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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
E9Q3T6 | PRD14_MOUSE | MALPPSGETQSQDKANYLPQSNPHHLTTYYAHAPGYSHFRNLATTEEEFQPWKLAAAVLESQAMAPLDAFRMTAPLLNPGLAVQSEPLYNLPWYKLSPWNRIPQFTPEVPRFLDSTEHRSSGSSNQNLVLGGGGGQISGQRWEAENLLLPSPVIASLLPDGIKSSQSISVPQTLNQEGKLPFCGFNFTEEELSFVLYGAIASPEHPTDLQHAISGILVPTESSGSNHLHKTLDKDSLQLPEGLCLMQTSFGDVPHFGVFCSDFIAKGVRFGPFRGRVVNASEVKAHRDNSRMWEIFEDGHLSHFIDGKGSGNWMSYVNCARFPKEQNLLAVQHQGQIFYESCRDIQRNQELLVWYGNGYEKFLGVPMNLRVTEQGGQQLSESSEESAEGYRCERCGKVFTYKYYRDKHLKYTPCVDKGDRKFPCSLCQRSFEKRDRLRIHILHVHERHRPYLCSTCGKSFSQSSSLNKHMRVHSGDRPYQCVYCTKKFTASSILRTHIRQHSGEKPFKCKHCGKAFASHAAHDSHVRRSHKDNGRSSCDICGKGFLDQEAFYAHMRLHKTC | 2.1.1.- | null | cell fate specification [GO:0001708]; cell morphogenesis [GO:0000902]; embryo implantation [GO:0007566]; epigenetic regulation of gene expression [GO:0040029]; fertilization [GO:0009566]; fibroblast growth factor receptor signaling pathway [GO:0008543]; germ cell development [GO:0007281]; germ-line stem cell population maintenance [GO:0030718]; homeostasis of number of cells within a tissue [GO:0048873]; inactivation of paternal X chromosome by genomic imprinting [GO:0060818]; inner cell mass cell fate commitment [GO:0001827]; methylation [GO:0032259]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of stem cell population maintenance [GO:1902459]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; stem cell population maintenance [GO:0019827] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcription factor that has both positive and negative roles on transcription (By similarity). Plays a role in cellular pluripotency. Essential for germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation. {ECO:0000250, ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:26523391}. | Mus musculus (Mouse) |
E9Q401 | RYR2_MOUSE | MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGQVDVEKWKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWHVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKEKADVKSTAFAFRSSKEKLDVGVRKEVDGMGTSEIKYGDSICYIQHVDTGLWLTYQAVDVKSARMGSIQRKAIMHHEGHMDDGLNLSRSQHEESRTARVIRSTVFLFNRFIRGLDALSKKVKLPTIDLPIESVSLSLQDLIGYFHPPDEHLEHEDKQNRLRALKNRQNLFQEEGMINLVLECIDRLHVYSSAAHFADVAGREAGESWKSILNSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPEALNIIKEGHIKSIISLLDKHGRNHKVLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRLVNHVSSMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTAEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLWSGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAACYEAVLPKEKLKVEHSREYKQERTYTRDLLGPTVSLTQAAFTPVPVDTSQIVLPPHLERIRERLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFCKLPEQERNYNLQMSLETLKTLLALGCHVGIADEHAEEKVKKMKLPKNYQLTSGYKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVRTLLGYGYHLEAPDQDHASRAEVCSGTGERFRIFRAEKTYAVKAGRWYFEFEAVTAGDMRVGWSRPGCQPDLELGSDDRAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCMVDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKDVSTLKYFTICGLQEGYEPFAVNTNRDITMWLSKRLPQFLQVPSNHEHIEVTRIDGTIDSSPCLKVTQKSFGSQNNNTDIMFYRLSMPIECAEVFSKSVAGGLPGAGFYGPKNDLEDFDVDSDFEVLMKTAHGHLVPDRIDKDKETPKPEFNNHKDYAQEKPSRLKQRFLLRRTKPDYSTGHSARLTEDVLADDRDDYEYLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESIKRSNCYMVCAGESMSPGQGRNNSNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFELGRIKNVMPLSAGLFKSEHKNPVPQCPPRLHVQFLSHVLWSRMPNQFLKVDVSRISERQGWLVQCLDPLQFMSLHIPEENRSVDILELTEQEELLQFHYHTLRLYSAVCALGNHRVAHALCSHVDEPQLLYAIENKYMPGLLRAGYYDLLIDIHLSSYATARLMMNNEFIVPMTEETKSITLFPDENKKHGLPGIGLSTSLRPRMRFSSPSFVSISNDCYQYSPEFPLDILKAKTIQMLTEAVKEGSLHARDPVGGTTEFLFVPLIKLFYTLLIMGIFHNEDLKHILQLIEPSVFKEAAVPEEEGGTPEKEISIEDAKLEGEEEAKGGKRPKEGLLQMKLPEPVKLQMCLLLQYLCDCQVRHRIEAIVAFSDDFVAKLQDNQRFRYNEVMQALNMSAALTARKTREFRSPPQEQINMLLNFKDDKSECPCPEEIRDQLLDFHEDLMTHCGIELDEDGSLDGSNDLTIRGRLLSLVEKVTYLKKKQAEKPVASDSRKCSSLQQLISETMVRWAQESVIEDPELVRAMFVLLHRQYDGIGGLVRALPKTYTINGVSVEDTINLLASLGQIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEITFPKMVANCCRFLCYFCRISRQNQKAMFDHLSYLLENSSVGLASPAMRGSTPLDVAAASVMDNNELALALREPDLEKVVRYLAGCGLQSCQMLVSKGYPDIGWNPVEGERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALRGEGGNGLLAAMEEAIKIAEDPSRDGPSPTSGSSKTLDIEEEEDDTIHMGNAIMTFYAALIDLLGRCAPEMHLIHAGKGEAIRIRSILRSLIPLGDLVGVISIAFQMPTIAKDGKVVEPDMSAGFCPDHKAAMVLFLDRVYGIEVQDFLLHLLEVGFLPDLRAAASLDTAALSATDMALALNRYLCTAVLPLLTRCAPLFAGTEHHASLIDSLLHTVYRLSKGCSLTKAQRDSIEVCLLSICGQLRPSMMQHLLRRLVFDVPLLNEHAKMPLKLLTNHYERCWKYYCLPGGWGNFGAASEEELHLSRKLFWGIFDALSQKKYEQELFKLALPCLSAVAGALPPDYMESNYVSMMEKQSSMDSEGNFNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKIQPLMKPYKLLSEKEKEIYRWPIKESLKTMLAWGWRIERTREGDSMALYNRTRRISQTSQVSIDAAHGYSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKLELESKGGGNHPLLVPYDTLTAKEKAKDREKAQDIFKFLQISGYVVSRGFKDLDLDTPSIEKRFAYSFLQQLIRYVDEAHQYILEFDGGSRSKGEHFPYEQEIKFFAKVVLPLIDQYFKNHRLYFLSAASRPLCTGGHASNKEKEMVTSLFCKLGVLVRHRISLFGNDATSIVNCLHILGQTLDARTVMKTGLDSVKSALRAFLDNAAEDLEKTMENLKQGQFTHTRSQPKGVTQIINYTTVALLPMLSSLFEHIGQHQFGEDLILEDVQVSCYRILTSLYALGTSKSIYVERQRSALGECLAAFAGAFPIAFLETHLDKHNVYSIYNTRSSRERAALSLPANVEDVCPNIPSLEKLMTEIIELAESGIRYTQMPYMMEVVLPMLCSYMSRWWEHGPENHPERAEMCCTALNSEHMNTLLGNILKIIYNNLGIDEGAWMKRLAVFSQPIINKVKPQLLKTHFLPLMEKLKKKAAMVVSEEDHLKAEARGDMSEAELLILDEFTTLARDLYAFYPLLIRFVDYNRAKWLKEPNPEAEELFRMVAEVFIYWSKSHNFKREEQNFVVQNEINNMSFLITDTKSKMSKAAISDQERKKMKRKGDRYSMQTSLIVAALKRLLPIGLNICAPGDQELIALAKNRFSLKDTEEEVRDIIRSNIHLQGKLEDPAIRWQMALYKDLPNRTEDPSDPERTVERVLGIANVLFHLEQKSKYTGRGYFSLVEHPQRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRAVNLFLQGYEKSWIETEEHYFEDKLIEDLAKPGAELPEEDEAMKRVDPLHQLILLFSRTALTEKCKLEEDFLYMAYADIMAKSCHDEEDDDGEEEVKSFEEKEMEKQKLLYQQARLHDRGAAEMVLQTISASKGETGPMVAATLKLGIAILNGGNSTVQQKMLDYLKEKKDVGFFQSLAGLMQSCSVLDLNAFERQNKAEGLGMVTEEGSGEKVLQDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISDFYWYYSGKDIIDEQGQRNFSKAIQVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMQMKLSQDSSQIELLKELMDLQKDMVVMLLSMLEGNVVNGTIGKQMVDMLVESSNNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGVISKRDFHKAMESHKHYTQSETEFLLSCAETDENETLDYEEFVKRFHEPAKDIGFNVAVLLTNLSEHMPNDTRLQTFLELAESVLNYFQPFLGRIEIMGSAKRIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEKEKMELFVNFCEDTIFEMQLAAQISESDLNERLANKEESEKERPEEQAPRMGFFSLLTIQSALFALRYNVLTLVRMLSLKSLKKQMKRMKKMTVKDMVLAFFSSYWSVFVTLLHFVASVCRGFFRIVSSLLLGGSLVEGAKKIKVAELLANMPDPTQDEVRGDEEEGERKPLESALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMTNPVPVPEVQEKFQEQKAKEEKEEKEETKSEPEKAEGEDGEKEEKAKDEKSKQKLRQLHTHRYGEPEVPESAFWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSSVVEGKELPTRTSSDTAKVTNSLDSSPHRIIAVHYVLEESSGYMEPTLRILAILHTIISFFCIIGYYCLKVPLVIFKREKEVARKLEFDGLYITEQPSEDDIKGQWDRLVINTQSFPNNYWDKFVKRKVMDKYGEFYGRDRISELLGMDKAALDFSDAREKKKPKKDSSLSAVLNSIDVKYQMWKLGVVFTDNSFLYLAWYMTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDGDTPDMKCDDMLTCYMFHMYVGVRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGNDYFDTVPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWEFFPAGDCFRKQYEDQLN | null | null | calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport into cytosol [GO:0060402]; calcium-mediated signaling [GO:0019722]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cardiac muscle hypertrophy [GO:0003300]; cellular response to caffeine [GO:0071313]; cellular response to epinephrine stimulus [GO:0071872]; detection of calcium ion [GO:0005513]; embryonic heart tube morphogenesis [GO:0003143]; establishment of localization in cell [GO:0051649]; establishment of protein localization to endoplasmic reticulum [GO:0072599]; intracellular calcium ion homeostasis [GO:0006874]; left ventricular cardiac muscle tissue morphogenesis [GO:0003220]; manganese ion transmembrane transport [GO:0071421]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; positive regulation of heart rate [GO:0010460]; positive regulation of sequestering of calcium ion [GO:0051284]; positive regulation of the force of heart contraction [GO:0098735]; Purkinje myocyte to ventricular cardiac muscle cell signaling [GO:0086029]; regulation of atrial cardiac muscle cell action potential [GO:0098910]; regulation of AV node cell action potential [GO:0098904]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of heart rate [GO:0002027]; regulation of SA node cell action potential [GO:0098907]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to caffeine [GO:0031000]; response to calcium ion [GO:0051592]; response to hypoxia [GO:0001666]; response to magnesium ion [GO:0032026]; response to muscle activity [GO:0014850]; response to muscle stretch [GO:0035994]; response to redox state [GO:0051775]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; striated muscle contraction [GO:0006941]; type B pancreatic cell apoptotic process [GO:0097050]; ventricular cardiac muscle cell action potential [GO:0086005] | A band [GO:0031672]; calcium channel complex [GO:0034704]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; Z disc [GO:0030018] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; organic cyclic compound binding [GO:0097159]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; scaffold protein binding [GO:0097110]; suramin binding [GO:0043924] | PF13499;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;1.10.238.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR2 subfamily | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2807 and Ser-2813 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca(2+) levels. {ECO:0000269|PubMed:17693412, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440}.; PTM: Phosphorylation at Ser-2030 by PKA enhances the response to lumenal calcium. {ECO:0000269|PubMed:17693412}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:10473538}; 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:10473538, ECO:0000269|PubMed:33536282}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) cytosolic levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development. {ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440, ECO:0000269|PubMed:33536282, ECO:0000269|PubMed:9628868}. | Mus musculus (Mouse) |
