNLHLCLKCDKRFSRWSNLQRHRKKCDPEHETLAPNKDRRPVTRTQASEGEAGHKEGEPQCPGEQALGHQGEAAGSQSPDHGLTCEIIFNMMDK | null | null | establishment of protein localization to chromatin [GO:0071169]; genomic imprinting [GO:0071514]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634] | chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone binding [GO:0042393]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00096; | 3.30.160.60; | CTCF zinc-finger protein family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17048991}. | null | null | null | null | null | FUNCTION: Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites. Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters. {ECO:0000269|PubMed:17048991}. | Mus musculus (Mouse) |
A2APX8 | SCN1A_MOUSE | MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVQWPPTNASLEEHSIEKNITMDYNGTLVNETVFEFDWKSYIQDSRYHYFLEGVLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEAAQQAAATTASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDDDEFHKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHIVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEHFNHVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIATDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGIAYVKRKIYEFIQQSFVKKQKILDEIKPLDDLNNRKDNCISNHTTEIGKDLDCLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPAEEQPVIEPEETLEPEACFTEGCVQRFKCCQISVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGDIFEISEVNNHSDCLKLIERNETARWKNVKVNFDNVGFGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSDYVTSILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKLKGGANLLVKEDMLIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK | null | null | adult walking behavior [GO:0007628]; cardiac muscle cell action potential involved in contraction [GO:0086002]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; determination of adult lifespan [GO:0008340]; establishment of localization in cell [GO:0051649]; membrane depolarization during action potential [GO:0086010]; nerve development [GO:0021675]; neuromuscular process controlling posture [GO:0050884]; neuronal action potential [GO:0019228]; neuronal action potential propagation [GO:0019227]; regulation of membrane potential [GO:0042391]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814] | axon [GO:0030424]; axon initial segment [GO:0043194]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; nuclear body [GO:0016604]; presynaptic membrane [GO:0042734]; sodium channel complex [GO:0034706]; T-tubule [GO:0030315]; voltage-gated sodium channel complex [GO:0001518]; Z disc [GO:0030018] | sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.1/SCN1A subfamily | PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27281198}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:27281198}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes (PubMed:16921370, PubMed:17928448, PubMed:27281198). Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons (PubMed:16921370, PubMed:22914087). Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli (PubMed:27281198). {ECO:0000269|PubMed:16921370, ECO:0000269|PubMed:17928448, ECO:0000269|PubMed:22914087, ECO:0000269|PubMed:27281198}. | Mus musculus (Mouse) |
A2AQ07 | TBB1_MOUSE | MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGVLFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGKMSTKEVDQQLLSIQTRNSNCFVEWIPNNVKVAVCDIPPRGLNMAATFLGNNTAIQELFTRVSEHFSAMFRRRAFVHWYTSEGMDISEFGEAESDIHDLVSEYQQFQDVRAGLEDSEEDVEEAEVEAEDKDH | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; platelet aggregation [GO:0070527]; platelet formation [GO:0030220]; spindle assembly [GO:0051225]; thyroid gland development [GO:0030878]; thyroid hormone transport [GO:0070327] | cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; microtubule [GO:0005874]; mitotic spindle [GO:0072686] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility (PubMed:33414192). {ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Glutamylation is also involved in cilia motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q9H4B7}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Mus musculus (Mouse) |
A2AQ19 | RTF1_MOUSE | MRGRLCVGRAAAVAAAVAAAAVAVPLAGGQEGSQGGVRRGSRGTTMVKKRKGRVVIDSDTEDSGSDENLDQELLSLAKRKRSDSEEKEPPVSQPAASSDSETSDSDDEWTFGSNKNKKKGKTRKVEKKGAMKKQANKAASSGSSDRDSSAESSAPEEGEVSDSESSSSSSSSDSDSSSEDEEFHDGYGEDLMGDEEDRARLEQMTEKEREQELFNRIEKREVLKRRFEIKKKLKTAKKKEKKEKKKKQEEEQEKKKLTQIQESQVTSHNKERRSKRDEKLDKKSQAMEELKAEREKRKNRTAELLAKKQPLKTSEVYSDDEEEEDDDKSSEKSDRSSRTSSSDEEEEKEEIPPKSQPVSLPEELNRVRLSRHKLERWCHMPFFAKTVTGCFVRIGIGNHNSKPVYRVAEITGVVETAKVYQLGGTRTNKGLQLRHGNDQRVFRLEFVSNQEFTESEFMKWKEAMFSAGMQLPTLDEINKKELSIKEALNYKFNDQDIEEIVKEKERFRKAPPNYAMKKTQLLKEKAMAEDLGDQDKAKQIQDQLNELEERAEALDRQRTKNISAISYINQRNREWNIVESEKALVAESHNMRNQQMDPFTRRQCKPTIVSNSRDPAVQAAILAQLNAKYGSGVLPDAPKEMSKGQGKDKDLNSKTASDLSEDLFKVHDFDVKIDLQVPSSESKALAITSKAPPAKDGAPRRSLNLEDYKKRRGLI | null | null | blastocyst growth [GO:0001832]; chromatin organization [GO:0006325]; endodermal cell fate commitment [GO:0001711]; negative regulation of transcription by RNA polymerase II [GO:0000122]; stem cell population maintenance [GO:0019827]; transcription elongation by RNA polymerase II [GO:0006368]; Wnt signaling pathway [GO:0016055] | Cdc73/Paf1 complex [GO:0016593]; nucleolus [GO:0005730] | RNA polymerase II C-terminal domain phosphoserine binding [GO:1990269]; single-stranded DNA binding [GO:0003697] | PF03126; | 3.90.70.200; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Binds single-stranded DNA (By similarity). Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex. {ECO:0000250, ECO:0000269|PubMed:19345177}. | Mus musculus (Mouse) |
A2AQ25 | SKT_MOUSE | MEESEGQKCEPNLPPSGDSRQMPQQGRSNLHVTSQEDAACRRPRERLSNGNARAQVSKPARNIPRRHTLGGPRSSKEILGMQPSEMDRKREAFLEHLKQKYPHHATAIMGHQERLRDQTKSPKLSHSPQPPNLGDPVEHLSETSGDSLEAMSEGEVPSPFARGSRTRASLPVVRSANQTKERSLGVLYLQYGDETKQLRMPNEVTSTDTIRALFVSAFPQQLTMKMLESPSVAIYIKDDSRNVYYELNDVRNIQDRSLLKVYNKDPSHAFNHMTKAVNGDMRMQREIVYARGDGLVAPRPGSVAHPPHVIPNSPPSTPVPHSLPPSPSRIPYGGSRPMAIPGNATIPRDRLSSLPVSRSISPSPSAILERRDVKPDEDMSSKNLVMFRNEGFYADPYLYHEGRMSIASSHGGHPLDVPDHVIAYHRTAIRSASAYCSPSLQAEMHMEQSLYRQKSRKYPDSHLPTLGSKTPPASPHRVGDLRMIDLHPHLNTHGPPHTLQPDRASPSRQSFKKEPGTLVYIEKPRNTSGLSSLVDLGPPLVEKQGFAYSTTTIPKDRETRERMQAMEKQIASLTGLVQSALFKGPITSSSKEASSEKMVKATANRNQADGAGTAHVSAGKVLGSVEFSLPPSQPLPAGTSPIHTSLLDMRRNVAELRLQLQQMRQLQLQNQEILRAMMKKAELEISNKVKETMKRLEDPVQRQRTLVEQERQKYLHEEERIVKKLCELEDFVEDLKKDSSSTGRVVTLKDVEDGAFLLRQVGEAVATLKGEFPTLQNKMRAVLRIEVEAVRFLKEEPHKLDSLLKRVRSMTDVLTMLRRHVTDGLLKGTDASQAAQYVAMEKATAAEVLKHQEETAHAPGQPLHCSTGSPGDVKSEVVPLSTMTVHHVQSSPVVMQPSQHSSALMNPAQNLPGGTRPHTASPPAITQEVTSAQSAPGPQSPQTPVNGSSMQSLFIEEIHSVSAKNRAVSIEKAEKKWEEKRQNLEHYNGKEFEKLLEEAQANIMKSIPNLEMPPASSPVSKGDAAGDKLELSEDSPNSEQELDKIGGKSPPPPPPPPRRSYLPGSGLTTTRSGDVVYTGRSMSKVSSEDPGPTPQTRATKCPPEEPASAWAPSPPPVPAPSSKEEEEEEEEGDKIMAELQAFQKCSFMDVNPNSHAEQSRANSHLKDTRAGATAPPKEKKNLEFYHEDVRKSDVECENGPQVESQKVTAGALRPSGPPKWERVMVDSISDTSRTSECRADTFTEENATPNKSLFRDSRNYSQKNVPKVSFSSSGLNSLEGEINKGPNVSGLQCAIPDLENQKLNFGKTKEIGQQGQENADKSHIPLPTRSAEFSIHDVKTQDQDVPVTGYGQVVLRSKVGRHANMNMNEDGESTPSSPSEEHTATDNIAFMITKTAVQVLSSGEVHDIVSQKGQDVQTVNIDGRKETASQHEGTEGEEPVVCLDKKPVIIIFDEPMDIRSAYKRLSTIFEECDEELERMLTEEKIEEEEEDENEDSGVRTSSQMSCEQVDSRSDRMGQKAETQSQPHVLSAELLTPGVQGVRKAEQRKLSSADSPDSGNKCGMVDDQFESPKKKFKFKFPKKQLAALTQAIRTGTKTGKKTLQVVVYEEEEEDGTLKQHKEAKRFEITRSQPEDALKTMARRQEQLSPEGTLPASRTDEIRKSTYRTLDSLEQTIKQLENTISEMSPRALVDTSCSSNRDCGASLPHMAQEVSPRSLLVLDEVPPAPEPPTSISPASRKGSSTTPQTSRMPVPMTSKNRPGSLDKASKQSKLQDPRQYRQANGSAKKAGGDCKPTSPSLPASKIPALSPSSGKSSSLPSASGDSSNLPNAPATKPSIASTPLSPQAGRSAHSASLIPSVSNGSLKFQSPPHAGKGHHHLSFALQTQNGRAAPTTSSSSSPPSPASPTSLNQGARGIRTIHTPSLASYKAQNGSSSKATPSTAKETS | null | null | embryonic skeletal system development [GO:0048706] | centrosome [GO:0005813]; cytoplasm [GO:0005737] | null | PF03915; | 1.20.58.1540; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5T5P2}. Cytoplasm {ECO:0000269|PubMed:16204209}. | null | null | null | null | null | FUNCTION: Required for normal development of intervertebral disks. {ECO:0000269|PubMed:16204209}. | Mus musculus (Mouse) |
A2AR95 | LRAD3_MOUSE | MWLLGPLCLLLSSTAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCRNGLCIDKSFICDGQNNCQDNSDEESCESSLEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGVQYVATQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSAYSASSQAASSLLSVEASSHNPEQPGSPEGSAEPRDSVPSQGTEEV | null | null | receptor-mediated endocytosis [GO:0006898]; regulation of protein processing [GO:0070613] | membrane [GO:0016020]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540] | PF00057; | 4.10.400.10; | LDLR family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21795536}; Single-pass type I membrane protein {ECO:0000269|PubMed:21795536}. | null | null | null | null | null | FUNCTION: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production (PubMed:21795536). May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86YD5, ECO:0000269|PubMed:21795536}. | Mus musculus (Mouse) |
A2ARA8 | ITA8_MOUSE | MSAGTHCGPPGNRAPPFARLCCVSAALGMLWSPACLAFNLDVDKLTVYSGPEGSYFGYSLDFYIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPSERSAQCKQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVRAHKGKVVACAPLYHWRTLKPNPAKDPVGTCYVAIQNFSAYAEHSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITVSIADIIANYSFKDILRKLAAEKQTDVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNNDGMDDILVGAPLFMEREFESNPREVGQVYLYLQASALLFQDPQVLTGTETFGRFGSSVAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNPRGLHSKPSQVLQGIWGSQTIPSGFGFSLRGDADIDKNDYPDLLVGAFGKGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQIPEFPTPVACFSVRVCASIAGQSISNTIALLAEVQLDFLKQKGAIKRTLFLHNHQSHFTFPFVMKQQKSLHCQDFMVYLRDETEFRDKLSPINISLNYSLDDSTFKDSLEVKPILNHYRDNVVTEQAHILVDCGEDNLCVPDLKLSARPDKHQIIIGDENHLMLIINARNEGEGAYEAELFVIIPEEADYVGIERNNKGLRPLSCEYKMENVTRMVVCDLGNPMVTGTNFSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFERVQINITAIAQVEIRGVSHPPQIVLPIHNWEPEKKPHKEEEVGPLVEHIYELHNIGPSTISDSILDVGWPFSARDEFLLYIFHLQTLGPLQCQTNPEINPQDIKPAASPEDTPELSAFLRNATIPHLVRKRDVPVVQLHRQSPARILNCTNIDCLQISCAVGRLGGGESAVLKVRSRLWAHTFLKRKNDHYALASLVSFEVKKMPYKEQPAKLPAGSTAVKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQDEMTDREQLTSDKTPEA | null | null | cell adhesion mediated by integrin [GO:0033627]; cell projection organization [GO:0030030]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; establishment of protein localization [GO:0045184]; extracellular matrix organization [GO:0030198]; inner ear morphogenesis [GO:0042472]; integrin-mediated signaling pathway [GO:0007229]; memory [GO:0007613]; mesodermal cell differentiation [GO:0048333]; metanephros development [GO:0001656]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; smooth muscle cell differentiation [GO:0051145]; smooth muscle tissue development [GO:0048745]; substrate adhesion-dependent cell spreading [GO:0034446]; transforming growth factor beta receptor signaling pathway [GO:0007179] | apical part of cell [GO:0045177]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; glutamatergic synapse [GO:0098978]; integrin complex [GO:0008305]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839] | integrin binding [GO:0005178]; metal ion binding [GO:0046872] | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10742111}; Single-pass type I membrane protein {ECO:0000269|PubMed:10742111}. Cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons. {ECO:0000269|PubMed:10742111, ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11891185, ECO:0000269|PubMed:12787402, ECO:0000269|PubMed:17537792, ECO:0000269|PubMed:9054500, ECO:0000269|PubMed:9548928, ECO:0000269|PubMed:9614184}. | Mus musculus (Mouse) |