E9Q414 | APOB_MOUSE | MGPRKPALRTPLLLLFLLLFLDTSVWAQDEVLENLSFSCPKDATRFKHLRKYVYNYEAESSSGVQGTADSRSATKINCKVELEVPQICGFIMRTNQCTLKEVYGFNPEGKALMKKTKNSEEFAAAMSRYELKLAIPEGKQIVLYPDKDEPKYILNIKRGIISALLVPPETEEDQQELFLDTVYGNCSTQVTVNSRKGTVPTEMSTERNLQQCDGFQPISTSVSPLALIKGLVHPLSTLISSSQTCQYTLDPKRKHVSEAVCDEQHLFLPFSYKNKYGIMTRVTQKLSLEDTPKINSRFFSEGTNRMGLAFESTKSTSSPKQADAVLKTLQELKKLSISEQNAQRANLFNKLVTELRGLTGEAITSLLPQLIEVSSPITLQALVQCGQPQCYTHILQWLKTEKAHPLLVDIVTYLMALIPNPSTQRLQEIFNTAKEQQSRATLYALSHAVNSYFDVDHSRSPVLQDIAGYLLKQIDNECTGNEDHTFLILRVIGNMGRTMEQVMPALKSSVLSCVRSTKPSLLIQKAALQALRKMELEDEVRTILFDTFVNGVAPVEKRLAAYLLLMKNPSSSDINKIAQLLQWEQSEQVKNFVASHIANILNSEELYVQDLKVLIKNALENSQFPTIMDFRKFSRNYQISKSASLPMFDPVSVKIEGNLIFDPSSYLPRESLLKTTLTVFGLASLDLFEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGRVPDGVSKVLVDHFGYTTDGKHEQDMVNGIMPIVDKLIKDLKSKEIPEARAYLRILGKELSFVRLQDLQVLGKLLLSGAQTLQGIPQMVVQAIREGSKNDLFLHYIFMDNAFELPTGAGLQLQVSSSGVFTPGIKAGVRLELANIQAELVAKPSVSLEFVTNMGIIIPDFAKSSVQMNTNFFHESGLEARVALKAGQLKVIIPSPKRPVKLFSGSNTLHLVSTTKTEVIPPLVENRQSWSTCKPLFTGMNYCTTGAYSNASSTESASYYPLTGDTRYELELRPTGEVEQYSATATYELLKEDKSLVDTLKFLVQAEGVQQSEATVLFKYNRRSRTLSSEVLIPGFDVNFGTILRVNDESAKDKNTYKLILDIQNKKITEVSLVGHLSYDKKGDGKIKGVVSIPRLQAEARSEVHTHWSSTKLLFQMDSSATAYGSTISKRVTWRYDNEIIEFDWNTGTNVDTKKVASNFPVDLSHYPRMLHEYANGLLDHRVPQTDVTFRDMGSKLIVATNTWLQMATRGLPYPQTLQDHLNSLSELNLLKMGLSDFHIPDNLFLKTDGRVKYTMNRNKINIDIPLPLGGKSSKDLKMPESVRTPALNFKSVGFHLPSREVQVPTFTIPKTHQLQVPLLGVLDLSTNVYSNLYNWSASYTGGNTSRDHFSLQAQYRMKTDSVVDLFSYSVQGSGETTYDSKNTFTLSCDGSLHHKFLDSKFKVSHVEKFGNSPVSKGLLTFETSSALGPQMSATVHLDSKKKQHLYVKDIKVDGQFRASSFYAQGKYGLSCERDVTTGQLSGESNMRFNSTYFQGTNQIVGMYQDGALSITSTSDLQDGIFKNTASLKYENYELTLKSDSSGQYENFAASNKLDVTFSTQSALLRSEHQANYKSLRLVTLLSGSLTSQGVELNADILGTDKINTGAHKATLKIARDGLSTSATTNLKYSPLLLENELNAELGLSGASMKLSTNGRFKEHHAKFSLDGRAALTEVSLGSIYQAMILGADSKNIFNFKLSREGLRLSNDLMGSYAEMKLDHTHSLNIAGLSLDFFSKMDNIYSGDKFYKQNFNLQLQPYSFITTLSNDLRYGALDLTNNGRFRLEPLKLNVGGNFKGTYQNNELKHIYTISYTDLVVASYRADTVAKVQGVEFSHRLNADIEGLTSSVDVTTSYNSDPLHFNNVFHFSLAPFTLGIDTHTSGDGKLSFWGEHTGQLYSKFLLKAEPLALIVSHDYKGSTSHSLPYESSISTALEHTVSALLTPAEQTSTWKFKTKLNDKVYSQDFEAYNTKDKIGVELSGRADLSGLYSPIKLPFFYSEPVNVLNGLEVNDAVDKPQEFTIIAVVKYDKNQDVHTINLPFFKSLPDYLERNRRGMISLLEAMRGELQRLSVDQFVRKYRAALSRLPQQIHHYLNASDWERQVAGAKEKITSFMENYRITDNDVLIAIDSAKINFNEKLSQLETYAIQFDQYIKDNYDPHDLKRTIAEIIDRIIEKLKILDEQYHIRVNLAKSIHNLYLFVENVDLNQVSSSNTSWIQNVDSNYQVRIQIQEKLQQLRTQIQNIDIQQLAAEVKRQMDAIDVTMHLDQLRTAILFQRISDIIDRVKYFVMNLIEDFKVTEKINTFRVIVRELIEKYEVDQHIQVLMDKSVELAHRYSLSEPLQKLSNVLQRIEIKDYYEKLVGFIDDTVEWLKALSFKNTIEELNRLTDMLVKKLKAFDYHQFVDKTNSKIREMTQRINAEIQALKLPQKMEALKLLVEDFKTTVSNSLERLKDTKVTVVIDWLQDILTQMKDHFQDTLEDVRDRIYQMDIQRELEHFLSLVNQVYSTLVTYMSDWWTLTAKNITDFAEQYSIQNWAESIKVLVEQGFIVPEMQTFLWTMPAFEVSLRALQEGNFQTPVFIVPLTDLRIPSIRINFKMLKNIKIPLRFSTPEFTLLNTFHVHSFTIDLLEIKAKIIRTIDQILSSELQWPLPEMYLRDLDVVNIPLARLTLPDFHVPEITIPEFTIPNVNLKDLHVPDLHIPEFQLPHLSHTIEIPAFGKLHSILKIQSPLFILDANANIQNVTTSGNKAEIVASVTAKGESQFEALNFDFQAQAQFLELNPHPPVLKESMNFSSKHVRMEHEGEIVFDGKAIEGKSDTVASLHTEKNEVEFNNGMTVKVNNQLTLDSHTKYFHKLSVPRLDFSSKASLNNEIKTLLEAGHVALTSSGTGSWNWACPNFSDEGIHSSQISFTVDGPIAFVGLSNNINGKHLRVIQKLTYESGFLNYSKFEVESKVESQHVGSSILTANGRALLKDAKAEMTGEHNANLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVGFPLKLTGKIDFLNNYALFLSPRAQQASWQASTRFNQYKYNQNFSAINNEHNIEASIGMNGDANLDFLNIPLTIPEINLPYTEFKTPLLKDFSIWEETGLKEFLKTTKQSFDLSVKAQYKKNSDKHSIVVPLGMFYEFILNNVNSWDRKFEKVRNNALHFLTTSYNEAKIKVDKYKTENSLNQPSGTFQNHGYTIPVVNIEVSPFAVETLASSHVIPTAISTPSVTIPGPNIMVPSYKLVLPPLELPVFHGPGNLFKFFLPDFKGFNTIDNIYIPAMGNFTYDFSFKSSVITLNTNAGLYNQSDIVAHFLSSSSFVTDALQYKLEGTSRLMRKRGLKLATAVSLTNKFVKGSHDSTISLTKKNMEASVRTTANLHAPIFSMNFKQELNGNTKSKPTVSSSIELNYDFNSSKLHSTATGGIDHKFSLESLTSYFSIESFTKGNIKSSFLSQEYSGSVANEANVYLNSKGTRSSVRLQGASKVDGIWNVEVGENFAGEATLQRIYTTWEHNMKNHLQVYSYFFTKGKQTCRATLELSPWTMSTLLQVHVSQLSSLLDLHHFDQEVILKANTKNQKISWKGGVQVESRVLQHNAQFSNDQEEIRLDLAGSLDGQLWDLEAIFLPVYGKSLQELLQMDGKRQYLQASTSLLYTKNPNGYLLSLPVQELADRFIIPGIKLNDFSGVKIYKKLSTSPFALNLTMLPKVKFPGIDLLTQYSTPEGSSVPIFEATIPEIHLTVSQFTLPKSLPVGNTVFDLNKLANMIADVDLPSVTLPEQTIVIPPLEFSVPAGIFIPFFGELTARAGMASPLYNVTWSAGWKTKADHVETFLDSMCTSTLQFLEYALKVVETHKIEEDLLTYNIKGTLQHCDFNVEYNEDGLFKGLWDWQGEAHLDITSPALTDFHLYYKEDKTSLSASAASSTIGTVGLDSSTDDQSVELNVYFHPQSPPEKKLSIFKTEWRYKESDGERYIKINWEEEAASRLLGSLKSNVPKASKAIYDYANKYHLEYVSSELRKSLQVNAEHARRMVDEMNMSFQRVARDTYQNLYEEMLAQKSLSIPENLKKRVLDSIVHVTQKYHMAVMWLMDSFIHFLKFNRVQFPGYAGTYTVDELYTIVMKETKKSLSQLFNGLGNLLSYVQNQVEKSRLINDITFKCPFFSKPCKLKDLILIFREELNILSNIGQQDIKFTTILSSLQGFLERVLDIIEEQIKCLKDNESTCVADHINMVFKIQVPYAFKSLREDIYFVLGEFNDFLQSILQEGSYKLQQVHQYMKALREEYFDPSMVGWTVKYYEIEENMVELIKTLLVSFRDVYSEYSVTAADFASKMSTQVEQFVSRDIREYLSMLTDINGKWMEKIAELSIVAKETMKSWVTAVAKIMSDYPQQFHSNLQDFSDQLSSYYEKFVGESTRLIDLSIQNYHVFLRYITELLRKLQVATANNVSPYIKLAQGELMITF | null | null | artery morphogenesis [GO:0048844]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; establishment of localization in cell [GO:0051649]; fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; in utero embryonic development [GO:0001701]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; low-density lipoprotein particle clearance [GO:0034383]; low-density lipoprotein particle remodeling [GO:0034374]; nervous system development [GO:0007399]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; post-embryonic development [GO:0009791]; regulation of cholesterol biosynthetic process [GO:0045540]; response to carbohydrate [GO:0009743]; response to virus [GO:0009615]; spermatogenesis [GO:0007283]; triglyceride catabolic process [GO:0019433]; triglyceride mobilization [GO:0006642] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; lipid droplet [GO:0005811]; low-density lipoprotein particle [GO:0034362]; mature chylomicron [GO:0034359]; neuronal cell body [GO:0043025]; very-low-density lipoprotein particle [GO:0034361]; vesicle lumen [GO:0031983] | cholesterol transfer activity [GO:0120020]; heparin binding [GO:0008201]; lipase binding [GO:0035473]; low-density lipoprotein particle receptor binding [GO:0050750]; phospholipid binding [GO:0005543] | PF12491;PF06448;PF09172;PF01347; | 2.20.80.10;1.25.10.20; | null | PTM: Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}. Secreted {ECO:0000250|UniProtKB:P04114}. Lipid droplet {ECO:0000250|UniProtKB:P04114}. | null | null | null | null | null | FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. | Mus musculus (Mouse) |
E9Q4F7 | ANR11_MOUSE | MPKGGCSKTPQQEDFALSNDMVEKQTGKKDKDKVSLTKTPKLDRSDGGKEVRERATKRKLPFTVGANGEQKDSDTEKQGPERKRIKKEPVARKSGLLFGMGLSGIRAGYPLSERQQVALLMQMTAEESANSPVDTTPKHPSQSTVCQKGTPNSASKTKDKVNKRNERGETRLHRAAIRGDARRIKELISEGADVNVKDFAGWTALHEACNRGYYDIAKQLLAAGAEVNTKGLDDDTPLHDAANNGHYKVVKLLLRYGGNPQQSNRKGETPLKVANSPTMVNLLLGKGTYTSSEESSTESSEEEDAPSFAPSSSVDGNNTDSEFEKGLKLKAKNPEPQKTVTPVKDEYEFDEDDEQDRVPPVDDKHLLKKDYRKEAKANSFISIPKMEVKSYSKNNTLAPKKAAHRILSDTSDEEDVSVSIGAGEKLRLSAHTMLPGSKARESSSSRQQKEKNKLKKKRKKETKGKEVRFGKRSDKFCSSGSESESSESEEDDGDSVGSSGCLKGSPLVLKDPSLFSSLSASSTSSHGSAVAQKHGSGHTDQHTKHWRTDNWKAISSPAWSEVSSLSDSSRTGLTSESDCSSEGSSVESLKPTRRKQEHRKRGVLQSAPSEKRSSFHPCTDGAVPKLDKEGKVVKKHKTKHKHKHKEKGQCSVSQELKLKSFTYEYEDSKQKSDKAILLESDLSTENKLKVLKHDREHLKKEDKLGRMKPEDKDWLFKDEKVLKRIKDANKDMSRAFREDKDRASKAERERATKDKSPKEEKLRLYKEERKKKSKDRASRLERKNDMKEDKLSKEKEKAFKEDKEKLKKEKLYREDAAFDDYCNKSQFLDHEDTKFSLSDDQQERWFSDLSDSSFDFKGEDSWDSVTDYRDIKNDSVAKLILETVKEDSKEKKRDNKIREKRDFKDSFFRKRDRDCLDKNSEKRRDQTEKHKSIPSYLSEKDKKRRESAEGGRDRRDGRIRSEEVHREDLKECGFESSFKDKSDCDFPKNLEPWERPHAAREKEKKDALEKERKEKGRADKYKEKSSERERSDKSTLDKCQKDKEFEKCFKEKKDGKEKHKDIHSKDRKASFDQLREKKEKVFSSIISEDFSERKDDRKGKEKSWYIADIFTDESEDEKDDCVAGSFKATEASDTQRVDGLPEKEEGREHPSDRHRKSSSDRQHTEKPRDKEPKEKKKDRGASEGGKDKKEKMEKIFEKHKEKKDKECAERYKDRKERASADSAPEKKNKQKLPEKVEKKHFAEDKVKSKHKEKPEKEHSRERERKPSRGPDVEKSLLEKLEEEALHDYREDSNDKISEVSSDSFADHGQEPSLSTLLEVSFSEPPAEDKARDSACLSEKLREKERHRHSSSSSKKSHERERAKKEKAEKKEKSEDYKDSISSVRKDASQFEKDFLDAETYGVSYPTKADVEEELDKAIELFSSEKKDRSDPEREPAKRIEKELKPYGSSAISILKEKKKREKHRERWREEKERHRDKHVDGFLRHHKDEPKPAAKDKDNPPNSFKEKSREESLKLSETKLKEKFKENTEREKGDSIKMSNGNDKLVPSRDSGKKDSRPREKLLGDGDLMMTSFERMLSQKDLEIEERHKRHKERMKQMEKMRHRSGDPKLKEKKPTEDGRKKSLDFPSKKALGLDKKVKEPAPTLTTGESKPHSGPGTESKDWLSGQPLKEVLPASPRTEQSRPTGVPTPTSVVSCPSYEEVMHTPRTPSCSADDYPDLVFDCTDSQHSMPVSTASTSACSPPFFDRFSVASSVVSENAAGQTPTRPISTNLYRSISVDIRRTPEEEFSAGDKLFRQQSVPAPSSFDSPVQHLLEEKAPLPPVPAEKFACLSPGYYSPDYGIPSPKVDTLHCPPTAVVSATPPPDSVFSNLPPKSSPSPRGELLSPAIEGTLPPDLGLPLDATEDQQATAAILPQEPSYLEPLDEGPFTTVITEEPVEWTHTAAEQGLSSSSLIASASENPVSWPVGSELMLKSPQRFAESPKHFCPGESLHSTTPGPYSAAEPTYPVSPGSYPLPAPEPALEEVKDGGTGAIPVAISAAEGAAPYAAPARLESFFSNCKSHPDAPLDTAPEPTGVTAVAQVEALGPLESSFLDSNPSISTLSQVEPVSWHEAFTSPEDDLDLGPFSLPELPLQAKDASDVEAEAAKASPVPPAESPPGPTGVLGGGDVPAPAAEEPPAPPPQEASPQLSTEPEPSEEPKLDVVLEATVETEVLADDSAPEASISNSVPAPSPPQQQPPGGGDEEAETEDPSATPCCAPDGPTTDGLAQAHNSAEASCVVAAAEGPPGNVQAEATDPEPKPTSEVPKAPKVEEVPQRMTRNRAQMLASQSKQGIPAAEKDPMPTPASRAKGRASEEEDAQAQHPRKRRFQRSSQQLQQQLNTSTQQTREVIQQTLAAIVDAIKLDAIEPYHSDRSNPYFEYLQIRKKIEEKRKILCCITPQAPQCYAEYVTYTGSYLLDGKPLSKLHIPVIAPPPSLAEPLKELFKQQEAVRGKLRLQHSIEREKLIVSCEQEILRVHCRAARTIANQAVPFSACTMLLDSEVYNMPLESQGDENKSVRDRFNARQFISWLQDVDDKYDRMKTCLLMRQQHEAAALNAVQRMEWQLKAQELDPAGHKSLCVNEVPSFYVPMVDVNDDFVLLPA | null | null | anatomical structure morphogenesis [GO:0009653]; bone development [GO:0060348]; face morphogenesis [GO:0060325]; head morphogenesis [GO:0060323]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; odontogenesis of dentin-containing tooth [GO:0042475]; skeletal system morphogenesis [GO:0048705]; tissue homeostasis [GO:0001894] | nucleus [GO:0005634] | null | PF12796; | 1.25.40.20; | null | PTM: Subject to proteasomal degradation which is probably essential to regulate its activity. {ECO:0000269|PubMed:25413698}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25413698}. Note=Localizes to chromatin during prometaphase (By similarity). {ECO:0000250|UniProtKB:Q6UB99}. | null | null | null | null | null | FUNCTION: Chromatin regulator which modulates histone acetylation and gene expression in neural precursor cells (PubMed:25556659). May recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation (By similarity). Has a role in proliferation and development of cortical neural precursors (PubMed:25556659). May also regulate bone homeostasis (PubMed:17986521). {ECO:0000250|UniProtKB:Q6UB99, ECO:0000269|PubMed:17986521, ECO:0000269|PubMed:25556659}. | Mus musculus (Mouse) |
E9Q4J9 | AGRF2_MOUSE | MIPAHWLYCLMLLLPIESCRILCQASSKSKEKVTSRPHDVCDGVCNNNGTPCFQSCPPDSEGNMKFACKAKKWHKVTETCHTLNTHSIFEEDKELYSVQSSDSTIRTHMFHRELKTIMDTLMEKCPKDLSCVIKGIERSPRMPGNIAVVVQLLHNISTTLTKDVNEEKMQSYSAMANHILNSKSISNWTFIQDRNSSCVLLQSIHSFASKLFMKEHLINISHVFIHTLGTVVSRGSLGKNFTFSMRINETSDKVTGRLLLSPEELQKVPSAFQVISIAFPTLGAILEASLLENVTVNGLVLSVILPEELKNISLIFEKIRKSGERKSQCVGWHSLESRWDWRACKTIQENSRQAVCRCRPNKLYTSFSILMSPNTLESPVLTYITYIGLGISICSLIICLAIEVLVWSQVTKTEISYLRHLCIANIAATLLMADAWFIVASFLSGPVLHHNGCVAATFFVHFFYLSVFFWMLAKALLILYGILIVFHTLPKSCLVASLFSVGYGCPLVIAIITLAVTEPGKGYLRPEACWLNWDMTKALLAFVVPALAIVVVNLITVTMVIIKTQRAAIGSSMFQEVRAIVRICKNIAILTPLLGLTWGFGIATVINGHSLAFHIIFSLLNALQVSPDAAVDSELRECVHRFCG | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166] | membrane [GO:0016020] | G protein-coupled receptor activity [GO:0004930] | PF00002;PF01825; | 2.60.220.50;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Orphan receptor. | Mus musculus (Mouse) |
E9Q4N7 | ARI1B_MOUSE | MAARAAAAARARAGSGERRAPSGPRPAPGARDLETGARGAVAAPGPILGGGDGGLNNVHHHPLHPRHDLNMAHSASAAAAASSNSAQSGRSEAALKEGGSAAALSSSAAVAASSSSAGPGSTMETGLLPNHKLKAVGEAPAAPPHQQHHHHHAHHHHHHHAHHLHHLHHHHALQQQLNQFQQPQPPQPQQQQPPPPPQQQHPTANNSLGGAGGGAPQPGPDMEQPQHGGAKDSVAGNQADPQGQPLLSKPGDEDDAPPKMGEPAGSRYEHPGLGAQQQPAPVAVPGGGGGPAAVSEFNNYYGSAAPASGGPGGRAGPCFDQHGGQQSPGMGMMHSASAAAGAPSSMDPLQNSHEGYPNSQYNHYPGYSRPGAGGGGGGGGGGGGSGGGGGGGGAGGAGGAAAAAAGAGAVAAAAAAAAAAAAAAGGGGGGGYGSSSSGYGVLSSPRQQGGGMMMGPGGGGAASLSKAAAGAAAAAGGFQRFAGQNQHPSGATPTLNQLLTSPSPMMRSYGGSYPDYSSSSAPPPPSQPQSQAAAGAAAGGQQAAAGMGLGKDLGAQYAAASPAWAAAQQRSHPAMSPGTPGPTMGRSQGSPMDPMVMKRPQLYGMGTHPHSQPQQSSPYPGGSYGPPGAQRYPLGMQGRAPGALGGLQYPQQQMPPQYGQQAVSGYCQQGQQPYYNQQPQPSHLPPQAQYLQPAAAQSQQRYQPQQDMSQEGYGTRSQPPLAPGKSNHEDLNLIQQERPSSLPDLSGSIDDLPTGTEATLSSAVSASGSTSSQGDQSNPAQSPFSPHASPHLSSIPGGPSPSPVGSPVGSNQSRSGPISPASIPGSQMPPQPPGSQSESSSHPALSQSPMPQERGNYSRTPTYSGVPSASYSGPGPGMGINANNQMHGQGPAQPCGAMPLGRMPSAGMQNRPFPGTMSSVTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLVASSSPYSQSMNNNSSLMSTQAQPYSMTPTMVNSSTASMGLADMMSPSESKLSVPLKADGKEEGVSQPESKSKDSYGSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSPKSSSSSTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKTERGEEPPPEVFSTGDSKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQSGRSSTVSVHDPFSDVSDSAYPKRNSMTPNAPYQQGMGMPDMMGRMPYEPNKDPFSGMRKVPGSSEPFMTQGQVPNSGMQDMYNQSPSGAMSNLGMGQRQQFPYGTSYDRRHEAYGQQYPGQGPPTGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYGSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYNRERMQGPGQMQPHGIPPQMMGGPMQSSSSEGPQQNMWATRNDMPYPYQSRQGPGGPAQAPPYPGMNRTDDMMVPEQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQSSYQTPPSLPNHISRAPSPASFQRSLESRMSPSKSPFLPTMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPILKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHRSGKKDDSQSLEDDSGKEDDDAECLVEEEEEEEEEEEDSEKIESEGKSSPALAAPDASVDPKETPKQASKFDKLPIKIVKKNKLFVVDRSDKLGRVQEFSSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSTGKKKELEGKGDSEEQPEKSIIATIDDVLSARPGALPEDTNPGPQTDSGKFPFGIQQAKSHRNIRLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDTLAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL | null | null | chromatin remodeling [GO:0006338]; dendritic cell dendrite assembly [GO:0097026]; dendritic spine development [GO:0060996]; neuron-neuron synaptic transmission [GO:0007270]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357] | brahma complex [GO:0035060]; nBAF complex [GO:0071565]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]; synapse [GO:0045202] | DNA binding [GO:0003677]; nucleosome binding [GO:0031491] | PF01388;PF12031; | 1.10.150.60;1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000255|PROSITE-ProRule:PRU00355}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). Binds DNA non-specifically. {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. | Mus musculus (Mouse) |
E9Q4S1 | PDE8B_MOUSE | MGCAPSIHVSQSGVIYCRDSDESNSPRQTSSVSQGPTAPLHGLFVQTDAADAMPPSRAAGPPGAVRVRRSRAELGSGSSTGSSGPATTTCRGRRRHCCSSAEAETQTSYTSVKVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQSRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDSNKQIHRIHRDSGDNSQTEPHSFRHKSRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHHSHSHLSMPITINDVPPSIAQLLDNEESWDFNIFELEAVTHKRPLVYLGLKVFSRFGVCEFLNCTETTLRAWLQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPLAAESEGSDCECNPTGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKTLRLPSDS | 3.1.4.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250}; | behavioral fear response [GO:0001662]; cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; negative regulation of insulin secretion [GO:0046676]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of steroid hormone biosynthetic process [GO:0090032]; neuromuscular process controlling balance [GO:0050885]; operant conditioning [GO:0035106]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; visual learning [GO:0008542] | cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872] | PF13426;PF08629;PF00233; | 1.10.1300.10;3.30.450.20; | Cyclic nucleotide phosphodiesterase family, PDE8 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; | null | PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. | null | null | FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