A2ARI4 | LGR4_MOUSE | MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVHLESLTLTGTKISSIPDDLCQNQKMLRTLDLSYNDIRDLPSFNGCRALEEISLQRNQISLIKETTFQGLTSLRILDLSRNLIREIHSGAFAKLGTITNLDVSFNELTSFPTEGLNGLNQLKLVGNFQLKDALAARDFANLRSLSVPYAYQCCAFWGCDSYANLNTEDNSPQDHSVTKEKGATDAANATSTAESEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALLFNLLVILTVFASCSSLPASKLFIGLISVSNLLMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGSLAVFSSESAVFLLTLAAVERSVFAKDVMKNGKSSHLRQFQVAALVALLGAAIAGCFPLFHGGQYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAIIYTKLYCNLEKEDPSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKDDWKLLKRRVTRKHGSVSVSISSQGGCGEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPVLTVASCQRPEAYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVRD | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; axon guidance [GO:0007411]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; digestive tract development [GO:0048565]; epithelial cell proliferation [GO:0050673]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; hair follicle development [GO:0001942]; hormone-mediated signaling pathway [GO:0009755]; innate immune response [GO:0045087]; intestinal stem cell homeostasis [GO:0036335]; male genitalia development [GO:0030539]; metanephric glomerulus development [GO:0072224]; metanephric nephron tubule morphogenesis [GO:0072282]; negative chemotaxis [GO:0050919]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of cytokine production [GO:0001818]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; osteoblast differentiation [GO:0001649]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; spermatogenesis [GO:0007283]; tube morphogenesis [GO:0035239]; Wnt signaling pathway [GO:0016055] | plasma membrane [GO:0005886] | heparin binding [GO:0008201]; protein-hormone receptor activity [GO:0016500]; Roundabout binding [GO:0048495]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF13855;PF01462; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21693646}; Multi-pass membrane protein {ECO:0000269|PubMed:21693646}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and pro-inflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP (PubMed:24353284). Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (PubMed:32493844). {ECO:0000269|PubMed:18955481, ECO:0000269|PubMed:19605502, ECO:0000269|PubMed:21508962, ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:23393138, ECO:0000269|PubMed:23444378, ECO:0000269|PubMed:23533175, ECO:0000269|PubMed:23589304, ECO:0000269|PubMed:24353284, ECO:0000269|PubMed:32493844}. | Mus musculus (Mouse) |
A2ARP1 | VIP1_MOUSE | MWSLTANEDESTTAHFFLGAGDEGLGTCGIGMRTEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPACPEECSLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPEAEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASNEGQDLQREPLAPSLLLVLKWGGELTPDGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTGSTSLLNSMSVIQNPVKVCDQVFALIENLTHQIRERMQDPSSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKVEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLYSRGVLSPGRHVRTRLYFTSESHVHSLLSVFRYGGLLDETQDAQWQRALAYLSAISELNYMTQIVIMLYEDNTRDPLSEERFHVELHFSPGVKGVEEGSAPAGCGFRPASSENEEMKTDPGSIENLCPGKASDEPDRALQTSPQPVEGTGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARTHGKKLPPASLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLTKVCQRHTDAHAQASAALFDSMHNHQASDSPFSPPRTLHSPPLQLRHRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSHFGFSDQSSVNIHMTEEKQGFGLLQETPGDGTRELHIERQQELVEPAQSPQELPVEICPSGSQGVTKVSQTCQEVPDIVQPCHNIHEEIGQPQQEVPDISQLLLKDHDTTTNTCHLCQASQLSQKVCEEICQLCQDNHEESNQLCQEVSVKLGRMVHGFPVNVDSTAQETLMEIGRPTQEIPEDPYQEFSVKVGVLAQKAPAISELSQDIPEADKPSQELSEETELQAQEVSEEIDQESEVVDELPPEAIS | 2.7.4.24 | null | inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827] | PF00328;PF18086; | 3.40.50.11950;3.30.470.20;3.40.50.1240; | Histidine acid phosphatase family, VIP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway. {ECO:0000250|UniProtKB:Q6PFW1}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q6PFW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; Evidence={ECO:0000250|UniProtKB:Q6PFW1}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q6PFW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; Evidence={ECO:0000250|UniProtKB:Q6PFW1}; | null | null | null | null | FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress. {ECO:0000250|UniProtKB:Q6PFW1}. | Mus musculus (Mouse) |
A2ARP9 | CTSR2_MOUSE | MAQEQGHFQLLRADAIRSKLIDTFSLIEHLQGLSQAVPRHTLREILDPSYQQKLMSGDQEQLVRFSIKPRRMGHITHSRRLLSRLRVRCSRMPPLSLWAGWVLDSSVFSKFIISLIFLNTFVLMVEIELMESTNTALWPVKLALEVADWFILLSFIVEILLMWLASFSLFWKDAWNVFDFFVTLLSLLPELVVLLGVPAHSVWLQLLRVCRVLRSLKLFARFRQIKVILLALVRALKSMTFLLMLLLIFFYIFAVTGVYFFREYSRSTIEGLEYNMFFSDLLNSLVTVFILFTLDHWYAVLQDIWKVPESSRVFSSIYVILWLLLGSIIFRNIIVAMMVTNFQNIRSELSEEMSHLEVQYKADMFKQQIIQRRQHSESLRGTSLGKVSEDIIETSDASDDDDDDDDDDDDDDDDDDDKSDATESDNEESDSENSESENSESEKIDPEKDYAKKSYPEKSHPEKSYPEKSHPEKSYPEKSHPKKSYDEQAEAEKVKEESKEKAYPVSHSISSHGSTAADTAFLENLDWETLVHENLPGLMDMDQDDRIVWPRDSLFRYFELLEKLQYNLEERKKLQEFAVQALMSFEDK | null | null | fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240] | CatSper complex [GO:0036128]; sperm flagellum [GO:0036126] | calcium channel activity [GO:0005262]; calcium-activated cation channel activity [GO:0005227] | PF00520; | 1.10.287.70;1.20.120.350; | Cation channel sperm-associated (TC 1.A.1.19) family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:11675491}; Multi-pass membrane protein {ECO:0000269|PubMed:34225353}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:21412339}; | null | null | null | null | FUNCTION: Pore-forming subunit of the CatSper complex, a sperm-specific voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. {ECO:0000269|PubMed:14657366, ECO:0000269|PubMed:16036917, ECO:0000269|PubMed:17174296, ECO:0000269|PubMed:21412339}. | Mus musculus (Mouse) |
A2ARV4 | LRP2_MOUSE | MERGAAAAAWMLLLAIAACLAPVSGQECGSGNFRCDNGYCIPASWRCDGTRDCLDDTDEIGCPPRSCGSGFFLCPAEGTCIPSSWVCDQDKDCSDGADEQQNCPGTTCSSQQLTCSNGQCVPIEYRCDHVSDCPDGSDERNCYYPTCDQLTCANGACYNTSQKCDHKVDCRDSSDEANCTTLCSQKEFQCGSGECILRAYVCDHDNDCEDNSDEHNCNYDTCGGHQFTCSNGQCINQNWVCDGDDDCQDSGDEDGCESNQRHHTCYPREWACPGSGRCISMDKVCDGVPDCPEGEDENNATSGRYCGTGLCSILNCEYQCHQTPYGGECFCPPGHIINSNDSRTCIDFDDCQIWGICDQKCESRQGRHQCLCEEGYILERGQHCKSNDSFSAASIIFSNGRDLLVGDLHGRNFRILAESKNRGIVMGVDFHYQKHRVFWTDPMQAKVFSTDINGLNTQEILNVSIDAPENLAVDWINNKLYLVETRVNRIDVVNLEGNQRVTLITENLGHPRGIALDPTVGYLFFSDWGSLSGQPKVERAFMDGSNRKDLVTTKLGWPAGITLDLVSKRVYWVDSRYDYIETVTYDGIQRKTVARGGSLVPHPFGISLFEEHVFFTDWTKMAVMKANKFTDTNPQVYHQSSLTPFGVTVYHALRQPNATNPCGNNNGGCAQICVLSHRTDNGGLGYRCKCEFGFELDADEHHCVAVKNFLLFSSQTAVRGIPFTLSTQEDVMVPVTGSPSFFVGIDFDAQHSTIFYSDLSKNIIYQQKIDGTGKEVITANRLQNVECLSFDWISRNLYWTDGGSKSVTVMKLADKSRRQIISNLNNPRSIVVHPAAGYMFLSDWFRPAKIMRAWSDGSHLMPIVNTSLGWPNGLAIDWSTSRLYWVDAFFDKIEHSNLDGLDRKRLGHVDQMTHPFGLTVFKDNVFLTDWRLGAIIRVRKSDGGDMTVVRRGISSIMHVKAYDADLQTGTNYCSQTTHPNGDCSHFCFPVPNFQRVCGCPYGMKLQRDQMTCEGDPAREPPTQQCGSSSFPCNNGKCVPSIFRCDGVDDCHDNSDEHQCGALNNTCSSSAFTCVHGGQCIPGQWRCDKQNDCLDGSDEQNCPTRSPSSTCPPTSFTCDNHMCIPKEWVCDTDNDCSDGSDEKNCQASGTCHPTQFRCPDHRCISPLYVCDGDKDCVDGSDEAGCVLNCTSSQFKCADGSSCINSRYRCDGVYDCKDNSDEAGCPTRPPGMCHPDEFQCQGDGTCIPNTWECDGHPDCIQGSDEHNGCVPKTCSPSHFLCDNGNCIYNSWVCDGDNDCRDMSDEKDCPTQPFHCPSSQWQCPGYSICVNLSALCDGVFDCPNGTDESPLCNQDSCLHFNGGCTHRCIQGPFGATCVCPIGYQLANDTKTCEDVNECDIPGFCSQHCVNMRGSFRCACDPEYTLESDGRTCKVTASENLLLVVASRDKIIMDNITAHTHNIYSLVQDVSFVVALDFDSVTGRVFWSDLLEGKTWSAFQNGTDKRVVHDSGLSLTEMIAVDWIGRNIYWTDYTLETIEVSKIDGSHRTVLISKNVTKPRGLALDPRMGDNVMFWSDWGHHPRIERASMDGTMRTVIVQEKIYWPCGLSIDYPNRLIYFMDAYLDYIEFCDYDGQNRRQVIASDLVLHHPHALTLFEDSVFWTDRGTHQVMQANKWHGRNQSVVMYSVPQPLGIIAIHPSRQPSSPNPCASATCSHLCLLSAQEPRHYSCACPSGWNLSDDSVNCVRGDQPFLISVRENVIFGISLDPEVKSNDAMVPISGIQHGYDVEFDDSEQFIYWVENPGEIHRVKTDGSNRTAFAPLSLLGSSLGLALDWVSRNIYYTTPASRSIEVLTLRGDTRYGKTLITNDGTPLGVGFPVGIAVDPARGKLYWSDHGTDSGVPAKIASANMDGTSLKILFTGNMEHLEVVTLDIQEQKLYWAVTSRGVIERGNVDGTERMILVHHLAHPWGLVVHGSFLYYSDEQYEVIERVDKSSGSNKVVFRDNIPYLRGLRVYHHRNAADSSNGCSNNPNACQQICLPVPGGMFSCACASGFKLSPDGRSCSPYNSFIVVSMLPAVRGFSLELSDHSEAMVPVAGQGRNVLHADVDVANGFIYWCDFSSSVRSSNGIRRIKPNGSNFTNIVTYGIGANGIRGVAVDWVAGNLYFTNAFVYETLIEVIRINTTYRRVLLKVSVDMPRHIVVDPKHRYLFWADYGQKPKIERSFLDCTNRTVLVSEGIVTPRGLAVDHDTGYIYWVDDSLDIIARIHRDGGESQVVRYGSRYPTPYGITVFGESIIWVDRNLRKVFQASKQPGNTDPPTVIRDSINLLRDVTIFDEHVQPLSPAELNNNPCLQSNGGCSHFCFALPELPTPKCGCAFGTLEDDGKNCATSREDFLIYSLNNSLRSLHFDPQDHNLPFQAISVEGMAIALDYDRRNNRIFFTQKLNPIRGQISYVNLYSGASSPTILLSNIGVTDGIAFDWINRRIYYSDFSNQTINSMAEDGSNRAVIARVSKPRAIVLDPCRGYMYWTDWGTNAKIERATLGGNFRVPIVNTSLVWPNGLTLDLETDLLYWADASLQKIERSTLTGSNREVVISTAFHSFGLTVYGQYIYWTDFYTKKIYRANKYDGSDLIAMTTRLPTQPSGISTVVKTQQQQCSNPCDQFNGGCSHICAPGPNGAECQCPHEGSWYLANDNKYCVVDTGARCNQFQFTCLNGRCISQDWKCDNDNDCGDGSDELPTVCAFHTCRSTAFTCANGRCVPYHYRCDFYNDCGDNSDEAGCLFRSCNSTTEFTCSNGRCIPLSYVCNGINNCHDNDTSDEKNCPPITCQPDFAKCQTTNICVPRAFLCDGDNDCGDGSDENPIYCASHTCRSNEFQCVSPHRCIPSYWFCDGEADCVDSSDEPDTCGHSLNSCSANQFHCDNGRCISSSWVCDGDNDCGDMSDEDQRHHCELQNCSSTEFTCINSRPPNRRCIPQHWVCDGDADCADALDELQNCTMRACSTGEFSCANGRCIRQSFRCDRRNDCGDYSDERGCSYPPCRDDQFTCQNGQCITKLYVCDEDNDCGDGSDEQEHLCHTPEPTCPPHQFRCDNGHCIEMGTVCNHVDDCSDNSDEKGCGINECQDSSISHCDHNCTDTITSFYCSCLPGYKLMSDKRTCVDIDECKETPQLCSQKCENVIGSYICKCAPGYIREPDGKSCRQNSNIEPYLVFSNRYYIRNLTIDGTSYSLILQGLGNVVALDFDRVEERLYWIDAEKQIIERMFLNKTNQETIISHRLRRAESLAVDWVSRKLYWLDAILDCLFVSDLEGRQRKMLAQHCVDANNTFCFENPRGIVLHPQRGYVYWADWGDHAYIARIGMDGTNKTVIISTKIEWPNAITIDYTNDLLYWADAHLGYIEFSDLEGHHRHTVYDGTLPHPFALTIFEDTVFWTDWNTRTVEKGNKYDGSGRVVLVNTTHKPFDIHVLHPYRQPIMSNPCATNNGGCSHLCLIKAGGRGFTCECPDDFQTVQLRDRTLCMPMCSSTQFLCGNNEKCIPIWWKCDGQKDCSDGSDESDLCPHRFCRLGQFQCRDGNCTSPQALCNARQDCADGSDEDRVLCEHHRCEANEWQCANKRCIPEYWQCDSVDDCLDNSDEDPSHCASRTCRPGQFKCNNGRCIPQSWKCDVDNDCGDYSDEPIHECMTAAYNCDNHTEFSCKTNYRCIPQWAVCNGFDDCRDNSDEQGCESVPCHPSGDFRCGNHHCIPLRWKCDGIDDCGDNSDEESCVPRECTESEFRCADQQCIPSRWVCDQENDCGDNSDERDCEMKTCHPEHFQCTSGHCVPKALACDGRADCLDASDESACPTRFPNGTYCPAAMFECKNHVCIQSFWICDGENDCVDGSDEEIHLCFNVPCESPQRFRCDNSRCIYGHQLCNGVDDCGDGSDEKEEHCRKPTHKPCTDTEYKCSNGNCVSQHYVCDNVDDCGDLSDETGCNLGENRTCAEKICEQNCTQLSNGGFICSCRPGFKPSTLDKNSCQDINECEEFGICPQSCRNSKGSYECFCVDGFKSMSTHYGERCAADGSPPLLLLPENVRIRKYNISSEKFSEYLEEEEHIQAIDYDWDPEGIGLSVVYYTVLSQGSQFGAIKRAYLPDFESGSNNPVREVDLGLKYLMQPDGLAVDWVGRHIYWSDAKSQRIEVATLDGRYRKWLITTQLDQPAAIAVNPKLGLMFWTDQGKQPKIESAWMNGEHRSVLASANLGWPNGLSIDYLNGDRIYWSDSKEDVIESIKYDGTDRRLIINDAMKPFSLDIFEDQLYWVAKEKGEVWRQNKFGKGNKEKLLVVNPWLTQVRIFHQLRYNQSVSNPCKQVCSHLCLLRPGGYSCACPQGSDFVTGSTVECDAASELPITMPSPCRCMHGGSCYFDENDLPKCKCSSGYSGEYCEIGLSRGIPPGTTMALLLTFAMVIIVGALVLVGFFHYRKTGSLLPSLPKLPSLSSLAKPSENGNGVTFRSGADVNMDIGVSPFGPETIIDRSMAMNEQFVMEVGKQPVIFENPMYAAKDSTSKVGLAVQGPSVSSQVTVPENVENQNYGRSIDPSEIVPEPKPASPGADETQGTKWNIFKRKPKQTTNFENPIYAEMDTEQKEAVAVAPPPSPSLPAKASKRSSTPGYTATEDTFKDTANLVKEDSDV | null | null | amyloid-beta clearance [GO:0097242]; aorta development [GO:0035904]; cell population proliferation [GO:0008283]; cellular response to growth factor stimulus [GO:0071363]; chemoattraction of axon [GO:0061642]; coronary artery morphogenesis [GO:0060982]; coronary vasculature development [GO:0060976]; diol metabolic process [GO:0034311]; endocytic hemoglobin import into cell [GO:0020028]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; folate import across plasma membrane [GO:1904447]; forebrain development [GO:0030900]; heart development [GO:0007507]; kidney development [GO:0001822]; male gonad development [GO:0008584]; metal ion transport [GO:0030001]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; neural tube closure [GO:0001843]; neuron projection arborization [GO:0140058]; outflow tract septum morphogenesis [GO:0003148]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of endocytosis [GO:0045807]; positive regulation of lipoprotein transport [GO:0140077]; positive regulation of neurogenesis [GO:0050769]; positive regulation of oligodendrocyte progenitor proliferation [GO:0070447]; protein import [GO:0017038]; protein transport [GO:0015031]; pulmonary artery morphogenesis [GO:0061156]; receptor-mediated endocytosis [GO:0006898]; response to leptin [GO:0044321]; response to X-ray [GO:0010165]; secondary heart field specification [GO:0003139]; sensory perception of sound [GO:0007605]; transcytosis [GO:0045056]; vagina development [GO:0060068]; ventricular compact myocardium morphogenesis [GO:0003223]; ventricular septum development [GO:0003281]; vitamin D metabolic process [GO:0042359] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; axonal growth cone [GO:0044295]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; endosome lumen [GO:0031904]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; receptor complex [GO:0043235] | calcium ion binding [GO:0005509]; hemoglobin binding [GO:0030492]; hormone binding [GO:0042562]; insulin-like growth factor I binding [GO:0031994]; low-density lipoprotein particle receptor binding [GO:0050750]; nuclear receptor binding [GO:0016922]; PDZ domain binding [GO:0030165]; protein transporter activity [GO:0140318]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; SH3 domain binding [GO:0017124] | PF12662;PF07645;PF14670;PF00057;PF00058; | 2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression. {ECO:0000250|UniProtKB:P98158}.; PTM: N-glycosylation is required for ligand binding. Contains core-fucosylated N-glycans in kidney proximal convoluted tubules (PCTs) and hybrid-type N-glycans in proximal straight tubules (PSTs). Interacts with ligands in a glycoform-dependent manner. Retinol-binding protein and the vitamin D carrier GC/DBP are endocytosed primarily by PCTs, albumin is endocytosed equally by PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed primarily by PSTs. {ECO:0000269|PubMed:27773703}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, coated pit {ECO:0000269|PubMed:22340494}. Cell projection, dendrite {ECO:0000269|PubMed:20637285}. Cell projection, axon {ECO:0000269|PubMed:20637285}. Note=Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form. {ECO:0000250|UniProtKB:P98158}. | null | null | null | null | null | FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (PubMed:10766831). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (PubMed:22841573). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (PubMed:24825475). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (PubMed:10052453). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (PubMed:18174160). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (PubMed:15623804). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (PubMed:22340494). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (PubMed:24639464). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (PubMed:20460439). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (PubMed:20637285). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (PubMed:22354480). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (PubMed:26439398). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (PubMed:16143106). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensin 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (PubMed:26822476). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082). {ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:10766831, ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:20637285, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480, ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:23825075, ECO:0000269|PubMed:24639464, ECO:0000269|PubMed:24825475, ECO:0000269|PubMed:26439398, ECO:0000269|PubMed:26822476, ECO:0000269|PubMed:28659595}. | Mus musculus (Mouse) |
A2AS55 | ANR16_MOUSE | MALPGDPRRLCRLVQEGRLRDLQEELAVARGCRGPAGDTLLHCAARHGRQDILAYLVEAWSMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLDVIQDLVEHGANPLLKNKDGWNSFHIASREGHPVILRYLLTVCPDAWKTESNIRRTPLHTAAMHGCLEAVQVLLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLEQHKACSSAADSMGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALHYAAKEGQTNTVQTLLSLGADINSTDERNRSVLHLACAGQHVACTRLLLQSGLKDSEDLTGTLAQQLTRSVDILQDFDHDVKS | null | null | tRNA modification [GO:0006400] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF12796;PF13637; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29769718}. Nucleus {ECO:0000269|PubMed:29769718}. | null | null | null | null | null | FUNCTION: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity (PubMed:29769718). Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides (PubMed:29769718). {ECO:0000269|PubMed:29769718}. | Mus musculus (Mouse) |
A2AS89 | GDAH_MOUSE | MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVVGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV | 3.5.3.-; 3.5.3.1; 3.5.3.17; 3.5.3.7 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; | putrescine biosynthetic process from arginine, using agmatinase [GO:0033389]; urea cycle [GO:0000050] | mitochondrion [GO:0005739] | agmatinase activity [GO:0008783]; arginase activity [GO:0004053]; guanidinobutyrase activity [GO:0047971]; guanidinopropionase activity [GO:0047972]; metal ion binding [GO:0046872] | PF00491; | 3.40.800.10; | Arginase family, Agmatinase subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-guanidinopropanoate + H2O = beta-alanine + urea; Xref=Rhea:RHEA:16029, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:57593, ChEBI:CHEBI:57966; EC=3.5.3.17; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16030; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; CATALYTIC ACTIVITY: Reaction=4-guanidinobutanoate + H2O = 4-aminobutanoate + urea; Xref=Rhea:RHEA:19501, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:57486, ChEBI:CHEBI:59888; EC=3.5.3.7; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19502; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; CATALYTIC ACTIVITY: Reaction=H2O + taurocyamine = taurine + urea; Xref=Rhea:RHEA:75931, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58064, ChEBI:CHEBI:507393; EC=3.5.3.17; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75932; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20570; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; | null | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9BSE5}. | null | null | FUNCTION: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency. {ECO:0000250|UniProtKB:Q9BSE5}. | Mus musculus (Mouse) |
A2ASI5 | SCN3A_MOUSE | MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFEINTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRPEGDRFPKSESEDSVKRRSFLFSLDGNPLSGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRAMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDSWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINEDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDYVKNKIRECFRKAFFRKPKVIEIHEGNKIDSCMSNNTGVVEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNMTTGSMFDMSEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPVYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISNTYDKETIKGRIVLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEV | null | null | behavioral response to pain [GO:0048266]; cellular response to antibiotic [GO:0071236]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; response to pyrethroid [GO:0046684]; sodium ion transmembrane transport [GO:0035725] | axon [GO:0030424]; basal plasma membrane [GO:0009925]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; sarcoplasm [GO:0016528]; voltage-gated sodium channel complex [GO:0001518] | calmodulin binding [GO:0005516]; sodium channel activity [GO:0005272]; sodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.3/SCN3A subfamily | PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.; PTM: Phosphorylation at Ser-1453 in a highly conserved cytoplasmic loop slows inactivation of the channel and reduces peak sodium currents. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Basal cell membrane {ECO:0000269|PubMed:29142310}. Note=In enterochromaffin cells, localized highly asymmetrically, almost exclusively at the basal side. {ECO:0000269|PubMed:29142310}. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:29142310). May contribute to the regulation of serotonin/5-hydroxytryptamine release by enterochromaffin cells (PubMed:29142310). In pancreatic endocrine cells, required for both glucagon and glucose-induced insulin secretion (PubMed:25172946). {ECO:0000269|PubMed:25172946, ECO:0000269|PubMed:29142310}. | Mus musculus (Mouse) |