E9Q4Z2 | ACACB_MOUSE | MVLLLFLTCLVFSCLTFSWLKIWGKMTDSKPLTNSKVEANLLSSEESLSASELSGEQLQEHGDHSCLSYRGPRDASQQRNSLPSSCQRPPRNPLSSNDTWPSPELQTNWTAAPGPEVPDANGLSFPARPPSQRTVSPSREDRKQAHIKRQLMTSFILGSLDDNSSDEDPSAGSFQNSSRKSSRASLGTLSQEAALNTSDPESHAPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGLTVEWTEDSRHQGKCISVPEDVYEQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPIPFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYALKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGVILEAGCVVARLELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLPEPFFSMKLKDWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSGTRGYMKAVVLDLLRKYLNVEHHFQQAHYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQTDTLLFSKACTSLYSEEDSKSLREEPIHILNVAIQCADHMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLDISLYREVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVAFKMRFKTPEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKDNRSPVPITTPSDPIDREIEFTPTKAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDGLRLYEQPILIYIPPCAELRGGSWVVLDSTINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLVGQLGKAQLPDKDRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARTFFYWRLRRLLLEAQVKQEILRASPELNHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSAKDGLRSTIRENINYLKRDSVLKTIQSLVQEHPEVIMDCVAYLSQHLTPAERIQVAQLLSTTESPASS | 6.4.1.2 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250|UniProtKB:O00763}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; | acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]; malonyl-CoA biosynthetic process [GO:2001295]; negative regulation of catalytic activity [GO:0043086]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of gene expression [GO:0010629]; negative regulation of lipid catabolic process [GO:0050995]; pentose-phosphate shunt [GO:0006098]; positive regulation of heart growth [GO:0060421]; positive regulation of lipid storage [GO:0010884]; protein homotetramerization [GO:0051289]; purine nucleotide metabolic process [GO:0006163]; regulation of cardiac muscle hypertrophy in response to stress [GO:1903242]; regulation of glucose metabolic process [GO:0010906]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; tricarboxylic acid metabolic process [GO:0072350] | mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786; | 2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10; | null | PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000250|UniProtKB:O00763}.; PTM: Phosphorylated by AMPK at Ser-212 inactivates the enzyme (PubMed:24913514). Required for the maintenance of skeletal muscle lipid and glucose homeostasis (PubMed:24913514). {ECO:0000269|PubMed:24913514}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000250|UniProtKB:O00763}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309; Evidence={ECO:0000250|UniProtKB:O00763}; | null | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:O00763}. | null | null | FUNCTION: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (By similarity). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (By similarity). Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (PubMed:24913514). Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (PubMed:24913514). {ECO:0000250|UniProtKB:O00763, ECO:0000269|PubMed:24913514}. | Mus musculus (Mouse) |
E9Q555 | RN213_MOUSE | MECPQCGHVSSEKAPKFCSECGQKLPSAATVQGDLKNDNTLVVSSTPEGKTEQGAVLREEEVLLSSTDPGKELEKPEESDSNASWTTQMSKKEKRRRKRQGTISSSEAPSSGLWSLDMPPSPGSHNSALPQNQAQQGGAASQPGHPLDTENMPMEDGFVHTEGSGSPLQGQAAERTDAQSNLAPSDLAEVKDLNTSKPSVDKGLPLDGGPALSAFKGHPKMTDASQKAPLPESKGETSGQEKKVPPIDAAASPVKTAGKETGEDVRKPKPSPVSPVASKHGDQEAELKGKLATPVRKSNEGGNTQPEDQRKPGEGRNFAAAVKTQQAAAPQQAAAPEPTSAFNPRDTVTVYFHAIVSRHFGFNPEEHKVYVRGGEGLGQKGWTDACEMYCTQDLHDLGSLVEGKMDIPRQSLDKPIPYKYVIHRGGSSKDTVEYEFIYEQAQKKGEHVNRCLRVVSTSLGNGDWHQYDDIICMRSTGFFQQAKNRILDSTRKELLKGKKQAAVVMLDRIFSVLQPWSDINLQSFMTQFLQFYSVVREPMIHDGRARKWTSLQYEEKEVWTNLWEHVKKQMAPFLEGKSGESLPADCPVRSKLTLGLSILFMVEAAEFTVPKKDLDSLCYLLIPSAGSPEALHSDLSPVLRIRQRWRIYLTNLCLRCIDERCDRWLGILPLLHTCMQKSPPKKNSKSQPEDTWAGLEGISFSEFRDKAPTRSQPLQFMQSKMALLRVDEYLFRSWLSVVPLESLSSYLENSIDYLSDVPVRVLDCLQGISYRLPGLRKISNQNMKKDVENVFKMLMHLVDIYQHRIFGENLLQIYLTECLTLHETVCNITANHQFFEIPALSAELICKLLELSPPGHTDEGLPEKSYEDLVTSTLQEALATTRNWLRSLFKSRMLSISSAYVRLTYSEEMAVWRRLVEIGFPEKHGWKGSLLGDMEGRLKQEPPRLQISFFCSSQCRDGGLHDSVSRSFEKCVIEAVSSACQSQTSVLEGLSCQDLQKFGTLLSAVITKSWPVHNGEPVFDVDEIFKYLLKWPDVRQLFELCGTNEKIIDNITEEGRQLMATAESVFQKVAGELENGTIVVGQLELILEHQSQFLDIWNLNRRRLPSQEKACDVRSLLKRRRDDLLFLKQEKRYVESLLRQLGRVKHLVQVDFGNIEIIHSQDLSNKKLNEAVIKLPNSSSYKRETHYCLSPDIREMASKLDSLKDSHIFQDFWQETAESLNTLDKDPRELKVSLPEVLEYLYNPCYDNFYTLYENLKSGKITFAEVDAIFKDFVDKYDELKNDLKFMCTMNPQDQKGWISERVGQIKEYHTLHQAVSSAKVILQVRRALGVTGDFSVLNPLLNFADSFEDFGNEKLDQISPQFIKAKQLLQDISEPRQRCLEELARQTELVAWLHKALEDINELKVFVDLASISAGENDIDVDRVACFHDAVQGYASLLYKMDERTNFSDFMNHLQELWRALDNDQHLPDKLKDSARNLEWLKTVKESHGSVELSSLSLATAINSRGVYVIEAPKDGQKISPDTVLRLLLPDGHGYPEALRTYSTEELKELLNKLMLMSGKKDHNSNTEVEKFSEVFSNMQRLVHVFIKLHCAGNMLFRTWTAKVYCCPDGGIFMNFGLELLSQLTEKGDVIQLLGALCRQMEDFLDNWKTVVAQKRAEHFYLNFYTAEQLVYLSSELRKPRPSEAALMMLSFIKGKCTVQDLVQATSACESKADRYCLREVMKKLPQQLLSEPSLMGKLQVIMMQSLVYMSAFLPHCLDLDALGRCLAHLATMGGTPVERPLPKGLQAGQPNLILCGHSEVLPAALAIYMQAPRQPLPTFDEVLLCTPATTIEEVELLLRRCLTSGSQGHKVYSLLFADQLSYEVGCQAEEFFQSLCTRAHREDYQLVILCDAAREHCYIPSTFSQYKVPLVPQAPLPNIQAYLQSHYQVPKRLLSAATVFRDGLCVGIVTSERAGVGKSLYVNTLHTKLKAKLRDETVPLKIIRLTEPHLDENQVLSALLPFLKEKYQKMPVIFHIDISTSVQTGIPIFLFKLLILQYLMDINGKIWRRSPGHLYLVEIPQGLSVQPKRSSKLNARAPLFKFLDLFPKVTCRPPKEVIDMELTPERSHTDPAMDPVEFCSEAFQRPYQYLKRFHQQQNLDTFQYEKGSVEGSPEECLQHFLIYCGLINPSWSELRNFAWFLNCQLKDCEASIFCKSAFTGDTLRGFKNFVVTFMILMARDFATPTLHTSDQSPGRQSVTIGEVVEEDLAPFSLRKRWESEPHPYVFFNGDHMTMTFIGFHLETNNNGYVDAINPSNGKVIKKDVMTKELFDGLRLQRVPFNIDFDNLPRYEKLERLCLALGIEWPIDPDETYELTTDNMLKILAIEMRFRCGIPVIIMGETGCGKTRLIKFLSDLKRGSVEAETMKLVKVHGGTTPSMIYSKVKEAERTAFSNKAQHKLDTILFFDEANTTEAVSCIKEILCDRTVDGEHLHEDSGLHIIAACNPYRKHSQEMILRLESAGLGYRVSAEETADRLGSIPLRQLVYRVHALPPSLIPLVWDFGQLNDSAEKLYIQQIVQRLVDSVSVNPSETCVIADVLSASQMFMRKRENECGFVSLRDVERCVKVFRWFHDHSDMLLKELDKFLHESSDSTHTFERDPVLWSLVMAIGVCYHASLEEKASYRTAIARCFPKPYNSSRAILDEVTHVQDLFLRGAPIRTNIARNLALKENVFMMVICIELKIPLFLVGKPGSSKSLAKIIVADAMQGQAAFSELFRCLKQVHLVSFQCSPHSTPQGIISTFKQCARFQQGKDLGQYVSVVVLDEVGLAEDSPKMPLKTLHPLLEDGCIEDDPAPYKKVGFVGISNWALDPAKMNRGIFVSRGSPNEKELIESAEGICSSDRLVQDKIRGYFAPFAKAYETVCQKQDKEFFGLRDYYSLIKMVFAKAKASKRGLSPQDITHAVLRNFSGKDNIQALSIFTASLPEARYKEEVSTVELIKQNIYPGPQASSRGLDGAESRYLLVLTRNYVALQILQQTFFEGQQPEIIFGSSFPQDQEYTQICRNINRVKICMETGKMVVLLNLQNLYESLYDALNQYYVYLGGQKYVDLGLGTHRVKCRVHTAFRLIVIEEKDVVYKQFPVPLINRLEKHYLDMNTVLQPWQKSIVQELQQWAHEFADVKADQFIARHKYSPADVFIGYHSDACASVVLQAVERQGCRDLTEELYRKVSEEARSILLDCATPDAVVRLSGSSLGSFTAKQLSQEYYYAQQHNSFVDFLQAHLRMTHHECRAVFTEITTFSRLLTGNDCDVLASELRGLASKPVVLSLQQYDTEYSFLKDVRSWLTNPGKRKVLVIQADFDDGTRSAQLVASAKYTAINEINKTQGTKDFVFVYFVTKLSRMGSGTSYVGFHGGLWRSVHIDDLRRSTIMASDVTKLQNVTISQLFKPEDKPEQEEMEIETSQSKELAEEQMEVEDSEEMKKASDPRSCDCSQFLDTTRLVQSCVQGAVGMLRDQNESCARNMRRVTILLDLLNEDNTRNASFLRESKMRLHVLLNKQEENQVRSLKEWVTREAANQDALQEAGTFRHTLWKRVQDVVTPILASMIAHIDRDGNLELLAQPDSPAWVQDLWMFIYSDIKFLNISLVLNNTRSNSEMSFILVQSHMNLLKDAYNAVPFSWRIRDYLEELWVQAQYITDTEGLSKKFVEIFQKTPLGVFLAQFPVAQQQKLLQSYLKDFLLLTMKVSSREELMFLQMALWSCLRELQEASGTPDETYKFPLSLPWVHLAFQHFRTRLQNFSRILTIHPQVLSSLSQAAEKHSLAGCEMTLDAFAAMACAEMLKGDLLKPSPKAWLQLVKNLSTPLELVCSEGYLCDSGSMTRSVIQEVRALWNRIFSIALFVEHVLLGTESHIPELSPLVTTYVSLLDKCLEEDSNLKTCRPFVAVMTTLCDCKDKASKKFSRFGIQPCFICHGDAQDPVCLPCDHVYCLRCIQTWLIPGQMMCPYCLTDLPDKFSPTVSQDHRKAIEKHAQFRHMCNSFFVDLVSTMCFKDNTPPEKSVIDTLLSLLFVQKELLRDASQKHREHTKSLSPFDDVVDQTPVIRSVLLKLLLKYSFHEVKDYIQNYLTQLEKKAFLTEDKTELYLLFISCLEDSVHQKTSAGCRNLEQVLREEGHFLRTYSPGLQGQEPVRIASVEYLQEVARVRLCLDLAADFLSELQEGSELAEDKRRFLKHVEEFCTRVNNDWHRVYLVRKLSSQRGMEFVQSFSKQGHPCQWVFPRKVIAQQKDHVSLMDRYLVHGNEYKAVRDATAKAVLECKTLDIGNALMACRSPKPQQTAYLLLALYTEVAALYRSPNGSLHPEAKQLEAVNKFIKESKILSDPNIRCFARSLVDNTLPLLKIRSANSILKGTVTEMAVHVATILLCGHNQILKPLRNLAFYPVNMANAFLPTMPEDLLVHARTWRGLENVTWYTCPRGHPCSVGECGRPMQESTCLDCGLPVGGLNHTPHEGFSAIRNNEDRTQTGHVLGSPQSSGVAEVSDRGQSPVVFILTRLLTHLAMLVGATHNPQALTVIIKPWVQDPQGFLQQHIQRDLEQLTKMLGRSADETIHVVHLILSSLLRVQSHGVLNFNAELSTKGCRNNWEKHFETLLLRELKHLDKNLPAINALISQDERISSNPVTKIIYGDPATFLPHLPQKSIIHCSKIWSCRRKITVEYLQHIVEQKNGKETVPVLWHFLQKEAELRLVKFLPEILALQRDLVKQFQNVSRVEYSSIRGFIHSHSSDGLRKLLHDRITIFLSTWNALRRSLETNGEIKLPKDYCCSDLDLDAEFEVILPRRQGLGLCGTALVSYLISLHNNMVYTVQKFSNEDNSYSVDISEVADLHVISYEVERDLNPLILSNCQYQVQQGGETSQEFDLEKIQRQISSRFLQGKPRLTLKGIPTLVYRRDWNYEHLFMDIKNKMAQSSLPNLAISTISGQLQSYSDACEALSIIEITLGFLSTAGGDPGMDLNVYIEEVLRMCDQTAQVLKAFSRCQLRHIIALWQFLSAHKSEQRLRLNKELFREIDVQYKEELSTQHQRLLGTFLNEAGLDAFLLELHEMIVLKLKGPRAANSFNPNWSLKDTLVSYMETKDSDILSEVESQFPEEILMSSCISVWKIAATRKWDRQSR | 2.3.2.-; 2.3.2.27; 3.6.4.- | null | angiogenesis [GO:0001525]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; regulation of lipid metabolic process [GO:0019216]; sprouting angiogenesis [GO:0002040]; ubiquitin-dependent protein catabolic process [GO:0006511]; xenophagy [GO:0098792] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00097;PF20173; | 3.40.50.300;3.30.40.10; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}. | 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; Evidence={ECO:0000250|UniProtKB:Q63HN8}; 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; Evidence={ECO:0000269|PubMed:32573437}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000269|PubMed:32573437}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}. | null | null | FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:32573437). {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:32573437, ECO:0000269|PubMed:34012115}. | Mus musculus (Mouse) |
E9Q557 | DESP_MOUSE | MSCNGGSHPRINTLGRMTRAESGPDLRYEMTYSGGGGGGGGGGGGGTSRTFYSHSRRCTVNDQNSDGYCQTGTMSRHQNQNTIQEMLQNCSDCLMRAELIAQPELKFGEGMQLAWNRELDEYFTQANDQMEIIDGLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGAGGYTCQSGSGWDEFTKRLTGECLGWMRQQREEMDLMAWGVDAGSVEQHINSHRSIHNTIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFSIRMSQLEVKEKELNKLKQESDQLVLNQHPASDKIEAYMDTLQTQWSWILQITKCIDVHLKENAAYFQFFEEAQSTEAYLKGLQDSIRKKYPCDKNMPLQHLLEQIKELEKEREKIIEYKRQVQNLVNKSKKIVQLKPRNPDYRSNKPIILRALCDYKQDQKIVHKGDECILKDNNERSKWYVTGPGGVDMLVPSVGLIIPPPNPLAVDLSCKIEQYYEAILALWNQLYINMKSLVSWHYCMIDIEKIRAMTIAKLKTMRQEDYMKTIEDLELHYQDFIKNSQGSEMFGDDDKRRMQSQFTDAQKHYQTLVIQLPGHPQHQTVTKTEITHLGTCQDVNHNKVIETNRENDKQETWLLMELQKIRRQMEHCEARMTLKNLLLAEQGSTHHITVKINELKSVQNDSQALAEVLNQLKDMLANFRGSEKYCYLQNEIFGLFQKLENINGVSDGYLNSLCSVRALLQAILQTEDMLKVYEARLTEEETVCLDLDKVEAYRCGLKKIKNDLNLKKSLLATMKTELQKAQQIHSQSSQQYPLYDLDLGKFTEKVTQLTDRWQKIDKQIDFRLWDLEKQIKQLRNYRDNYQSFCKWLYDAKRRQDSLESMKFGDSNTVMRFLNEQKNLHSEISGKRDKSEEVHKIAELCANSIKDYELQLASYTSGLETLLNIPIKRTMVQSPSGVILQEAADIHARYIELLTRSGDYYRFLSEMLKSLEDLKLKNTKIEVLEEELRLARDANSENCNKNKFLDQNLQKYQAECSQFKAKLVSLEELKRQAELDGKSAKQNLDKCYGQIKELNEKITRLTYEIEDEKRRRKTVEDRFDQQKNDYDQLQKARQCEKENLSWQKLESEKAIKEKEYEIERLRVLLQEEGARKREYENELAKVRNHYNEEMSNLRNKYETEINITKTTIKEISMQKEDDSKNLRNQMDRLSRENRDLKDEIVRLNDSILQATEQRRRAEENALQQKACGSETMQKKQRLEIELKQVIQQRSEDNARHKQSLEEAAKTIQDKNKEIERLKAEYQEEAKRRWEYENELSKVRNSYDEEIISLKNQFETEINITKTTIHQLTMQKEEDTSGYRAQIDNLTRENRSLCEEVKRLKNTLAQTTENLRRVEENAQQQKATGSEMSQRKQQLEIELRQVTQMRTEESMRYKQSLDDAAKTIQDKNKEIERLKQLVDKETNERKCLEDENSKLQRVQYDLQKANNSATEAMSKLKVQEQELTRLRIDYERVSQERTVKDQDITRIQSSLKDLQLQKQKAEEELSRLKRTASDESSKRKMLEEELEAMRRSLKEQAVKITNLTQQLEQASIVKKRSEDDLRQQRDVLDGHVREKQRTQEELRRLSLDVEALRRQLVQEQENVKQAHLRNEHFQKAIEDKSRSLNESKIEIERLQSLTENLTKEHLMLEEELRNLRLEYDDLRRGRSEADSDKNSTISELRSQLQISNNRTLELQGLINDLQRERENLRQEIEKFQKQALEASNRIQESKSQCTQVVQERESLLVKIKVLEQDKARLQRLEDELNRAKATLEAESRVKQRLECEKQQIQNDLNQWKTQYSRKEETIRKIESEREKSEREKNSLRSEIERLQAEIKRIEERCRRKLEDSSRETQSQLESERCRLQKEIEKLRQRPYGSHRETQTEYEWTVDSSKLVFDGLRKKVTAMQLYECQLIDKTTLDKLLKGKKSVEEVASEIQPFLRGAGAIAGASASPKEKYSLVEAKRKKFITPESTVMLLEAQAATGGIIDPHRNEKLTVDNAVARDLIDFDDRQQIYTAEKAITGFDDPFSGKTVSVSEAIKKNLIDRETGMRLLEAQLASGGVVDPVNSVFLPKDVALARGLIDRDLYRSLNDPRDSQKNFVDPITKKKVSYMQLRERCRIEPHTGLLLLSVQKRSMSFQGIRQPVTVTELVDSGILRPSTVNELESGQISYDEVGERIKDFLQGSSCIAGIYNETTKQKLGIYEAMKIGLVRPGTALELLEAQAATGFIVDPVSNLRLPVEEAYKRGLVGIEFKEKLLSAERAVTGYNDPETGNIISLFQAMNKELIEKGHGIRLLEAQIATGGIIDPKESHRLPVDMAYKRGYFNEELSEILSDPSDDTKGFFDPNTEENLTYLQLKERCIKDEETGLCLLPLKEKKKQVQTSQKNTLRKRRVVIVDPETNKEMSVQEAYKKGLIDYDTFKELCEQECEWEEITITGSDGSTRVVLVDRKTGSQYDIQDAIDKGLVDRKFFDQYRSGSLSLTQFADMISLKNGVGNSSGLGGSVNDDVFSSSRHDSVSKISTISSVRNLTIRSSSLSDPLEESSPIAAIFDTENLEKISIAEGIERGIVDSITGQRLLEAQACTGGIIHPTTGQKLSLQDAVNQGLIDQDMATRLKPAQKAFIGFEGVKGKKKMSAAEAVKEKWLPYEAGQRFLEFQFLTGGLVDPEVHGRISTEEAIRKGFIDGRAAQRLQDISSYAKILTCPKTKLKISYKDAMNRSMVEDITGLRLLEAASVSSKGLPSPYNMSAPGSRSGSRSGSRSGSRSGSRSGSRRGSFDATGNSSYSYSYSFSSSSIGGY | null | null | adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; epithelial cell-cell adhesion [GO:0090136]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109]; keratinocyte differentiation [GO:0030216]; protein localization to cell-cell junction [GO:0150105]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; skin development [GO:0043588]; ventricular compact myocardium morphogenesis [GO:0003223]; wound healing [GO:0042060] | adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | protein kinase C binding [GO:0005080]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198] | PF00681;PF17902;PF18373;PF21019; | 1.20.58.1060;1.20.58.60;3.30.160.780;3.90.1290.10;2.30.30.40; | Plakin or cytolinker family | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000269|PubMed:15479741, ECO:0000269|PubMed:22515648}. Cell membrane {ECO:0000269|PubMed:21285247, ECO:0000269|PubMed:22515648, ECO:0000269|PubMed:26403541}. Note=Localizes at the intercalated disk in cardiomyocytes. {ECO:0000269|PubMed:15479741, ECO:0000269|PubMed:26403541}. | null | null | null | null | null | FUNCTION: Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}. | Mus musculus (Mouse) |
E9Q5C9 | NOLC1_MOUSE | MADTGLRRVVPSDLYPLVLRFLRDSQLSEVASKFAKATGATQQDANASSLLDIYSFWLNRSTKAPKVKLQSNGPVTKKAKKETSSSDSSEDSSEDEDKKAQGLPTQKAAAQVKRASVPQHAGKAAAKASESSSSEESSEEEEEDKKKKPVQQKAAKPQAKAVRPPAKKAESSESDSDSDSDSSSEEETPQTQKPKAAVAAKAQTKAEAKPGTPAKAQPKVANGKAAASSSSSSSSDDSEEEKKAAAPPKKTVPKKQVVAKAPVKVAAAPTQKSSSSEDSSSEEEEGQRQPMKKKAGPYSSVPPPSVPLPKKSPGTQAPKKAAAQTQPADSSDDSSDDSDSSSEEEKKPPAKTVVSKTPAKAAPVKKKAESSSDSSDSDSSEDEAPAKPVSTTKSPKPAVTPKPSAAKAVTTPKQPAGSNQKPQSRKADSSSSEEESSSSEEEEASKKSATTPKAKVTAKAAPAKQAPQAAGDSSSDSDSSSSEEEEKTPKPPAKKKAAGGAVSTPAPGKKAEAKSSSSSSSSSSEDSSEEEKKKKPKATTPKIQASKANGTPASLNGKAAKESEEEEEEEETEEKKKAAGTKPGSGKKRKQNETADEATTPQAKKVKLETPNTFPKRKKGERRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSVKFDSE | null | null | box H/ACA RNA metabolic process [GO:0033979]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; nucleolus organization [GO:0007000]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of protein import into nucleus [GO:0042306]; regulation of translation [GO:0006417] | box C/D RNP complex [GO:0031428]; box H/ACA snoRNP complex [GO:0031429]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532] | box C/D RNA binding [GO:0034512]; box C/D snoRNP complex binding [GO:0062064]; box H/ACA snoRNA binding [GO:0034513]; box H/ACA snoRNP complex binding [GO:0062065]; nuclear localization sequence binding [GO:0008139]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein kinase inhibitor activity [GO:0004860]; protein-macromolecule adaptor activity [GO:0030674]; TFIIB-class transcription factor binding [GO:0001093] | PF05022; | null | NOLC1 family | PTM: Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated proteins in the cell. {ECO:0000250|UniProtKB:Q14978}.; PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue (PubMed:15604408, PubMed:17873058). {ECO:0000269|PubMed:15604408, ECO:0000269|PubMed:17873058}.; PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. {ECO:0000250|UniProtKB:Q14978}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14978}. Cytoplasm {ECO:0000250|UniProtKB:Q14978}. Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. {ECO:0000250|UniProtKB:Q14978}. | null | null | null | null | null | FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (By similarity). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (By similarity). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:11424213). It has intrinsic GTPase and ATPase activities (By similarity). {ECO:0000250|UniProtKB:Q14978, ECO:0000269|PubMed:11424213}. | Mus musculus (Mouse) |
E9Q5F9 | SETD2_MOUSE | MKPLPSQQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPVFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSFTKKTLQNRFLTALSNEKQSDSPNSPAPPLQVDSNPKVKMDAGDTFPATEESSPPKSRVELGRIHFKKHLLHVTSRPQLAASTTAASPLPPTTQLPAVLAESMIDSPPSSPPPPPPPPQASSPSPPAQISEPVALPQPPATALMTSPPGPLPGDVAVRAQKESPVKSGPEVLEVDTKQDIVSNSLEEHTVQTLKEQADHLLQKEDSHIGKEEEVSDGSKISLSSKKASSKKKSSQFEGTFLGSESDEDSVRTSSSQRSHDLKSSTSIDKERDFKKSSAPSKSEDLGKSSRSKTERDDRYCSYSKLERDTRYVSSRCRSERDRRRSRSRSRSDRASRTSLSYSRSERSHYYDSERRYHRSSPYRERTRYSRPYTDNRARESSDSEDEYKKTYPRRTSAHSYRDLRTSSSYSKFDRDCKTETSYLEMERRGKYTSKLERESKRTSEHETIKRCCSPPNELGFRRGSSYSKHDNSTSRYKSALSKSISKNDKFKNSFCCTELNEENKQSHSFSLQTPCSKGSELRTINKISEREKTGSPTPSNQLNDSPTFKKLDESPVLKPEFIGHDGRESIKELELSKVKNDQLRNFCSIELNVNGSPETEADVATFCTSKTDAISMTSDDSVTGSEVSPLIKACMLSSNGFQNVGRCRERDSDDTCRQHNTSKSPFREMEPLLSPHHDKLMSLPVKTIDYPKTLIKEPVDKRHSCCKTKDSDIYCSPNENPEAENAEPSAMTISSHSFVNVHLESKTVICDNREPTDRHSENTCDEYKQSIGSTSSASHNHFDGLYEPIGSSGISSLQSPPSGIRCEENTSPTLDAVESKKGIDFLKYARKETDVGSALPDSGKGFSWENRHNNVLSGQSLQEAQEEGNSILHERRGRPEIPLDEEQRGHTHISDDSEVVFPYDLNLTMEDSDGITYTLKCDSSGNAPEIVSTVHEDYSGSSASSSDESDSEDTESDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYKHYSDRWEDGLETRRHAYEEEYESKGCSQTEKYFLHKGTERSAESCYSQFGRKADNHLPDIAHAQSDGVDSTSQTDSRSDHLGHLNPEDTLRAKTSRPQELPVYSDDFEDLPNKSRQQMIFSNRPDSSRLGKTELSFSSSCDISRMDGLHSSEELRNLGWDFSQQERPTTTYQQPDSSYGTCGTHKYQQSTEHYGGTHNYWQGNGYWDPRSAGRPPGTGLAYDRIQGQVPDSLTDDREEEEHWDQRSGSHFSSPSNKFFFHQKDKGSVQAPEISSNSIKDALVMNERKDFSKNFEKNDIKERGPPKKRRQELESDSESDGELQARKKVRVEMEQGESSVPQHSELMGPSCAMDDFRDPQRWKEFAKLGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEVACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLKLIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPQLSEGDGYSSENTSRAHTPLNTPDPSAKPSTEMDTDTPKKLIFRRLKIISENSMDSAVSDVTSELECKDGKEDLDQLETVTVEEDEELQSQQLLPQQLCESKVESEATIEVSKLPTSEPEADTETEPKDSNGTKLEETIAEETPSQDEEEGVSDVESERSQEPPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKESTVAERGRDAAAFRDQTAPKTPNRSRERDPDKQSQNKEKRKRRGSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPFDSLGYNASHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTESLAAPPSVPVVPHVAASVEVSSSQYVAQNESVVHQDSNVPVMPVQAPGPVQGQNYNVWESNQQSVSVQQQYSPAQSQTTIYYQGQTCSTVYSVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPTAAVTSIVAPGQPQSLQPPEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKTSKKPKTAEADTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE | 2.1.1.