A2ASQ1 | AGRIN_MOUSE | MPPLPLEHRPRQQPGASVLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTAAPSMPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPCDQTPSPCRGAQCAFGATCTVKNGKAVCECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPCDRCGQCRFGSLCEVETGRCVCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHCQTCGETVCTFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPCEPAECGSGGSGSGEDNACEQELCRQHGGVWDEDSEDGPCVCDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQELYVAAQGACRGPTLAPLLPMASPHCAQTPYGCCQDNVTAAQGVGLAGCPSTCHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGHSGCTPCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDGQALGHLGCEADPTTPVTCVEMHCEFGASCVEEAGFAQCVCPTLTCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPCRESVAPGVSPTSASMTTPRHILSRTLASPHSSLPLSPSTTAHDWPTPLPTSPQTVVGTPRSTAATPSDVASLATAIFRESGSTNGSGDEELSGDEEASGGGSGGLEPPVGSVVVTHGPPIERASCYNSPLGCCSDGKTPSLDSEGSNCPATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFDPTTAFQAPDVGQALLQQIQVSRPWALAVRRPLREHVRFLDFDWFPTFFTGAATGTTAAVATARATTVSRLSASSVTPRVYPSYTSRPVGRTTAPLTTRRPPTTTASIDRPRTPGPQRPPKSCDSQPCLHGGTCQDLDSGKGFSCSCTAGRAGTVCEKVQLPSVPAFKGHSFLAFPTLRAYHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATVLDRTSVGIGLKGCIRMLDINNQQLELSDWQRAVVQSSGVGECGDHPCSPNPCHGGALCQALEAGVFLCQCPPGRFGPTCADEKNPCQPNPCHGSAPCHVLSRGGAKCACPLGRSGSFCETVLENAGSRPFLADFNGFSYLELKGLHTFERDLGEKMALEMVFLARGPSGLLLYNGQKTDGKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVLGESPKSRKVPHTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLLTQEHVLRAVDVAPFAGHPCTQAVDNPCLNGGSCIPREATYECLCPGGFSGLHCEKGIVEKSVGDLETLAFDGRTYIEYLNAVTESELTNEIPAPETLDSRALFSEKALQSNHFELSLRTEATQGLVLWIGKVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQKLPVGQALPKAYGTGFVGCLRDVVVGHRQLHLLEDAVTKPELRPCPTL | null | null | cell differentiation [GO:0030154]; chemical synaptic transmission [GO:0007268]; circadian rhythm [GO:0007623]; enzyme-linked receptor protein signaling pathway [GO:0007167]; motor neuron apoptotic process [GO:0097049]; negative regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903407]; negative regulation of sodium ion export across plasma membrane [GO:1903277]; neuromuscular junction development [GO:0007528]; plasma membrane organization [GO:0007009]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of motor neuron apoptotic process [GO:2000673]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein binding [GO:0032092]; positive regulation of protein geranylgeranylation [GO:2000541]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein transport [GO:0015031]; receptor clustering [GO:0043113]; regulation of axon guidance [GO:1902667]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of cardiac muscle contraction [GO:0055117]; regulation of GTPase activity [GO:0043087]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of protein phosphorylation [GO:0001932]; regulation of synapse organization [GO:0050807]; regulation of synaptic activity [GO:0060025]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]; synapse assembly [GO:0007416] | axonal growth cone [GO:0044295]; basement membrane [GO:0005604]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; sarcolemma [GO:0042383]; synapse [GO:0045202]; synaptic cleft [GO:0043083] | acetylcholine receptor regulator activity [GO:0030548]; ATPase inhibitor activity [GO:0042030]; BMP binding [GO:0036122]; calcium ion binding [GO:0005509]; chondroitin sulfate binding [GO:0035374]; dystroglycan binding [GO:0002162]; heparan sulfate proteoglycan binding [GO:0043395]; receptor ligand activity [GO:0048018]; sialic acid binding [GO:0033691]; transforming growth factor beta binding [GO:0050431]; transmembrane transporter binding [GO:0044325] | PF00008;PF00050;PF07648;PF00053;PF00054;PF01390; | 2.60.120.200;3.30.60.30;2.10.25.10;3.30.70.960; | null | PTM: Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity). Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. {ECO:0000250}.; PTM: At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ). Cleavage is developmentally regulated. In developing brain, neurotrypsin-mediated cleavage occurs mainly during late fetal days and in the first postnatal week. {ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:21885656}. | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:8653787}. Cell membrane {ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480}; Single-pass type II membrane protein {ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480}. | null | null | null | null | null | FUNCTION: [Isoform 1]: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; FUNCTION: Isoform 2 and isoform 3: these isoforms lacking the 'z' insert (z0) are muscle-specific, have no AChR clustering ability and may be involved in nervous system endothelial cell differentiation.; FUNCTION: [Agrin N-terminal 110 kDa subunit]: Involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:21885656, ECO:0000269|PubMed:8653787}.; FUNCTION: [Agrin C-terminal 22 kDa fragment]: This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. | Mus musculus (Mouse) |
A2ASS6 | TITIN_MOUSE | MTTQAPMFTQPLQSVVVLEGSTATFEAHVSGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLVTAETAPPNFSQRLQSMTVRQGSQVRLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELVVQGEEVVPAKKTKTIVSTAQISETRQTRIEKKIEAHFDARSIATVEMVIDGATGQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAGRISTSPIRSVKSPLLIRKTQTTTMATGPEVPPPWKQEGYVASSTEAEMRETTMTSSTQIRREERWEGRYGVQEQVTISGAAAAAASASVSSSFTAGAITTGTKEVKQETDKSAAVATVVAAVDMARVREPAISAVEQTAQRTTTTAVHIQPAQEQARKEAEKTAVTKVVVAADKAKEQELKSRTREVMVTTQEQTHISHEQIRKETEKAFVPKVVISATKAKEQETRITGEITTKQEQKRITQETIRQETEEIAASMVVVATAKSTKLEAAVGVQEETAIQQDQMHLTHEQMMKETRKTVVPKVIVATPKIKEQDLVSRSREAITTKRDQVQITQEKKRKEVETTALSTIAVATAKAKEQETVLRSREAMATRQEHIQVTHGQVGVGKKAEAVATVVAAVDQARVREPREPTHVEESHSQQTTLEYGYKEHISTTKVPEQPRRPASEPHVVPQAVKPAVIQAPSETHIKTTDQMGMHISSQVKKTTDISTERLVHVDKRPRTASPHFTVSKISVPKTEHGYEASIAGSAIATLQKELSATSSTQKITKSVKAPTVKPGETRVRAEPTPSPQFPFADMPPPDTYKSQAGIEVKKEVGVSISGSTVREEHFEVLRGREAKVTETARVPAPAEVPVTPPTLVSGLKNVTVIEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQGGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQVSEEFDKETTLTEKFATEEKRFVESRDVVMTDTSITEEQAGPGEPAAPFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRNKHGETSASASLLEEADYEALVKTQQEMLYQTQMSTFIQEPKVGEIAPGFAYSEYEKEYEKEQALIRKKMAKDTVMVRTFVEDQEFHISSFEERLIKEIEYRIIKTTLEELLEEDGEEKMAVDISESEAIESGFDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRHGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYVEPAAPFSAPTYMPTPEAVSRIRSVSPRSLSRSPIRMSPAMSPARMSPARMSPARMSPARMSPGRRLEETDESQLERLYKPVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPASPSDSGEWTVVAQNRAGKSTISVTLTVEAVEHQIKPAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTRGEAALKIDSIISQDSAWYTATAINKAGRDTTRCKVNVEVEFAEPEPERKLIIPRGTYRAKEIAAPELEPLHLRYGQEQWEEGDLYDKEKQQKPFFKKKLTSLRLKRFGPAHFECRLTPIGDPTMVVEWLHDGKPLEAANRLRMINEFGYCSLDYGAAYSRDSGVITCRATNKYGTDHTSATLIVKDEKSLVEESQLPDGKKGLQRIEELERMAHEGALTGVTTDQKEKQKPDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEGVTEHKVKLEIQQREDFRSVLRRAPEPKPEFHVHEPGKLQFEVQKVDRPVDTSETKEVVKLKRAERITHEKVSEESEELRSKFKRRTEEGYYEAITAVELKSRKKDESYEELLKKTKDELLHWTKELTEEEKKALAEEGKITIPTFKPERIELSPSMEAPKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLLVQAKQLITFTQELQDVVAKEKDTMATFECETSEPFIKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCVLVEDENIKTTAKLIVEGAVVEFVKELQDIEVPESYSGELECIISPENIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEYSFVVDGKKTTCKLKMKPRPIAILQGLSDQKVCEGDIVQLEVKVSLENVEGVWMKDGQEVQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGNVSVYSVDVITPLKDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMVGRVETSCNLSVEKIKIIRGLRDLTCTETQNVVFEVELSHSGIDVVWNFKGKEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYAGENTTSGKLTVAGGAISTPLTDQTVAESQEAVFECEVANPESEGEWLKDGKHLALSNNFRGESDGHKRRLVIAAAKLDDAGEYTYKVATSKTSAKLKVEAVKIKKTLRNLTVTETQDAVFSVELTHPDVKGVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFKLGRLGASARLHVETVKIIKKPKDVTALENATVTFEVSVSHDTVPVKWFHKNVEIKPSDKHRLVSERKVHKLMLQSISPSDAGEYTAMVGQLECKAKLFVETLHITKTMKSIEVPETKAASFECEVSHFNVPSMWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGNDQVSATLTVTPIMITSMLKDINAEEKDTITFEVTVNYEGISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVAGKATSTATLYVEARHIEFRKHIKDIKVLEKKRAMFECEVSEPDITVQWMKDGQELQIADRIKIQKEKYVHRLLIPSTRMSDAGKYTVVAGGNMSTANLFVEGRDVRIRSIKKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVQERHQYVVERRIHRMFISETRHSDAGEYTFVAGRNRSSVTLYVNAPEPPQVLQELQPVTVQSGKPARFCAVISGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLSVEVPEVVSPDQEMPVYPPAIVTPLQDTVTSEGRPARFQCQVSGTDLKVSWYCKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYAFVANNAVGQVSSTATLRLEAPESILHERIGQQIEMEMKEIASLLSAEEDFQTYSSDLRLPNANETLELLSEPPARSTQFDSRQEGAAPVFIREISDVEISVEDVAKLSVTVTGCPKPKIQWFFNGMLLTPSADYKFVFDGDTHSLIILFTRFQDEGEYTCLASNEYGKAVCSAHLRISPRGERSTEMESGEKKALEKPKGPCPPYFFKELKPVHCGPGIPAVFEYSVHGEPAPTVLWFKEDMPLYTSVCYTIIHSPDGSGTFIVNDPQRGDSGLYLCKAQNLWGESTCAAELLVLPEDTDVPDASCKEESTLGVPGDFLETSARGPLVQGVDSRQEITAFAEGTISKAALIAEETLQLSYERSVDDSEVGTGVTIGAQKLPPVVLSTPQGTGELPSIDGAVHTQPGRGPPPTLNLQAVQAQTTLPKEATLQFEEPEGVFPGASSAAQVSPVTIKPLITLTAEPKGNYPQSSTAAPDHALLSSVAAETLQLGEKKIPEVDKAQRALLLSQSLAEGCVESLEVPDVAVSNMRSEPQVPFQHTCTEGKILMASADTLKSTGQDVALRTEEGKSLSFPLALEEKQVLLKEEQSEVVAVPTSQTSKSEKEPEAIKGVKEVREQELLSKETLFPSMPEEQRLHLKTQVRRALQAAVAREQANLFSEWLRNIDKVEVTAVNFTQEPKRILCTYLITSVSSLTEELTVTIEDIDPQMANLETGLKDALCSIVCEERNILMAEDPRIHEEDKIDVQGGRDHLSDAQKVETVIEAEADSKYLVSKEEVSWSKVESQLKDGDTNEVPQAETLKLAEESGTQKTSTEMSQEEAEGTLADLCPAVLKHLVDTISEEGDTVHLTSSISNAKEVHWYFKGNLVPSDGKFKCLKEQNAYTLVIEAVKTEDEGEYVCEASNDSGKAKTSAKLTVGERAAPVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYVSSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKALTTFVGKAAKFLCTVSGTPVIEIIWQKDGAALSPSPDCRVTDADNKHSLELSNLTVQDRGIYSCKASNKFGADICQAELTIIDKPHFIKELEAVQSAINKKIHLECQVDEDRKVTITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYTCTASNEAGSSSSSAAVAVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFVNSEAILDITDVKVDDSGTYSCEATNDVGSDSCSTEVVIKEPPSFIKTLEPADIVRGANALLQCEIAGTGPFEVNWFKDKKQIRSSKKYRLFTQKTFVYLEISSFNSADVGDYECVVANEVGKCGCVATHLLKEPPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSNGVAVLTIPDVQISLGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKELTASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSRDVLPGSAVCLKSAFQGSAPLTIKWFKGDKELVSGGSCYITKETSESSLELYAVKTSDSGTYTCKVSNVAGSVECSADLFVKEPATFIEKLEPSQLLKKGDGTQLACKVTGTPPIKITWFANDRELRESSKHKMSFAESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTGIVIVKESPYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFLQDQLVSLQVLKFVAADAGEYQCRVTNEVGSSTCSARVTLREPPSFIKKIEATSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATIMEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASINVLDLIIPPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKHKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTVKEPPYFVEKPQSQDVNPGTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSKATIFVKEPPQFIKKPSPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRKYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKVKEPPIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCDPSDVGEYQCIIANEGGSCACSARVALKEPPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGIERCYAFLLVQEPAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQDIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILTVKEPPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDSSKTGQYTCQVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIIKAGDSARLECKITGSPEIQVVWYRNEHELTASDKYQMTFIDSVAVIQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKVASKNFHASIHILNVESTDIGEYHCKAQNEVGSDACVCAVKLKEPPKFISKLNSLTVVAGEPAELQASIEGAQPISVQWLKEKEEVIRESENIRISFVNNVATLQFAKVEPANAGKYICQVKNDGGVRENMATLTVLEPAVIIEKAGSMTVTVGETCALECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVDVSDRMVPPSFTRRLKDTGGVLGTSCILECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTVQEPPSFVKEPEPLEVLPGKNITFTSVIRGTPPFKVGWFRGARELVKGNRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPATFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVSITPSERCNIVTTEKTCILEILSSTKGDAGHYSCEIENEAGRDACDALVSTLEPPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVSINDSGEYTCMAENSIGTAASKTIFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSTARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFIKKLDASKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASAEDTGDYICEAHNGVGDASCSTALKVKAPPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKITSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTVKFKEPPRFVKKLSDASTLIGDPVELQAVVEGFQPISVVWLKDKGEVIRESENVRISFVDNIATLQLGSPEASQSGKYVCQIKNDAGMRECSAVLTVLEPATIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWFKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYTFEVENRVGKSSCTVSVHVSDRVVPPSFVRRLKDTSATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQSSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVSGEACTISLEDFVTELELLEVEPGQSGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADTSVETGSPIVLEATYSGTPPISVSWMKNEYPLSQSPNCGITTTEKSSILEILESTIEDYAQYACLIENEAGQDICEALVSVLEPPYFIEPLEHVEAAIGEPITLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAVLVIKERKLPPSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGELLKDDANLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGVQEPPRFIKKLDQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHSLSVEDSGDYTCEARNAAGSASSSTSLKVKEPPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWHKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVGSVTMKAPPQFVKKLTDISTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISYSENIATLQFSRAEPANAGKYTCQIKNDAGMQECYATLSVLEPAAIVEKPESIKVTTGDTCTLECTVSGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVVPGDSGVYSFEVQNPVGKDSCKVSIQVSDRIIPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVLWFHDGNEISSGRKYQTTLTDNTCALTVNMLEEADAGDYTCIATNVAGSDECSAPLTVREPPSFVQKPDPMDVLTGSNVTFTSIVKGSPPFTVSWFKGSTELVPGARCNVSLQDSVGELELFDVDTSQSGEYTCIVSNEAGRASCTTRLFVKAPAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGINVIASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTATCKMHFKNNVATLVFTQVDSSDSGEYICRAENSVGEVSSSTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNIQTSFLDNIATLNIFKTDRSLSGQYSCTATNPIGSASSGAKLILTEGKNPPFFDIPLAPMDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKKLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNVEIHPTSNCEIMFKNNALLLQVKRASMADAGLYTCKATNDAGSALCTSSIVIKEPKKPPVFDQHLAPVTASEGDSVQLSCHVQGSEPIRIQWLKAGREVKPSDRCSFSFASGTAMLELKETAKADSGDYVCKASNVAGSDTSKCKVTIKEKPAAAPAAKKAAVDGKLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGDEAKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPALKKGSGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEELEKSERDEKEFEELVAFIQQRLTQTEPVTLIKDIENQTVLKDNDAIFEIDIKINYPEIKLSWYKGTEKLEPSNKYEISIDGDRHTLRVKNCQPKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTCQFSVPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGQYTCKHEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLEMKPPDIPDSRVPIPTMPIRAVPPEEIPPAVAPSIPLLLPLPEEKKPPAKRIEVTKKGVKKDTKKVVTKPKEEAPPPPVAKKPPPPTPMIPAKASEIIDVSSKAEEVKITTITRKKEVHKEKEAVYEREEAVYEKKVHIEPWEEPYEELETEPYTEPYEEPYYEEPDEDYEEIKVEAKKQVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEIYHEREIIQVQKEVHEELHEKKIPAKVPEKKVPPPKVVKKPVVEKVEKTTRRMEEEKVQVIKVPEVSKKIVPQKPSRTPVQEEIIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVSVPEVQKKTVTEEKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAAKVPEAPKKPVPEEKKPVPIPKKKEPAAPPQVPEAPKKPAPEEKIPVPVTKKKEAPPAKVPEVQKKVVTEEKIAIITQREESPPPAVPEIPKKKVPEEKRPVPRKEEVPPPKVPVPPKKAVPEAVVPAPIPKKAPPRAEVSKKTVVEEKRFAAEEKLSVAVPQRVELMRHEEEEWTYSEEEERVSVSVYREEERDEEEAEITEYEVLEEPEEYVVEEKMHFISKKVEVEPAKVPEKKIIPKPKVPAKIEEPPPTKVPEPPKKIVPEKKVPAPAPKKVPPAKAPEESKRPVPEKRAPAEEVGIEEPPPTKVAERHMKITQEEKVLVAVTKKEAPPRARVPEEPKKVAPEERFPKLKPRREEEPPAKVTEVRKRAVKEEKVSIEVPKREPRPTKEVTVTEEKKWSYTREEETVSEHREEEYEDYEDYEEYKEFEEYEPTEEYDQYDEYAEREVEHYEEHEEYVTEPKKPVPVKPAQEPVPAKPKAPPPKVLKKAVPEEKAPLPIQKKLKPLPPKAPEEPKKVVEEKIQISITKREKQQVTEPVAKVPMKPKRVVPEAKIPAPTKEVAVPVRVPGVPKKRELEEVVVFKEEVEAHEEYIVEEEEEYVHEEEYVHKEEYVHEEEYVHKEEYIHEEEEHLHEEEETIAEEEVVPVAPVKVPVVPKKPVPEEKKPVPVPKKKEAPPAKVPEIPKKPEEKVPVPIPKKEKAPPAKVPEVPKKPVPEEKPPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKVEAPPAKVPEVPKKPIPEEKKPTALLKKMEAPPPKAPKKREVVPVPVALPREEEEEEVPFEEVPEEEILPEEEVPSEEEAPPEEVPPEEEEVLPEEEEVLPEEEEVLPEEEEVQPEEEALPEIKPKVPKPAPVPKKTVPEKKVPVPVPKKVEPPPPPKVPEIKKKVPEKKVVVPKKEEAPPTKVPEVSKKVEERRIIPPKEEEVPPAEVYEEAEEPTPEEIPEEPPSIEEEEIVEEEEEEEEVLPPRAPEVVKKAVPEAPTPVPKKAEAPPAKVPKKIPEEKVPVPVQKKEAPPAKVPEKKKIPEKKVPVPKKEAVPPAKGKAVFEEKISVAYQQEELVQERIELELVEAKVEEAFEEEEFHEVQEYFEEEEFHEVEEFIRVEERRFQEEHKVEEVHRVIEFLEAEEVEVYEKPKIPPKKGPEVSEKVIPPKKPPTKVIPRKEPPAKVPEVTKKTVVEEKIRAPEEPKVPAPKAPEVPKKITPEEKVREAVPKKPEVPPPKVPEVPKKIIQEEKLPVVLPEDTEIYMYEASEETVIEEEHVTLPQKARLKVAKVPAPPQTVVTEEKTYVTIRKTRETLALKESETTREAFPELKSYKAVPEIPEPPSPEDLEIIEDVLPEKRPPASKRRKTQLPTAPEAPREMPPEMNTFEEISVEPEMLPTQVLDTYQEATVEKKTLRISRKKPELPSDEEVPEAPREVVAKKKVLPPQVPEVVPVKVPGAPKEVVSERKSLEEPPKKPAVRPVTVPEEPKEVIPEKKVSLVPPKKPAAPPVTVPEAPEEVFSEDEETLAPPQEPEAPPAKVPEAPKEVVPEKKVSVVPPKKPEAPPAKVPEAPKEAAPEKKVPVAPKKKPEAPPVKVPEAPKKVVPEKKLPVAAPKKPEAPAAEVPEVPKTAVPQKKIPEAIPPKPESPPLEVPEVPPKEVTPEKKVPAAPPTKPEIPPPKVPEAPQAAVVEEKTPEALPKKAEAAPVPVPQVQETVPEKTRPVGPPKKPEATTVPVPKVQKTIPEKTRPEAPPKRPEARTVPETVPEKTRPMAPPKKPEATTLPVPEVQETVPEKTRPVGPPKKPEATTVPVPEVQETIPEKTRPPKKPEATPVPVPEVQETVPEKTRPVGPPKKPEATTVSVPEVQETIPEKTRPAAPPKKPEATAVPETIPEKTRPEAPPKRPEATTVPVPEADQAVVPEKKVPRVPPKKVEAPPITVPEEPKEVIPEKKVSLVPPKKPAAPPVTVPEAPEEVFSEDEETLAPPQEPEAPPAKVPEAPKEVVPEKKVSVVPPKKPEAPPAKVPEAPKEAAPEKKVPVAPKKKPEAPPVKVPEAPKKVVPEKKLPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEAIPPKPESPPPEVYEEPEEEIVPEEPPEEAVEEPVPAPPPKVTEPPKKPVPEKKAPPAVVKKPEPPPAKVPEVPKEAPPEKKVPPKKPEAPPAKVPEVPKEVVTEKKVAVPKKPEVPPAKVPEVPKKPVIEEKPAIPVVEKVASPPAEVYEEPEEVTAEEEEPAPAVEEEEYEAPPPPAPVPEEPKKVVPEKKFPVIKKPEAPPPKVPEVPKKAVPVKKVPVVKKPEPPEAEVPEVPKKLVPVKKEPVPVTKKTEVLPEKVPEAPKKITPEKKESVPVPEEPEAPPASVEETPEETIYEEKATITIGRKETPPVEEREIEKFIQPEEPELEPEPEEIPVQEPEPEKKVIEKPKLKPRPPARPPSPPKEDVKEKMFQLKAVSKKKVPEKPEVVEKVEPAPLKVPTAEKKVRKLLPEPKPQPKEEVVLKSVLRKKPEEEEPKVEPKKVEKAKKPEEPQPPPKAVEVEAPPEPTPKERKVPEPAKVPEIKPAIPLPGPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPKGPIKGVAKKTPSPIEAERKKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIVLTEAESVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLIVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENANNLECSSCVKVVEIIREWLVKPIRDQHVKPKGTAVFTCDIAKDTPNIKWFKGYDEIPLEPNDKTEILKEGNHLFLKVKNAMPEDIDEYAVEIEGKRYPAKLTLGEREVELLKPIEDVTIYEKESASFDAEISEEDIPGEWKLKGELLRPSPTCEIKAEGGKRFLTLHKVKLDQAGEVLYQACNAITTAILTVKEIELDFAVPLKDVTVPEKRQARFECVLTREANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYTAEVEGKKTSAQLFVTGIRLKFISPLEDQTVKEGQTATFVCELSHEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKNLSSTANLKVLEADPYFTVKLHDKTGVEKDEIILKCEVSKDVPVKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYVCDCGTDTTKANVTVEARLIKVEKPLYGVEVFVGETARFEIELSEPDVHGQWKLKGEPLTASPDCEIIEDGKKHVLVLYNCQLDMTGEISFQAANAKSAANLKVKELPLIFITPLSDVKVFEKDEAKFECEVSREPKTFRWLKGTQEITGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDKRTSGKLIIEGIRLKFLTPLKDVTAKERENAVFTVELSHDNIPVSWFKNDQRLHTSKRVSMHDEGKTHSITFKDLSIDDTSQIRVEAMGISSEAKLTVLEGDPYFTGKLQDYTGVEKDEVILQCEISKADAPVKWFKDGKEIKPSKNVVIKADGKKRMLILKKALKSDIGQYTCDCGTDQTSGKLDIEDREIKLVRPLYSVEVMETETARFETEISEDDIHANWKLKGEALLQTPECEIKEEGKIHVLILHNCRLDQTGGVDFQAANVKSSAHLRVKPRVIGLLRPLKDVTVTAGETATFDCELSYEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAKDFKTQANLFVKEPPVEFTKPLEDQTVEEEATAVLECEVSRENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKDFKTSCNLNVVPPHVEFLRPLTDLQVKEKETARFECEISKENEKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVRTARTSGMLTVLEEEAVFTKNLANLEVSEGDTIKLVCEVSKPGAEVIWYKGDEEIIETGRFEILTDGRKRILIIQNAQLEDAGSYNCRLPSSRTDSKVKVHELAAEFISKPQNLEILEGEKAEFVCTISKESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMVGAARAAAHLTVIEKLRIIVPLKDTKVKEQQEVVFNCEVNTEGAKAKWFRNEEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFNVSLTNHRGENVKSAANLIVEEEDLRIVEPLKDIETMEKKSVTFWCKVNRLNVTLKWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYVVTAGQDKSVAELLIIEAPTEFVEHLEDQTVTEFDDAVFSCQLSREKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDRKSRARLFVEEIPVEIIRPPQDILEAPGADVIFLAELNKDKVEVQWLRNNMIVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDKEARAKLELAAAPKIKTADQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKTVDTTAEQTSFRISEAKKDDKGRYKIVLQNKHGKAEGFINLQVIDVPGPVRNLEVTETFDGEVSLAWEEPLTDGGSKIIGYVVERRDIKRKTWVLVTDRADSCEFTVTGLQKGGVEYLFRVSARNRVGTGEPVETDSPVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRIGVGKPSAATPFVKVADPIERPSPPVNLNASEQTQSSVQLTWEPPLKDGGSPILGYIIERREEGKDNWIRCNMKPVPELTYKVTGLQKGNKYLYRVSAENAAGVSDPSEILGPLTADDAFVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYPRPKATWTFGDQVLEEGDRVKMKTISAYAELVISPSERTDKGIYTLTLENPVKSISGEINVNVIAPPSAPKELKFSDITKDSVHLTWEPPDDDGGSPLTGYVVEKRDMSRKTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKCGPGEPAYTDEPVNMSAPATVPDPPENVKWRDRTANSIFLTWDPPKNDGGSRIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQGASKPSKPTEEIQAVDTQEAPEIFLDVKLLAGITVKAGTKIELPATVTGKPEPKITWTKADTLLKPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYVVERKATDSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENMYGVGEPVQAAPIIAKYQFDPPGPPTRLEPSDITKDAVTLTWCEPDDDGGSPITGYWVERLDPDTDKWVRCNKMPVKDTTYRVKGLTNKKKYRFRVLAENLAGPGKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNWTKPEHDGGAKIESYVIEMLKTGTDEWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAGESEPSEPSDPVLCREKLYPPSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENAIGQSDYTEIGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENEAGVGHPSEPTEILSIEDPTSPPSPPLDLHVTDAGRKHIAIAWKPPEKNGGSPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVEEGIVPDKEYVLRVRAVNAVGVSEPSEISENVVAKDPDCKPTIDLETHDIVVIEGEKLNIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVKVIGLPGPCKDIKASDITKSSCKLTWEPPEFDGGSPILHYVLERREAGRRTYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKIGGGEYIELKNPVIAQDPKQPPDPPVDVEVHNPTAKAMTITWKPPLYDGGSKIMGYIIEKITKGEDRWKRCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGIGEPSRATPPTKAVDPIDAPKVILRTSLEVKRGDEIALDATISGSPYPTITWIKDENVIVPEEIKKRAAPPVRRKKGEAEEEEPFSLPLTERLSINNSKQGESQLRIRDSLRPDHGQYMIKVENDHGVAKAPCSVSVLDTPGPPINFVFEDIRKDSVLCKWEPPLDDGGSEIINYTLEKKDKTKPDSDWIVITSTLRNCKYSVTKLIEGKEYLFRVRAENRFGPGPPCVSKPLLAKDPFEPPDAPDKPIVEDVTSNSMLVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKTLLSSLKTKVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTARDPISPPGPPVPRVADTSSTTIELEWEPPAFNGGGEIMGYFVDKQLVGTNEWSRCTEKMIKVRQFTVKEIREGADYKLRVSAVNAAGEGPPGETEPVTVAEPQEPPTVELDVSVKGGIQIMAGKTLRIPAEVTGRPVPTKVWTIEEGELDKERVIIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAVRVEVFDVPGPVLDLKPVVTNRKMCLLNWSDPADDGGSDITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKFGCGPPVEIGPILAVDPLGPPTSPERLTYTERTKSTITLDWKEPRSDGGSPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVENLDEHQMYEFRVKAVNDVGESEPSLPLNVVIQDDEVPPTIKLRLAVRGDTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIDKPTDTLNITKEEVSRSEAKTELSIPKAAREDKGTYTITASNRLGSVFRNVHVEVYDRPSPPRNLAVTDIKAESCYLTWDAPLDNGGSEITHYIIDKRDASRKKSEWEEVTNTAVERRYGIWKLIPNGQYEFRVRAVNKYGISDECKSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGGSPITGYWLEKREEGGTYWSRVSRAPITKVGLKGVEFNVPRLIEGVKYQFRAMAINAAGIGPPSEPSDPAVAGDPIYPPGPPSCPEVKDKTKSSISLAWKPPAKDGGSPIKGYIVEMQEEGTTDWKPVNEPDKLLTACECVVPNLKELRKYRFRVKAVNEAGESEPSDTTGEIPATDIQEVPEVFIDIGAQDCLVCKAGSQVKIPAVIKGRPTPKSSWEFDGKAKKAMKDGVHDIPEDAQLETAENSSVIIIPECTRAHSGKYSITAKNKAGQKTANCRVKVMDAPGPPKDLKVSDITRGSCRLSWKMPDDDGGDRIKGYVIEKKTIDGKAWTKVNPNCGSTTFVVPDLISEQQYFFRVRAENRFGIGPPAETIQRTTARDPIYPPDPPIKLKIGLITKNTVHLSWKPPKNDGGSPVTHYIVECLAWDPTGKKKEAWRQCNRRDVEELEFTVEDLIEGGEYEFRVKAVNEAGVSKPSATVGPVIVKDQTCPPAIELKEFMEVEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGGSKITNYVIEKREANRKTWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQNKYGIGEPLDSEPETARNLFSVPGAPDKPTVSSVTRNSMTVNWEEPEYDGGSPVTGYWLEMKDTTSKRWKRVNRDPIKAMTLGVSYKVTGLIEGSDYQFRVYAINAAGVGPASLPSDPVTARDPVAPPGPPFPKVTDWTKSSVDLEWSPPLKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNVAGVGEPGEVTDVIEMKDRIVSPDLQLDASVRDRIVVHAGGVIRIIAYVSGKPPPTVTWSMNERALPQEAAIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIVDVLDVPGPVGIPFLSDNLTNDSCKLTWFSPEDDGGSPITNYVIQKREADRRAWTPVTYTVTRQNATVQGLIQGKSYFFRIAAENSIGMGPFVETPNALVIRDPITVPERPEDLEVKEVTKNTVSLTWNPPKYDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGKPSFCTKPITCKDELAPPTLDLDFRDKLTVRVGESFALTGRYSGKPKPKIDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGKYCVVVENSTGSRKGFCQVNVVDRPGPPVGPVIFDEVTKEYMVISWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAENLYGISDPLVSDSMKAKDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIHPYTKYRVPDLLEGCQYEFRVSAENEIGIGDPSPPSKPVFARDPIAKPSPPINPEAIDTTCNSVELTWQPPRHDGGSKILGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQSYKFRVLAVNEAGESDPAHVPEPVLVKDRLEPPELILDANMAREQHIRVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGTKTVSVKVLVLDKPGPPRDLEVSEIRKDSCYLTWKEPLDDGGSVVTNYVVERKDVATAQWSPLSTTSKKKSHMAKHLTEGNQYLFRVAAENQYGRGPFVETPKPIKALDPLHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGGSPITGYLVEYQEEGDKDWIKFKTVKNLDCVVTGLQQGKTYRFRVKAENIIGLGLPDTTIPIECQEKLVPPSVELDVKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWTTDGTEIKTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINILDVTPEYMTISWQPPKDDGGSPVINYIVEKQDTRKGTWGVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDSIPTVAKHKFSPPSPPGKPVVTDITENAATVSWTLPKSDGGSPITGYYVERREITGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENLAGLSNPSPSSDPIKACRPIKPPGPPINPKLKDKSKESADLVWTKPLSDGGSPILGYVVEYQKPGTAQWDRINKDELIRQCAFRVPGLIEGNEYRFRIRAANIVGEGEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNVLDRPGPCQNLKVSNVTKENCTISWENPLDNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLVKANLLANNEYYFRVCAENKVGVGPTIETKTPILAINPIDRPGEPENLHIADKGKTFVYLKWRRPDYDGGSPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNEGGESDWVRTEEVVVKEDLQKPVLDLKLSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVITATNPAGSFVAYATVNVLDKPGPVRNLKITDVSSDRCTIRWDPPEDDGGCEIQNYILEKCESKRMVWSTYSANVLTPSATVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTKYDRPGRPDPPEVTKVSKEEMTVVWNAPEYDGGKSITGYYLEKKEKHAVRWVPVNKSAIPERRLKVQNLLPGHEYQFRVKAENEVGIGEPSLPSRPVVAKDPIEPPGPPTNFKVVDTTKSSITLAWGKPVYDGGAPIIGYVVEMRPKIADASPDEGWKRCNAAAQLIRMEFTVTSLDENQEYEFRVCAQNQVGIGRPAELKEAIKPKEILEPPEIDLDASMRKLVVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVKVLDTPGPVADLKVSDVTKTSCHVSWAPPENDGGSQVTHYIVEKREAERKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNEYGPGVPTDIPKPVLASDPLSEPDPPRKLEVTEMTKNSATLAWLPPLRDGGAKIDGYIISYREEDQPADRWTEYSVVKDLSLIVTGLKEGKKYKFRVAARNAVGVSMPREAEGVYEAKEQLLPPKILMPEQITIKAGKKLRVEAHVYGKPNPICKWKKGDDEVVTSSHLAIHKADGSSVLIIKDVTRKDSGYYSLTAENSSGSDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWHIPLEDGGSNITNYIVEKCDVSRGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMLAKFPFDVPSEPKNARVTKVNKDCIFVAWDRPDSDGGSPITGYLIERKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPVDPPGKPEVVDVTKNSASLIWARPKHDGGSRIIGYFVEACKLPGDKWVRCNTTPHQIPQEEYTATGLEENAQYQFRAIAKTAVNISQPSEPSDPVTILAENVPPRIELSVEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDTTPIKQAEGIKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGPPASVKINKMYADRAMLSWEPPLEDGGSEITNYIIDKRETSRPNWAQVSATVPITSCTVEKLIEGHEYQFRICAENKYGVGDPILTEPAIAKNPYDPPGRCDPPVISNITKDHMTVSWKAPADDGGSPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAINKAGPGKPSDASKAVYAQDPLYPPGPPAFPKVYDTTRSSVSLSWGKPAYDGGSPIIGYLVEVKRADSDHWVRCNLPEKLQKTRFEVTGLMENTEYQFRVYAVNKIGYSDPSDVPDKHCPKDILIPPEGELDAELRKTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVVKVLDTPGPPVNVTVKEVSKDSAYVTWDPPIIDGGSPIINYVVEKRDAERKSWSTVTTECSKTSFRVSNLEEGKSYFFRVFAENEYGIGDPGETRDAVKASETPGPVVDLKALAITKSSCTIGWKKPRSDGGSRITGYVVDFLTEENKWQRVMKSLSLQYSTKDLKEGKEYTFRVSAENENGEGTPSEIVVVAKDDVVAPDLDLKDLPDLCYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIPTGPIKFDEVTAEAMTLKWGPPKDDGGSEITNYVLEKRDSVNNKWVTCASAVQKTTFRVTRLHEGIEYTFRVSAENKYGVGEGLKSEPIVAKHPFDVPDAPPPPNIVDVRHDSVSLTWTDPKKTGGSPITGYHIEFKERNSLLWKRANKTPIRMKDFKVTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVISVTRNSVTLIWTEPKYDGGHKLTGYIVEKRDLPSKSWMKANHVNVPDCAFTVTDLVEGGKYEFRIRAKNTAGAISAPSESTGTIICKDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPKSSWSRAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKVSVLDVPGPPGPIEISNVSAEKATLTWTPPLEDGGSPIKAYVLEKRETSRLLWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNHYGKGEPVQSEPVKMVDRFGPPGPPGKPEISNVTKNTATVSWKRPTDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPSDASNPVLMKDVAYPPGPPSNAHVTDTTKKSASLAWGKPHYDGGLEITGYVVEHQKVGDDAWIKDTTGTALRITQFVVPDLQTKEKYNFRISAINDAGVGEPAVIPNVEIVEKEVAPDFELDAELRRTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNVRVLDTPGPVLNLRPTDITKDSVTLHWDLPLIDGGSRITNYIVEKREATRKSYSTVTTKCHKCTYKVTGLTEGCEYFFRVMAENEYGVGEPTETTEPVRASEAPLPPDSLNIMDITKNTVSLAWPKPRHDGGSKITGYVIEAQRKGSDQWTHISTVKGLECVVRNLTEGEEYTFQVMAVNSAGRSAPRESRPVIVKEQTMLPELDLRGIYQKLVIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGPYPLTAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWEPPENDGGVPISNYVVEMRQTDSTTWVELATTVIRTTYKATRLTTGVEYQFRVRAQNRYGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGGSPILGYHIERKERNGILWQTVSKALVPGNIFKSTGLTDGIAYEFRVIAENMAGKSKPSKPSEPMFALDPIDPPGKPVPLNITRHTVALKWAKPEYTGGFKITSYVVEKRDLPNGRWLKANFSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAITCRDDLEAPRIMVDVRFKDTITLKAGEAFKLEADVSGRPPPTMEWTKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVKVLDRPGPPEGPLAVSDVTSEKCVLSWLPPLDDGGAKIDHYIVQKRETSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPLESEPVLAVDPYGPPDPPKNPEVTTITKDSMVVCWGHPDSDGGSEIINYIVERRDKAGQRWVKCNKKALTDLRFKVSGLTEGHEYEFRIMAENAAGISAPSATSPFYKACDTVFKPGPPGNPRVLDTSRSSISIAWNKPIYDGGSEITGYMVEIALPEEDEWQVVTPPAGLKATSYTITSLIENQEYKIRIYAMNSEGLGEPALVPGTPKAEERMLPPEIELDADLRKVVTIRACCTLRLFVPIKGRPAPEVKWAREHGESLDKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNVRVLDTPGPPQNLKIKEVTKTSVTLTWEPPLLDGGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKVDQLQEGCSYYFRVLAENEYGIGLPAETAESVKASERPLPPGKITLTDVTRNSVSLSWEKPEHDGGSRILGYIVEMQSKGSDRWATCATVKVTEATITGLIQGEEYSFRVSAQNEKGISDPRQLSVPVIAKDLVIPPAFKLLFNTFTVLAGEDLKIDVPFIGRPPPAVTWHKDDIPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIVLDKPGPPTGPVKMDEVTADSVTLSWEPPKYDGGSSINNYIVEKRDTSTTAWQIVSATVARTTIKACRLKTGCEYQFRIAAENRYGKSTYLNSEPVVAQYPFKVPGPPGTPFVTLASKDSMEVQWHEPVSDGGSKVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAENIVGIGKPSKPSECYAAHDPCDPPGRPEAIIVTRNSVTLQWKKPTYDGGSKITGYIVEKKELPDGRWMKASFTNIIDTQFEVTGLLEDHRYEFRVIARNAAGVFSEPSESTGAITARDEVEPPRISMDPKYRDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKSTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTINVKVLDRPGPPEGPVAISGVTAEKCTLAWKPPLQDGGSDITNYIVERRETSRLVWTLVDANVQTLSCKVLKLLEGNEYIFRIMAVNKYGVGEPLESESLIAKNPFVVPDAPKAPEVTAVTKDSMIVVWERPASDGGSEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLLENHNYEFRVSAENAAGLSEPSPPSAYQKACDPIYKPGPPNNPKVMDVTRSSVFLSWTKPIYDGGCEIQGYIVEKCDVSVGEWTMCTPPTGINKTNLEVEKLLEKHEYNFRICAINKAGVGEHADVPGPVMVEEKLEAPDIDLDLELRKVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGDIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSITWEPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENEYGIGLPARTADPIKVAEVPQPPGKITVDDVTRNSVSLSWTKPEHDGGSKIIQYIVEMQAKNTDKWSECARVKSLDAVITNLTQGEEYLFRVIAVNEKGRSDPRSLAVPIIAKDLVIEPDVRPAFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGMPLKQTTRINVTDSLDLTTLSIKETHKDDGGQYGITVSNVVGQKTAAIEIITLDKPDPPKGPVKFDEISAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESEPVVAQYPYKEPGPPGTPFVTAISKESMVVQWHEPINNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKALNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDPCDPPGTPEAIIVKRNEITLQWTKPVYDGGSMITGYIVEKRDLPEGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSDSTGPITAKDEVELPRISMDPKFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVKVLDRPGPPEGPVQVTGVTAEKCTLAWSPPLQDGGSDISHYVVEKRETSRLAWTVVASEVVTNSLKVTKLLEGNKYIFRIMAVNKYGVGEPLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGGSEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYKACDPVFKPGPPTNAHVVDTTKNSITLAWSKPIYDGGSEILGYVVEICKADEEEWQIVTPQTGLRVTRFEIAKLIEHQEYKIRVCALNKVGLGEAASVPGTVKPEDKLEAPELDLDSELRKGIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKVLDTPGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCNKTSFRVENLTEGAIYYFRVMAENEFGVGVPTETSDAVKASEPPSPPGKVTLTDVSQTSASLMWEKPEHDGGSRILGYVVEMQPKGTEKWSVVAESKVCNAVVSGLSSGQEYQFRVKAYNEKGKSDPRVLGIPVIAKDLTIQPSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLKQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNSAGTATENLSVIVLEKPGPPVGPVKFDEVSADFVVISWEPPAYTGGCQISNYIVEKRDTTTTNWQMVSATVARTTIKISKLKTGTEYQFRIFAENRYGKSTPLDSKPVVVQYPFKEPGPPGTPFVTSISKDQMLVQWHEPVNDGGSKVTGYHLEQKEKNSILWVKLNKIPIQDTKFKTTGLDEGLEYEFRVSAENIVGIGKPSKVSECYVARDPCDPPGRPEAIVITRNSVTLKWKKPVYDGGSKITGYIVEKKDLPDGRWMKASFTNVVETEFTVTGLVEDQRYEFRVIARNAADNFSEPSESSGAITARDEIDAPNASLDPKYRDVIIVHAGETFVLEADIRGKPIPDIIWSKDGNELEETAARMEIKSTLQKTTLIVKDCIRTDGGQYTLKLSNVGGTKTIPITVKVLDRPGPPEGPLKVTGVTAEKCYLAWNPPLQDGGASISHYIIEKRETSRLSWTQVSNEVQALNYKVTKLLPGNEYIFRVMAVNKYGIGEALESEPVIACNPYKRPGPPSTPEASAITKDSMVLTWTRPVDDGGAEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENAAGVGEPSEPSVFYRACDALYPPGPPSNPKVTDTSRSSVSLAWNKPIYDGGAPVRGYVIELKKAAADEWTTCTPPSGLQGKQFTVTKLKENTEYNFRICAFNTEGVGEPATIPGSVVAQERMEAPEIELDADLRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTIREVKKDSVTLSWEPPLIDGGAKITNYIVEKRETTRKAYATITNNCTKNTFKIENLQEGCSYYFRVLASNEYGIGLPAETAEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPESDGGSKITGYVVEMQTKGSEKWSACTQVKTLETTISGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVIAKDIEIKPSVELPFNTFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVASSKTVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVLDRPGPPGPIRIDEVSCDNVSISWNPPEYDGGCQISNYIVEKRETTSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVAEYPFSPPGPPGTPKVVHATKSTMVVSWQVPVNDGGSQVIGYHLEYKERSSILWSKANKVLIADTQMKVSGLDEGLMYEYRVYAENIAGIGKCSKACEPVPARDPCDPPGQPEVTNITRKSVSLKWSKPRYDGGAKITGYIVERRELPDGRWLKCNFTNVQETYFEVTELTEDQRYEFRVFARNAADSVSEPSESTGPITVKDDVEAPRIMMDVKFRDVIIVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDYTTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNCKVLDKPGPPAGPLEINGLTAEKCSLSWGRPQEDGGADIDYYIVEKRETSRLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGVGEPLESMAVKALDPFTTPSPPTSLEITSVTKDSMTLCWSRPETDGGSDISGYIIERREKNSLRWMRVNKKPVYDLRVKSTGLREGCEYEYRVFAENAAGLSLPSETSPLVRAEDPVFLPSPPSKPKIVDSGKTTITIGWVKPLFDGGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGLTTGDEYVFRVRSLNKMGASDPSDSSDPQVAKEREEEPVFDVDSEMRKTLIVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTLLTIENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANITVREVTKETAMLSWDVPENDGGAPVKNYHIEKREASKKAWVSVTNNCNRLSYKVTNLQEGAIYYFRVSGENEFGVGVPAETKEGVKITEKPSPPEKLGVTSVSKDSVSLSWLKPEHDGGSRIIHYVVEALEKGQKTWVKCAVVKTTHHVVSGLRESHEYFFRVFAENQAGLSDPRELLLPVLIKDQLEPPEIDMKNFPSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTTDAGRYEITAANSSGTTKTFINIIVLDRPGPPTGPVAISDITEESVTLKWEPPKYDGGSHVTNYIVLKRETSTAVWSEVSATVARTMIKVMKLTTGEEYQFRIKAENRFGISDHIDSVCVVVKLPYTTPGPPSTPWVSNVTRESITVGWHEPVSNGGSAVTGYHLEMKDRNSILWQKANKMIIRTTHFKVTTISAGLIYEFRVYAENAAGIGKPSHPSEPVLAIDACEPPRNVRITDISKNSVNLSWQQPAFDGGSKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVGSVSNPSEVVGPITCIDSYGGPVIDLPLEYTEVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQILDKPGPPGGPIEFKTVTAEKITLLWRPPADDGGAKITHYIVEKRETSRVVWSMVAENLEECIVTTTKIIKGNEYVFRVRAVNKYGIGEPLESEPVVAKNAFVTPGPPSIPEVTKITKNSMTVVWDRPTVDGGSEINGYFLERRDKKSLAWLKVLKETIRDTRQKVTGLTENSDYQYRVCAVNAAGVGPFSEPSDFYKAADPIDPPGPPAKIRIADSTKSSITLGWSKPVYDGGSDVTGYVVEMKQGDEEEWTIVSTRGEVRTTEYVVSNLKPGVNYYFQVSAVNCAGQGEPITMTEPAQAKDVLEEPEIDLDVALRTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDTRYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSLGTVTLLWDPPLIDGGSPIINYVIEKRDATKRTWSVVSHKCSGTSFKVTDLSEKTPFFFRVLAENEIGIGEPCETTEPVKAAEVPAPIRDLSMKDSTKTSVVLSWTKPDFDGGSIITDYLVERKGKGEQAWSHAGISKTCEIEIGQLKEQSVLEFRVSARNEKGQSDPVTIGPLTVKELVITPEVDLSEIPGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNSKKEHGGKYTVILDNAVCRNSFPITIITLGPPSKPKGPIRFDEIKADSAIMSWDIPEDDGGGEITCYSIEKREASQTNWKMVCSSVARTTFKVSNLVKDSEYQFRVRAENRYGVSEPLASNIIVAKHQFRIPGPPGKPVIYNVTSDGMSLTWDAPVYDGGSEVTGFHVEKKERNSILWQRVNTSPISGREYRATGLIEGLDYQFRVYAENSAGLSSPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVAYSIEKRQGSDRWVRCNFTDVSECQYTVTGLSPGDRYEFRIIARNAVGTISPPSQSSGLIMTRDENVPPTVEFGPEYFDGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEVTVKVQDTPGKVVGPIRFTNITGEKMTLWWEAPLNDGCAPVTHYIIEKRETSRLAWALIEDNCEALSYTAIKLITGNEYQFRISAVNKFGVGRPLESDPVVAQIQYTIPDAPGVPEPSNVTGNSITLTWTRPESDGGSEIQHYILERREKKSTRWVKVISKRPISETRFKVTGLVEGNEYEFHVMAENAAGIGPASGISRLIKCREPVNPPSAPSVVKVTDTSKTTVSLEWARPVFDGGMEIIGYIIEMCKADLGDWHKVNTEPCVKTRYTVTDLQAGEEYKFRVSAVNGAGKGDSCEVTGTIKAVDRLSAPELDIDANFKQTHIVRAGVSIRLFIAYQGRPTPTAVWSKPDSNLSIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGKKSITFTVKVLDSPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYVIEKREASRRSWQVVSEKCTRQILKVSELTEGVPYYFRVSAENEYGVGEPYEMPEPIVATEQPAPPRRLDVVDTSKSSAVLAWLKPDHDGGSRITSYLLEMRQKGSDFWVEAGHTKQLTFTVERLVENTEYEFRVKAKNDAGYSEPREAFSSVIIKEPQIEPTADLTGITNQLITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSIATTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWTEPKDDGGTEITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLTKYKEYCFRVSSENRFGVSKPLESVPIVAEHPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGGSKIVGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAAGVSKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLIWSAPVYDGGSKVVGYIIERKPVSEVGDGRWLKCNYTIVSDNFFTVTALSEGDTYEFRVLAKNAAGVISKGSESTGPVTCRDEYAPPKAELDARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKISLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVKVLDSPGPCGKLTVSRVTEEKCTLAWSLPQEDGGAEITHYIVERRETSRLNWVIVEGECLTASYVVTRLIKNNEYTFRVRAVNKYGLGVPVESEPIVARNSFTIPSQPGIPEEVGAGKEHIIIQWTKPESDGGNEISNYLVDKREKKSLRWTRVNKDYVVYDTRLKVTSLMEGCDYQFRVTAVNAAGNSEPSEASNFISCREPSYTPGPPSAPRVVDTTKRSISLAWTKPMYDGGTDIIGYVLEMQEKDTDQWCRVHTNATIRNNEFTVPDLKMGQKYSFRVAAVNAKGMSDYSETTAEIEPVERLEIPDLELADDLKKTVIVRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKVYDTPGPCPSVSVKEVSRDSVTITWEIPTIDGGAPVNNYIIEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEPCETSDAVLVSEVPLVPTKLEVVDVTKSTVTLAWEKPLYDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLEHTVISLNEGEQYLFRVRAQNEKGVSEPREIVTPVTVQDLRVLPTIDLSTMPQKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVTKLTIRETTIRDTGEYTLELKNVTGTTSETIKVIILDKPGPPTGPIKIDEIDATSVTISWEPPELDGGAPLSGYVVEQRDAHRPGWLPVSESVTRPTFKFTRLTEGNEYVFRVAATNRFGIGSYLQSEVIECRSSISIPGPPETLQIFDVSRDGMTLTWYPPEDDGGSQVTGYIVERKEVRADRWVRVNKVPVTMTRYRSTGLIEGLEYEHRVTAINARGTGKPSRPSKPTVAMDPIAPPGKPQNPRVTDTTRTSVSLAWSVPEDEGGSKVTGYLIEMQKVDQREWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNAGGPGEPAEVPGTVKVTEMLEYPDYELDERYQEGVFVRQGGVIRLTIPIKGKPFPVCKWTKEGQDISKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKVIGSPNTPEGPLEYDDIQARSVRVSWRPPADDGGADILGYILERREVPKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPLKSEEPVIPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETSPASEPVVCKDPFDKPSQPGELEILSISKDSVTLQWEKPECDGGKEILGYWVEYRQSGDSAWKKSNKERIKDRQFTIGGLLEATEYEFRVFAENETGLSRPRRTAMSVKTKLTSGEAPGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELIQSRKYKMSSDGRTHTLTVMTDEQEDEGVYTCVATNEVGEVESSSKLLLQAAPQFHPGYPLKEKYYGAVGSTLRLHVMYIGRPVPAMTWFHGQKLLQNSEKITIENTEHYTHLVMKNVQRKTHAGKYKVQLSNAFGTVDATLDVEIQDKPDKPTGPIVIEALLKNSVVISWKPPADDGGSWITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGISEPLEVASIVIIKSPFEKPGVPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLERREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENLGGESEWSEISEPVTPKSDVPIQAPHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEVEVPAKIHLPKTLEGMGAVHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFSNGVERKDAGFYVVCAKNRFGIDQKTVELDVADVPDPPRGVKVSDVSRDSVNLTWTEPASDGGSKVTNYIVEKCATTAERWLRVGQARETRYTVINLFGKTSYQFRVIAENKFGLSKPSEPSEPTVTKEDKTRAMNYDDEVDETREVTTTKASHSKTKELYEKYMIAEDLGRGEFGIVHRCVETSSKRTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINTSAFELNEREIVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSTIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSTATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFKEISLEAMDFVDRLLVKERKSRMTASEALQHPWLKQRIDRVSTKVIRTLKHRRYYHTLIKKDLNMVVSAARISCGGAIRSQRGVSVAKVKVASIEIGPVSGQIMHAIGEEGGYVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFVKGVREVYDYYCRRTKKVKRRTDAMRLLERPPEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDEKKYTFESDKGLYQLTINSVTTDDDAEYTVVARNKHGEDSCKAKLTVTLHPPPTETTLRPMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQVERLRYVKQEFQSKEERERHVQKQIDKTLRMAEILSGTETVPLTPVAQEALREAAILYKPAVSTKTVKGEYRLQTEEKKEERKLRMPYEVPEPRRFKQATVEEDQRIKQFVPMSDMKWYKKIRDQYEMPGKLDRVVQKRPKRIRLSRWEQFYVMPLPRITDQYRPKWRIPKLTQDDLEMVRPARRRTPSPDYDLYYYRRRRRSLGDMSDEELLLPIDDYLAMKRTEEERLRLEEELELGFSASPPSRSPPRFELSSLRYSSPPAHVKVEDRRRDFRYSTYHVPTKEETSTSYAELRERHAQASYRQPKLRQRIMAEKEEEELLRPVTTTQRLSEYKSELDYMSKEEKSKKKSKRQRQVTEITEIEEEYEISRRAQRESSSSVSRLLRRRRSLSPTYIELMRPVSELIRSHPRPAEEYEDDAERRSPTPERTRPRSPSPVSSERSLSRFERSARFDIFSRYESMKAALKTQKTSERKYEVLSQQPFTLDHAPRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDGGTYRAVCTNYKGEASDYATLDVTGGAYTTYASQRRDEEVPKSVFPELTKTEAYAVSSFKRTSELEAASSVREVKSQMTETRESLSTYEHYASAEMKSATSEEKSLEEKATVRKIKTTLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLREGQVVSTSARHQVTTTKYKSTFEISSVQASDEGNYSVVVENSDGKQEAQFTLTVQKARVIEKAVTSPPRVKSPEPRVKSPETVKSPKRVKSPEPVTSHPKAVSPTETKPTEKGQHLPVSAPPKITQSLKAEASKDIAKLTCAVESSALCAKEVAWYKDGKKLKENGHFQFHYSADGTYELKIHNLSESDCGEYVCEVSGEGGTSKTSFQFTGQSFKSIHEQVSSISETTKSVQKTAESPEAKKQEPIAPESISSKPVIVTGLRDTTVSSDSVAKFTIKVTGEPQPTITWTKDGKAIAQGSKYKLSSNKEEFILEILKTETSDGGLYACTVTNSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEVTSQKKASAQEEISQKALTSEEIKMSEVKSHETLAIKEEASKVLIAEEVKRSAAASLEKSIVHEEVTKTSQASEEVKTHAEIKTLSTQMNITKGQRATLKANIAGATDVKWVLNGTELPNSEEYRYGVSGSDQTLTIKQASHREEGILSCIGKTSQGVVKCQFDLTLSEELSDAPSFITQPRSQNINEGQNVLFSCEVSGEPSPEIEWFKNNLPISISSNISVSRSRNVYTLEIRNAAVSDSGKYTIKAKNFHGQCSATASLTVLPLVEEPPREVVLKTSSDVSLHGSVSSQSVQMSASKQEASFSSFSSSSASSMTEMKFASMSAQSMSSMQESFVEMSSSSFMGKSSMTQLESSTSRMLKAGGRGIPPKIEALPSDISIDEGKVLTVACAFTGEPTPEITWSCGGRKIQNQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATVNINIRSM | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; | adult heart development [GO:0007512]; cardiac muscle tissue development [GO:0048738]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac myofibril assembly [GO:0055003]; detection of muscle stretch [GO:0035995]; forward locomotion [GO:0043056]; heart development [GO:0007507]; heart growth [GO:0060419]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; muscle contraction [GO:0006936]; phosphorylation [GO:0016310]; regulation of relaxation of cardiac muscle [GO:1901897]; sarcomere organization [GO:0045214]; somitogenesis [GO:0001756]; striated muscle cell development [GO:0055002]; ventricular system development [GO:0021591] | A band [GO:0031672]; I band [GO:0031674]; M band [GO:0031430]; muscle myosin complex [GO:0005859]; nucleus [GO:0005634]; sarcomere [GO:0030017]; Z disc [GO:0030018] | ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307] | PF00041;PF07679;PF00069;PF02818;PF18362;PF09042; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q8WZ42}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; | null | null | null | null | FUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. {ECO:0000250|UniProtKB:Q8WZ42, ECO:0000269|PubMed:16702235, ECO:0000269|PubMed:17261657}. | Mus musculus (Mouse) |
A2ASZ8 | SCMC2_MOUSE | MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGMLDCARRILAKEGVAAFYKGYIPNMLGIIPYAGIDLAVYETLKNTWLQRYAVNSADPGVFVLLACGTISSTCGQLASYPLALVRTRMQAQASIEGAPEVTMSSLFKQILRTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKITLGVQSR | null | null | adipose tissue development [GO:0060612]; ADP transport [GO:0015866]; ATP metabolic process [GO:0046034]; ATP transport [GO:0015867]; calcium ion transmembrane transport [GO:0070588]; camera-type eye development [GO:0043010]; cellular respiration [GO:0045333]; multicellular organism growth [GO:0035264]; response to activity [GO:0014823]; response to dietary excess [GO:0002021]; response to food [GO:0032094] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP transmembrane transporter activity [GO:0005347]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509] | PF13499;PF13833;PF00153; | 1.10.238.10;1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:15054102}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6KCM7}; | null | null | null | null | FUNCTION: Electroneutral antiporter that most probably mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it could have a broader specificity for adenyl nucleotides. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. {ECO:0000269|PubMed:21296886}. | Mus musculus (Mouse) |
A2AT37 | RENT2_MOUSE | MPAERKKSASMEEKESLLNNKEKDCSERRPVSSKEKPRDDLKVTAKKEVSKVPEDKKKRLEEDKRKKEDKERKKKEEEKVKAEEELKKKEEEEKKKQEEEERKKQEEQAKRQQEEAAAQLKEKEESLQLHQEAWERHQLRKELRSKNQNAPDNRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKLSDVNCAAHLCSLFHQRYSDFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKSIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSQNKDSNKDDSKEAKEPKDNKEASSPDDLELELENLEINDDTLELEGADEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVRKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKESKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSEEEEEGEEEEEENTDYLTDSNKENETDEENAEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGETESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR | null | null | animal organ regeneration [GO:0031100]; liver development [GO:0001889]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; response to unfolded protein [GO:0006986] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; perinuclear region of cytoplasm [GO:0048471] | RNA binding [GO:0003723]; telomeric DNA binding [GO:0042162] | PF02854;PF04050; | 1.25.40.180;4.10.80.160;6.10.250.770; | null | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HAU5}. Cytoplasm {ECO:0000269|PubMed:27149095}. | null | null | null | null | null | FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000250|UniProtKB:Q9HAU5}. | Mus musculus (Mouse) |
A2AU37 | RD21L_MOUSE | MFYTHVLMSKRGPLAKIWLAAHWEKKLTKAHVFECNLEITIQKIISPKVKIALRTSGHLLLGVVRIYNRKAKYLLADCSEAFLKMKMTFRPGLVDLPKENFEAAYNTITLPEEFHDFEIYNINEIDISEPLAQNQSRPEEITLREEYSNDLLFQAGSFGDEPEILRRHSFFDDNILMNSSGLVVEHSSGSFAEEKSLFFDNGDGFGDEGAAGEMIDNLLQDESTFLEEAYLNKEVSLPPELPSSIMVEPGNSDDQCIPEDEEINEITLLSNEDEGFTLDPIDDLDIADRRRRKKRRLLVDPVKEISSKAMHRQLASFMDTLMVLDLAPPTQRLMMWKKRGGVDMLLSTATQDLINDELKMLFTKCFLSSDYKLAKLTLKESVRKEVGNQQIAEPSVMGEPNSHSELDQPQDWKDVTDESVGSFQENVNMNVNSEQDILGMISPAVEGLSSMNGSLAQENCPAELESSGSKQNTEAEKWNQRLFQTLNVLREFNKMGMQSFSLKKLCRNSDRKQAAAKFYTLLILKKHRAIELSQSVPYADIIATVGPMFYKM | null | null | double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; fertilization [GO:0009566]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic attachment of telomere to nuclear envelope [GO:0070197]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; seminiferous tubule development [GO:0072520]; sister chromatid cohesion [GO:0007062]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | chromosome [GO:0005694]; cohesin complex [GO:0008278]; condensed nuclear chromosome [GO:0000794]; lateral element [GO:0000800]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634] | chromatin binding [GO:0003682] | PF04824;PF04825; | 1.10.10.580; | Rad21 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Chromosome {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Note=In meiotic chromosomes, localized along axial elements in early meiosis: detectable on the axial elements in leptotene, and stays on the axial/lateral elements until mid pachytene. It then disappears and is replaced with RAD21. Compared to REC8, has mutually exclusive loading sites on the chromosomes: REC8 and RAD21L form distinct cohesin-enriched domains along the axial elements. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21743440}. | null | null | null | null | null | FUNCTION: Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I. Not required for meiosis in females in young mice, while it is required later as mice age. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440, ECO:0000269|PubMed:22711701}. | Mus musculus (Mouse) |
A2AU72 | ARMC3_MOUSE | MGKKIKKEVEPPPKDVFDPITIESKKAATVVLMLKSPEEDILAKACEAIYKFALKGEENKATLLELGAVEPLTKLLTHEDKTVRRNAMMIFGILASNSDVKKLLRELEVMNSVIAQLSPEEEVVIHEFASLCLANMSVEYTGKVQIFEHGGLEPLIRLLSSSDPDVKKNSIECIYNLVQDFQCRTTLQELNAIPPILELLRSEYPIIQLLALKTLGVITCDKEARTMLKENQGLDHLTKILETKELNDLHVEALSVIANCLEDMDTMVLMQQTGSLKKVLSFAESSTIPDIQKNAAKAIAKAAYDPENRKVFHEQEVEKCLVTLLGSDSDGTKIAASQAISALCENLSCKEFFNTQGIPQIVQLLRSDNEEVREAAALALANLTTSSPANANAAAEADAIDPLINILSSKRDGAIANAATVLTNMATQEPLRAIIQNHEIMHALLGPLHSTNTLVQSTAALTVAATACDVEARTQLRNCGGLVPLVGLLHSKNDEVRRHASWAVMVCAGDEPMAVELCRLGALNILEEINRSLSRKNKFSEAAYNKLLNNNLSLKYSQTGYLSSSNIISDGFYDYGRINPGTKLLSLKELCLQELNDQRAILLVNNKSDTSPPPSMEDKSSDVGYGRSISSSSSLRRGSKEKANAIFGSPTEEKSEPASVRNTILSRAFTKEKGVSKKKSRLQLICSSYLLWKGKGKKEEEKVKEEEEILALPKFTEGSPEKEWNPPPDPEFCVYVLEVTKSILPIVNLKEQIEVLAKYVADKMGGKIPKEKLADFSWELHISELKFQLKSNVVPIGYIKKGIFYHRALLFKALADKIGVGCSLVRGEYSRGWNEVKLVNEARKGMIGNLPPPEEYIVDLMFHPGNLLKLRSKEADLYRFL | null | null | flagellated sperm motility [GO:0030317]; ribophagy [GO:0034517]; spermatid development [GO:0007286] | null | null | PF00514;PF14381; | 1.25.10.10; | null | PTM: Palmitoylation is important for its function in autophagy. {ECO:0000269|PubMed:34428398}. | null | null | null | null | null | null | FUNCTION: Essential for male fertility and sperm motility. During spermatogenesis, promotes the autophagic degradation of excessive ribosomes, providing energy resources for mitochondria and thus ensuring sperm flagellar motility. {ECO:0000269|PubMed:34428398}. | Mus musculus (Mouse) |
A2AUC9 | KLH41_MOUSE | MDSQRELAEELRLYQSTLLQDGLKDLLEEKKFIDCTLKAGDKSFPCHRLILSACSPYFREYFLSEIEEEKKKEVALDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALSSRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEVVFEAVMKWVRTDKENRAKNLSEVFDCIRFRLMAEKYFKDHVEKDDIIKSNPEVQKKIKVLKDAFAGKLPEPSKNAEKAGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPMENECYLTALAEQIPRNHSSLVTQQNQVYVVGGLYVDEENKDQPLQSYFFQLDNVTSEWVGLPPLPSARCLFGLGEVDDKIYVVAGKDLQTEASLDSVLCYDPVAAKWSEVKNLPIKVYGHNVISHNGMIYCLGGKTDDKKCTNRVFIYNPKKGDWKDLAPMKTPRSMFGVAIHKGKIVIAGGVTEDGLSASVEAFDLKTNKWEVMTEFPQERSSISLVSLAGALYAIGGFAMIQLESKEFAPTEVNDIWKYEDDKKEWAGMLKEIRYASGASCLATRLNLFKLSKL | null | null | myofibril assembly [GO:0030239]; protein ubiquitination [GO:0016567]; pseudopodium assembly [GO:0031269]; regulation of myoblast differentiation [GO:0045661]; regulation of myoblast proliferation [GO:2000291]; regulation of skeletal muscle cell differentiation [GO:2001014]; skeletal muscle cell differentiation [GO:0035914] | Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; M band [GO:0031430]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]; ruffle [GO:0001726]; sarcoplasmic reticulum membrane [GO:0033017] | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | null | PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination. {ECO:0000250|UniProtKB:O60662}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18178185}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22562206}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24268659}. Note=Predominantly cytoplasmic but can colocalize with F-actin at the membrane ruffle-like structures at the tips of transformation-specific pseudopodia. | null | null | null | null | null | FUNCTION: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells. {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:21368295, ECO:0000269|PubMed:22562206}. | Mus musculus (Mouse) |
Subsets and Splits