-; 2.1.1.359 | null | angiogenesis [GO:0001525]; cell migration involved in vasculogenesis [GO:0035441]; coronary vasculature morphogenesis [GO:0060977]; defense response to virus [GO:0051607]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic organ development [GO:0048568]; embryonic placenta morphogenesis [GO:0060669]; endodermal cell differentiation [GO:0035987]; forebrain development [GO:0030900]; mesoderm morphogenesis [GO:0048332]; microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mismatch repair [GO:0006298]; morphogenesis of a branching structure [GO:0001763]; neural tube closure [GO:0001843]; nucleosome organization [GO:0034728]; peptidyl-lysine trimethylation [GO:0018023]; pericardium development [GO:0060039]; positive regulation of autophagy [GO:0010508]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of ossification [GO:0045778]; regulation of cytokinesis [GO:0032465]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of gene expression [GO:0010468]; regulation of mRNA export from nucleus [GO:0010793]; regulation of protein localization to chromatin [GO:1905634]; response to alkaloid [GO:0043279]; response to metal ion [GO:0010038]; response to organic cyclic compound [GO:0014070]; response to type I interferon [GO:0034340]; stem cell development [GO:0048864]; stem cell differentiation [GO:0048863]; transcription elongation by RNA polymerase II [GO:0006368]; vasculogenesis [GO:0001570] | chromosome [GO:0005694]; nucleus [GO:0005634] | alpha-tubulin binding [GO:0043014]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; metal ion binding [GO:0046872]; protein-lysine N-methyltransferase activity [GO:0016279] | PF17907;PF00856;PF08236;PF00397; | 2.20.70.10;1.20.930.10;2.170.270.10;1.10.1740.100; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET2 subfamily | PTM: May be automethylated. {ECO:0000250|UniProtKB:Q9BYW2}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18157086}. Chromosome {ECO:0000269|PubMed:18157086}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; Evidence={ECO:0000269|PubMed:18157086}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000250|UniProtKB:Q9BYW2}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000269|PubMed:27518565}; | null | null | null | null | FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:18157086, PubMed:20133625). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (By similarity). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (PubMed:18157086, PubMed:20133625). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (By similarity). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (By similarity). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (By similarity). Acts as a tumor suppressor (By similarity). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (By similarity). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (By similarity). Required during angiogenesis (PubMed:20133625). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (PubMed:25242323). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (By similarity). {ECO:0000250|UniProtKB:Q9BYW2, ECO:0000269|PubMed:18157086, ECO:0000269|PubMed:20133625, ECO:0000269|PubMed:25242323, ECO:0000269|PubMed:27518565}. | Mus musculus (Mouse) |
E9Q5G3 | KIF23_MOUSE | MKSAKAKTVRKPVIKKGSQTNLKDPVGVYCRVRPLSFPDQECCVEVINSTTLQLHTPEGYRLNRNGDYKETQYSFKRVFGTHTTQKELFDVVANPLVDDLIHGKNGLLFTYGVTGSGKTYTMTGSPGSGGLLPRCLNMIFNSIGSFQAKRYVFKSNDRNSMEIQCEVDALLERQKREALPIPKTPSSKRQADPEFADMINVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVQFDPIKPKLPQSKTLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFSIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTKAEGNRLREAGNINQSLMTLRTCMEVLRENQTYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEESLQVMRFAEVTQEVEVARPVDKVICGLTPGRRYRNLPRGGPVGDEPLVPEVILQSFPPLPPCKLLDINDEETLPKLADTLEKRHHLRQLMTEDLNKKCLAFKALLKEFDNSLSNKENYVQEKLNEREKVISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELESQNQKLQRQFSDKRRLEARLQGMVTETSMKWQKECERRVAATQLEMQNKLWVKDEKLKQLKAIVTEPKPEKPERPSRERDREKIIPRSVSPSPLPLSSNNIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKLSPFSTPVNVTSLARHRQQEPGQSKTCIVSDRRRGMCWTEGREMVPTFSSEIGVEEDHCRRNTPIPVRHRRSRSAGSRWVDHKPASNVQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIQTKVIKGDVYKTRGGGQSVQFTDIETLKQELPTGSRKRRSSTLAPAQPDGTESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP | null | null | microtubule-based movement [GO:0007018]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; Flemming body [GO:0090543]; intercellular bridge [GO:0045171]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF16540; | 3.40.850.10;2.60.40.4330; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody, Midbody ring {ECO:0000269|PubMed:19020301}. Note=Localizes to the interzone of mitotic spindles (By similarity). Detected at the midbody during later stages of mitotic cytokinesis. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
E9Q5G7 | OOG1_MOUSE | MVICLHCPDQDDSLEEVTEECYSPPTLQNLAIQSLLRDEALAISALTDLPQSLFPVIFEEAFTDGYIGILKAMIPVWPFPYLSLGKQINNCNLETLKAMLEGLDILLAQKVQTSRCKLRVINWREDDLKIWAGSHEGEGLPDFRTEKQPIENSAGCEVKKELKVTTEVLRMKGRLDESTTYLLQWAQQRKDSIHLFCRKLLIEGLTKASVIEIFKTVHADCIQELILRCICIEELAFLNPYLKLMKSLFTLTLDHIIGTFSLGDSEKLDEETIFSLISQLPTLHCLQKLYVNDVPFIKGNLKEYLRCLKKPLETLCISNCDLSQSDLDCLPYCLNICELKHLHISDIYLCDLLLEPLGFLLERVGDTLKTLELDSCCIVDFQFSALLPALSQCSHLREVTFYDNDVSLPFLKQLLHHTALLSQLIYECYPAPLECYDDSGVILTHRLESFCPELLDILRAKRQLHSVSFQTTKCSKCGGCYIYDRHTQCCRFVELL | null | null | negative regulation of apoptotic process [GO:0043066]; negative regulation of cell differentiation [GO:0045596]; negative regulation of DNA-templated transcription [GO:0045892]; oocyte development [GO:0048599]; positive regulation of cell population proliferation [GO:0008284] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | null | 3.80.10.10; | PRAME family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12890732, ECO:0000269|PubMed:16580637}. Cytoplasm {ECO:0000269|PubMed:12890732, ECO:0000269|PubMed:16580637}. Note=In early one-cell embryos, exists only in the cytoplasm and gradually moves to the nucleus at the middle one-cell stage. At the late one-cell and early two-cell stages, higher levels in nucleus than cytoplasm. After the middle two-cell stage, mainly cytoplasmic and completely cytoplasmic after the four-cell stage. {ECO:0000269|PubMed:12890732}. | null | null | null | null | null | FUNCTION: May down-regulate the expression of spermatogenesis-associated genes in female germ cells allowing their normal differentiation into oocytes (PubMed:29731491). May act as a Ras-mediated signaling protein in early embryogenesis. {ECO:0000269|PubMed:29731491, ECO:0000305|PubMed:16580637}. | Mus musculus (Mouse) |
E9Q5K4 | CP2CN_MOUSE | MELLGLPTLALLVLVMSLSLLSVWTKMRTGGRLPPGPTPLPIIGNILQLDLKDIPASLSKLAKEYGPVYTLYFGSWPTVVLHGYDVVKEALLNQGDEFLGRGPLPIIEDSQKGHGIVFSEGERWKLLRRFSLMTLKNFGMGKRSLEERVQEEARCLVEELHKTEAQPFDPTFILACAPCNVICSILFNERFPYNDKTFLNLMDLLNKNFYQLNSIWIQMYNLWPTIMKYIPGKHREFSKRLGGVKNFILEKVKEHQESLDPANPRDYIDCFLSKIEEEKHNLKSDFNLENLAICGSNLFTAGTETTSTTLRFGLLLLVKHPEVQAKVHEELDRVIGRHQPPSMKDKMKLPYTDAVLHEIQRYITLLPSSLPHAVVQDTKFRHYVIPKGTAVFPFLSSILLDQKEFPNPEKFDPGHFLDKNGCFKKTDYFVPFSLGKRSCVGEGLARMELFLFFTTILQKFSLKALVEPKDLDIKPVTTGLFNLPPPYKLRLVPR | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P33261}; | epoxygenase P450 pathway [GO:0019373]; icosanoid biosynthetic process [GO:0046456]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid 11,12-epoxygenase activity [GO:0008405]; arachidonic acid 14,15-epoxygenase activity [GO:0008404]; arachidonic acid epoxygenase activity [GO:0008392]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15084647}. Microsome membrane {ECO:0000269|PubMed:15084647}. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49884, 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:131975; Evidence={ECO:0000269|PubMed:15084647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885; Evidence={ECO:0000305|PubMed:15084647}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49880, 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:131970; Evidence={ECO:0000269|PubMed:15084647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881; Evidence={ECO:0000305|PubMed:15084647}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51472, 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:84024; Evidence={ECO:0000269|PubMed:15084647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51473; Evidence={ECO:0000305|PubMed:15084647}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 8,9-epoxy-(5Z,11Z,14Z,17Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52168, 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:136439; Evidence={ECO:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52169; Evidence={ECO:0000250|UniProtKB:P24470}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z,17Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52172, 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:136441; Evidence={ECO:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52173; Evidence={ECO:0000250|UniProtKB:P24470}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z,17Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52176, 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:136443; Evidence={ECO:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52177; Evidence={ECO:0000250|UniProtKB:P24470}; 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:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; Evidence={ECO:0000250|UniProtKB:P24470}; 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:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784; Evidence={ECO:0000250|UniProtKB:P24470}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:64980, 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:76624, ChEBI:CHEBI:137474; Evidence={ECO:0000250|UniProtKB:P24470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64981; Evidence={ECO:0000250|UniProtKB:P24470}; | null | PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000305|PubMed:15084647}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in polyunsaturated fatty acids (PUFAs) metabolism and signaling (PubMed:15084647). Catalyzes preferentially the epoxidation of double bonds of PUFAs (PubMed:15084647). Converts arachidonic acid (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-epoxyeicosatrienoate (EET) and 11R,12S-EET (PubMed:15084647). Plays a major role in the formation of EETs and hydroxy-EETs (HEETs) in kidney. Via EETs may inhibit the epithelial sodium channels (ENaCs) in nephron segments, preventing excessive sodium absorption during high dietary salt intake (PubMed:24368771, PubMed:24966089). Participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) by converting 20-hydroxyeicosatetraenoic acid (20-HETE) to 20,8,9-HEET, an activator of PPARA (By similarity). Metabolizes eicosapentaenoic acid (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers, 8,9-, 11,12-, 14,15-, and 17,18- EETeTr, preferentially producing 17R,18S enantiomer (By similarity). 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:15084647). {ECO:0000250|UniProtKB:P24470, ECO:0000269|PubMed:15084647, ECO:0000269|PubMed:24368771, ECO:0000269|PubMed:24966089}. | Mus musculus (Mouse) |
E9Q5K9 | YTDC1_MOUSE | MAADSREEKDGELNVLDDILTEVPEQDDELYNPESEQDKNEKKGSKRKSERMESTDTKRQKPSIHSRQLISKPLSSSVSNNKRIVSTKGKSVTEYKNEEYQRSERNKRLDADRKIRLSSSSSREPYKSQPEKTCLRKRDSERRAKSPTPDGSERIGLEVDRRASRSSQSSKEEVNSEDYGSDHETGSSGSSEQGNNTENEEEGGEEDVEEDEEVDEDAEDDEEVDEDAEEEEEEDEEEEEDEDEDEEEEEYEQDERDQKEEGNDYDTRSEASDSGSESVSFTDGSVRSGSGTDGSDEKKKERKRARGISPIVFDRSGSSASESYAGSEKKHEKLSSSVRAVRKDQTSKLKYVLQDARFFLIKSNNHENVSLAKAKGVWSTLPVNEKKLNLAFRSARSVILIFSVRESGKFQGFARLSSESHHGGSPIHWVLPAGMSAKMLGGVFKIDWICRRELPFTKSAHLTNPWNEHKPVKIGRDGQEIELECGTQLCLLFPPDESIDLYQLIHKMRHKRRMHSQPRSRGRPSRREPVRDVGRRRPEDYDIHNSRKKPRIDYPPEFHQRPGYVKDPRYQEVDSFTNLIPNRRFSGVRRDVFLNGSYNDYVREFHNMGPPPPWQGMPPYPGIEQPPHHPYYQHHAPPPQAHPPYSGHHPVPHEARYRDKRVHDYDMRVDDFLRRTQAVVSGRRSRPRERDRERERDRPRDNRRDRERDRGRDRERERERICDRDRDRGERGRYRR | null | null | dosage compensation by inactivation of X chromosome [GO:0009048]; in utero embryonic development [GO:0001701]; mRNA alternative polyadenylation [GO:0110104]; mRNA export from nucleus [GO:0006406]; mRNA splice site recognition [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; post-transcriptional regulation of gene expression [GO:0010608]; primary follicle stage [GO:0048160]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of mRNA splicing, via spliceosome [GO:0048024]; spermatogenesis [GO:0007283] | nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723] | PF04146; | 3.10.590.10; | null | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q9QY02}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29799838}. Nucleus speckle {ECO:0000250|UniProtKB:Q96MU7}. Note=Localizes to a novel subnuclear structure, the YT bodies. {ECO:0000250|UniProtKB:Q9QY02}. | null | null | null | null | null | FUNCTION: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:29262316, PubMed:29799838). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:29799838). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (By similarity). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (By similarity). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May also regulate alternative splice site selection (By similarity). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (By similarity). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (PubMed:29262316). Also recognizes and binds m6A on other RNA molecules (By similarity). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (By similarity). Also recognizes and binds m6A-containing single-stranded DNA (By similarity). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (PubMed:29799838). {ECO:0000250|UniProtKB:Q96MU7, ECO:0000269|PubMed:29262316, ECO:0000269|PubMed:29799838}. | Mus musculus (Mouse) |
E9Q5R7 | NAL12_MOUSE | MLPSTARDGLYRLSTYLEELEAGELKKFKLFLGIAEDLSQDKIPWGRMEKAGPLEMAQLMVAHMGTREAWLLALSTFQRIHRKDLWERGQGEDLVRVTPNNGLCLFESQSACPLDVSPNAPRKDLQTTYKDYVRRKFQLMEDRNARLGECVNLSNRYTRLLLVKEHSNPIWTQQKFVDVEWERSRTRRHQTSPIQMETLFEPDEERPEPPHTVVLQGAAGMGKSMLAHKVMLDWADGRLFQGRFDYVFYISCRELNRSHTQCSVQDLISSCWPERGISLEDLMQAPDRLLFIIDGFDKLHPSFHDAQGPWCLCWEEKQPTEVLLGSLIRRLLLPQVSLLITTRPCALEKLHGLLEHPRHVEILGFSEEARKEYFYRYFHNTGQASRVLSFLMDYEPLFTMCFVPMVSWVVCTCLKQQLESGELLRQTPRTTTAVYMFYLLSLMQPKPGTPTFKVPANQRGLVSLAAEGLWNQKILFDEQDLGKHGLDGADVSTFLNVNIFQKGIKCEKFYSFIHLSFQEFFAAMYCALNGREAVRRALAEYGFSERNFLALTVHFLFGLLNEEMRCYLERNLGWSISPQVKEEVLAWIQNKAGSEGSTLQHGSLELLSCLYEVQEEDFIQQALSHFQVVVVRSISTKMEHMVCSFCARYCRSTEVLHLHGSAYSTGMEDDPPEPSGVQTQSTYLQERNMLPDVYSAYLSAAVCTNSNLIELALYRNALGSQGVRLLCQGLRHASCKLQNLRLKRCQISGSACQDLAAAVIANRNLIRLDLSDNSIGVPGLELLCEGLQHPRCRLQMIQLRKCLLEAAAGRSLASVLSNNSYLVELDLTGNPLEDSGLKLLCQGLRHPVCRLRTLWLKICHLGQASCEDLASTLKMNQSLLELDLGLNDLGDSGVLLLCEGLSHPDCKLQTLRLGICRLGSVACVGIASVLQVNTCLQELDLSFNDLGDRGLQLLGEGLRHQTCRLQKLWLDNCGLTSKACEDLSSILGISQTLHELYLTNNALGDTGVCLLCKRLRHPGCKLRVLWLFGMDLNKKTHRRMAALRVTKPYLDIGC | null | null | cellular response to cytokine stimulus [GO:0071345]; dendritic cell migration [GO:0036336]; ERK1 and ERK2 cascade [GO:0070371]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 production [GO:0032692]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of Toll signaling pathway [GO:0045751]; positive regulation of MHC class I biosynthetic process [GO:0045345]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; regulation of canonical NF-kappaB signal transduction [GO:0043122] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; protein-macromolecule adaptor activity [GO:0030674] | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P59046}. | null | null | null | null | null | FUNCTION: Plays an essential role as an potent mitigator of inflammation (PubMed:26521018, PubMed:30559449). Primarily expressed in dendritic cells and macrophages, inhibits both canonical and non-canonical NF-kappa-B and ERK activation pathways (PubMed:30559449). Functions as a negative regulator of NOD2 by targeting it to degradation via the proteasome pathway (PubMed:30559449). In turn, promotes bacterial tolerance (PubMed:30559449). Inhibits also the RIGI-mediated immune signaling against RNA viruses by reducing the E3 ubiquitin ligase TRIM25-mediated 'Lys-63'-linked RIGI activation but enhancing the E3 ubiquitin ligase RNF125-mediated 'Lys-48'-linked RIGI degradation (By similarity). Acts also as a negative regulator of inflammatory response to mitigate obesity and obesity-associated diseases in adipose tissue (PubMed:30212649). {ECO:0000250|UniProtKB:P59046, ECO:0000269|PubMed:26521018, ECO:0000269|PubMed:30212649, ECO:0000269|PubMed:30559449}. | Mus musculus (Mouse) |
E9Q612 | PTPRO_MOUSE | MGHLPRGTLGGRRLLPLLGLFVLLKIVTTFHVAVQDDNNIVVSLEASDIVSPASVYVVRVAGESKNYFFEFEEFNSTLPPPVVFKATYHGLYYIITLVVVNGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFSRVNISYWEGRDFRTMLYKDFFKGKTVFNHWLPGLCYSNITFQLVSEATFNKSTLVEYSGVSHEPKQHRTAPYPPRNISVRFVNLNKNNWEEPSGSFPEDSFIKPPQDSIGRDRRFHFPEETPETPPSNVSSGSPPSNVSSAWPDPNSTDYESTSQPFWWDSASAAPENEEDFVSALPADYDTETTLDRTEKPTADPFSAFPVQMTLSWLPPKPPTAFDGFNILIEREENFTDYLTVDEEAHEFVAELKEPGKYKLSVTTFSSSGACETRKSQSAKSLSFYISPTGEWIEELTEKPQHVSVHVLSSTTALMSWTSSQENYNSTIVSVVSLTCQKQKESQRLEKQYCTQVNSSKPVIENLVPGAQYQVVMYLRKGPLIGPPSDPVTFAIVPTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNPTTMTSEWTTYYEIAATVSLTASVRIASLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSVEYFNSLLYISWTYGDATTDLSHSRMLHWMVVAEGRKKIKKSVTRNVMTAILSLPPGDIYNLSVTACTERGSNTSLPRLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVFCQQLGSGHNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDTPSVPTFIAVSTMVTEVNPNVVVISVLAILSTLLIGLLLVTLVILRKKHLQMARECGAGTFVNFASLEREGKLPYSWRRSVFALLTLLPSCLWTDYLLAFYINPWSKNGLKKRKLTNPVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWLRKKQQFCISDVIYENVSKS | 3.1.3.48 | null | axon guidance [GO:0007411]; cell morphogenesis [GO:0000902]; glomerulus development [GO:0032835]; lamellipodium assembly [GO:0030032]; monocyte chemotaxis [GO:0002548]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of glomerular filtration [GO:0003105]; peptidyl-tyrosine dephosphorylation [GO:0035335]; peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [GO:1990264]; podocyte differentiation [GO:0072112]; regulation of glomerular filtration [GO:0003093]; regulation of synapse organization [GO:0050807]; slit diaphragm assembly [GO:0036060] | apical plasma membrane [GO:0016324]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839] | cadherin binding [GO:0045296]; protein homodimerization activity [GO:0042803]; protein tyrosine phosphatase activity [GO:0004725]; Wnt-protein binding [GO:0017147] | PF00041;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 3 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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: Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function. {ECO:0000269|PubMed:11086029}. | Mus musculus (Mouse) |
E9Q634 | MYO1E_MOUSE | MGSKGAYRYHWQSHNVKHSGVDDMVLLSKITESSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEVEMYQGAAQYENPPHIYALADSMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYVSRVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASPEQKQSLGITSMDYYYYLSLSGSYKVDDIDDKRDFQETLHAMNVIGIFSEEQTLVLQIVAGILHLGNISFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIESKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPKDWEESRVKHQVEYLGLKENIRVRRAGYAYRRVFQKFLQRYAILTKATWPVWRGDEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRERKYDGYARVIQKTWRKFVARKKYVQMREEASDLLLNKKERRRNSINRNFIGDYIGMEERPELQQFVGKREKIDFADTVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGVVKEVLKRRIEVERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLAKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFHQGFGDLAILKPSNKVLQVSIGPGLPKNSRPTRRNTVTSRGYPGGTKNNYPMRAAPAPPGCHQNGVIRNQFVPPPHAFGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTPESLDFLKVPDQGVAGVRRQTSSRPPPAGGRPKPQPKPKPQVPQCKALYAYDAQDTDELSFNANDIIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI | null | null | actin filament organization [GO:0007015]; endocytosis [GO:0006897]; glomerular basement membrane development [GO:0032836]; glomerular filtration [GO:0003094]; glomerulus development [GO:0032835]; hemopoiesis [GO:0030097]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; podocyte development [GO:0072015]; post-embryonic hemopoiesis [GO:0035166]; vasculogenesis [GO:0001570]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; brush border [GO:0005903]; clathrin-coated endocytic vesicle [GO:0045334]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microvillus [GO:0005902]; myosin complex [GO:0016459]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol binding [GO:0035091]; protein-containing complex binding [GO:0044877] | PF00063;PF06017;PF00018; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005011}. Cell junction {ECO:0000269|PubMed:19005011}. Cytoplasmic vesicle {ECO:0000305|PubMed:19005011}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:19005011}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19005011}. Note=In podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with F-actin (By similarity). Detected in cytoplasmic punctae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated ve (By similarity)sicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity). {ECO:0000250, ECO:0000269|PubMed:19005011}. | Mus musculus (Mouse) |
E9Q649 | GCNT4_MOUSE | MKIFRCCFKYTLQQKLFILLLTLWLFSLLKLLNVGRLLFPQRDIYLVEYSLSTSPFVRNRFPESGDAARDNVNCSGVYEHEPLEIGKSLEIRRRSIIDLEDGDVVAMTSDCDVYQTLRQYHEKLVSREEEDFPIAYSLVVHKDAIMVERLIRAIYNQHNLYCIHYDLKSPDTFKAAMNNLAKCFPNIFIASKLETVEYAHISRLQADWNCLSDLLKSSVQWKYVINLCGQDFPLKSNFELVTELKSLQGRNMLETVRPPSAKTERFTYHHELRQVPYDYMKLPVKTNVSKGAPPHNIQVFVGSAYFVLSRAFVKYIFNSSLVEDFFAWSKDTYSPDEHFWATLIRIPGIPGGISSSSQDVSDLQSKTRLVKWFYYEGFLYPNCTGSHLRSVCIYGAAELRWLLNEGHWFANKFDSKVDPILMKCLAEKLEEQQRKLIALSSEKFMTEGTRQSHTL | 2.4.1.102 | null | inter-male aggressive behavior [GO:0002121]; kidney morphogenesis [GO:0060993]; neutrophil homeostasis [GO:0001780]; protein glycosylation [GO:0006486]; thyroid hormone metabolic process [GO:0042403]; tissue morphogenesis [GO:0048729] | Golgi membrane [GO:0000139] | acetylglucosaminyltransferase activity [GO:0008375]; beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity [GO:0003829] | PF02485; | null | Glycosyltransferase 14 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102; Evidence={ECO:0000250|UniProtKB:Q9P109}; CATALYTIC ACTIVITY: Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923, Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607; EC=2.4.1.102; Evidence={ECO:0000250|UniProtKB:Q9P109}; | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity. {ECO:0000250|UniProtKB:Q9P109}. | Mus musculus (Mouse) |
E9Q6W4 | ZN296_MOUSE | MSRRKAGRVPRRVDPDTDTDIEMPDLVMDVKPDLDLRSLAQGPWIARDMPISDVKRQLQTASRPLGAPSTCAPRMPLSSKSSDRQPWTDKHPDLLTCGRCGKIFPLGAIIAFMDHKKQGCQLLQVSDPISESKELKALSCLQCGRQYTSPWKLLCHAQWDHGLCIYQTQHLDTPEAPLLGLAEVAAAMSAVAVVAPVESKPPPVSSAARRSPTCDVCKKTLSSFSNLKVHMRSHTGERPYSCDQCSYACAQSSKLNRHKKTHRQLAPGSPSTSASSRGVSPAAPPEPAAYAAAPASTLPSQTVEKAGAAATAGVQEPGAPGSGAQGGPGFVGWGAPAKVERTDPVKIEKTAPRKSHGPGGKCEFCGKSFTNSSNLTVHRRSHTGERPYTCDQCPYACAQSSKLNRHRRTHGLGTGKTVKCPHCLVPFGLQATLDKHLRQKHPEMA | null | null | negative regulation of dendrite development [GO:2000171]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24161396}. | null | null | null | null | null | FUNCTION: May be a transcriptional corepressor with KLF4. {ECO:0000269|PubMed:24161396}. | Mus musculus (Mouse) |
E9Q784 | ZC3HD_MOUSE | MSKIRRKVTVENTKTISESTSRRPSVFERLGPSTGSTTETQCRNWLKTGSCLYGNTCRFIHGPSPRGKGYSSNYRRSPERPTGDLRERMKNKRQDVDSESQKRNTEEPSSPVRKESSRGRHRDKEDIKIVKERTPESEEENVEWETNRDDSDNGDINYDYVHELSLEMKRQKIQRELMKLEQENMDKREEIIIQKEVSPEVVRSKLSPSPSLRKSSKSPKRKSSPKASSAGKKERKAAVVASPLLDQQRNSKGNQSKKKGPRTPSPPPPILEDIILGKKYKEKYKVKDRIEEKPRDGKDRGRDFEKQREKRDKPRSSSPGQHHSPLSSRHHSSSSQSGSSIQRHSPSPRRKRTPSPSYQRTLTPSLRRSASPYPTHCLSSPQRKQSPPRHRSPMREKGRHDHERTSQSHDRRHERREETRGKRDREKDTREERESEHDHRDDREPRDSRDRRDTRDRRELRDSRDMRDSREMRDYSRDAKESRDPRDSRSARDVHDYRDREARDAHARDVRDARDARDARDARDIRDVRDVRDVRDVRDVRDVRDVRDVRDVRDARDVRDVRDARDVRDVRDVRDGHRKEDVYQEEARSYGRNHLREESSRVELRNDSRNESRSEIRNDRMGRSRGRGPELPEKGSRGTRGSQMDSHSSGSNYHDSWETRSSYPERDRYPERDTRDPARDSSFERRHGERDRRDNRERDQRPSSPIRHQGRSEELERDERREERRIDRVDERRDDRVRDRDRDREREREREREREREREKERERELERERAREREREREKERERERERERDQRDRDHDREREREREREREKEREREREERERERERERERERERERERERERERERERERAREREKERERQREWEDKDKGRDDRREKREDIHVREDRIPRDSHEERKSKKRYRNEGSPSPRQSPKRRREHSPDSDTYHSGDDKNEKHRLLSQVVRPQESRSLSPSHLTEDRQGRWKEEDRKSERKESSRRYEEQELKEKLSCGDRQREQAESVDSSRVRAQDLLSHRQAEDRDRDGSDRAHDEKKKAKAPKKPVKKKKEEDVGVERGNLETHEDSQVFSPKKGQKKKNIEKKRKRSKGDSDVSDEEAAPQNKKKRGPRTPPLAIKEELADISTDKDGVLEDPLKKENTAFSDWSDEDVPDRTEGLEAEHTAATATPGSTPSPLSSLLPPPPPVAAASTAATALASSAVSATTSATSSSSAATSNTNGSEDSHRKCHRARGEKVEVSHVTLEDTPHRKLVDQKRSSSLGSNRSHRSHTSGRLRSPSNDSAHRSGDDQGSRKRVLHSGSRDREKTKSLEITGERKSRIDQLKRGEPSRSTSSDRQDSRSHSSRRSSPESDRQVHSRSGSFDSRDRLQERDRYEHDRERERDRRDPRQREWDREAEKEWPRTRDRDRLRERDRDRDRRRDLDRERERLISDPMERDRERERTFETSQLESGKRSEVKLESEHERDLEGSSRDSVALDKERMDRDLGSVQGFEDVSKAERTESLEGDDESKLDDAHSLGSGAGEGYEPISDDELDEILAGDAEKREDQQEEEKMPDPLDVIDVDWSGLMPKHPKEPREPGAALLKFTPGAVLLRVGISKKLAGSELFTKVKETCQQLVEKPKDADSLFEHELGALNMAALLRKEERASLLSDLGPCCKALCFRRDSAIRKQLVKNEKGTVKQAYTNTPMVDNELLRLSLRLFKKKATCHAPGQEKTEDGKLGPCSIQQELCVS | null | null | mRNA methylation [GO:0080009]; mRNA processing [GO:0006397]; regulation of stem cell population maintenance [GO:2000036]; RNA splicing [GO:0008380] | nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396] | metal ion binding [GO:0046872] | PF00642; | 4.10.1000.10; | ZC3H13 family | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q5T200}. Nucleus, nucleoplasm {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 (PubMed:29535189, PubMed:29547716). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (PubMed:29547716). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (PubMed:29547716). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (PubMed:29547716). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (PubMed:29535189). {ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}. | Mus musculus (Mouse) |
E9Q7D5 | ARHG5_MOUSE | MEAEEPEYGVSTEVPDIEELKTIPEGIMRSSQIPALDPEAQEDRDPSYKWTDGHRPVMNQSKVLRDMGDHTPNSMAIFFKKESSDMETSQEILLAEACNTPDQQEAVIQSLKDRLSRTIAAPELLACAVQEEWLDIPSKLDNRVGAELQSELMSLTLAVSKEKEEEETSPDTSIPRGSWPPCKTHPGETEQTQGSGSELLRQGKQLQLEATQENQGQEGFLQSQEAQGLEEQEGQEVEIQEEGTLNEGICFGGLLGEQEEVEEGFNGNEEEQKQGQIQSYMLLGGQWENEGLSGELEGLNYSERGQENRERRVWVLRDSEEEGQDQESREVEERRVATQYTENQRLVEKSEIVKRKQRDHDQTGKVMPVRDQKEVVDSGDRVQGNGDSGGQTAVEGSRPGEDSKPSLPVASVDPEVLSPGTLFPGISSSVADIPQIQKEPVCEELSPQAPALEPTEWSHQPISPPASFAPEESLDNRTHNSQQEEFRLRKGIEVVSASTSVAPSGTRDSPPFSPPNVFSSTATLSPVSSSVILPEETPTASASADTPHHCGPCETPPLPAKSSRYPCATSDTANPHSPLSSYTGVTQHLRSNSFPGSHRTEQTPDSLGMSLSFSHLELPQRPPKPAIYGSLTPRRNRRSRDGIVFSDSSTALFALKQDSEEFTSNPERPSSPHGSPTWGSPQNSAFAIGSPANVSSPPTVSMDMTIREALLPIPPEKRHSYSHIVERDGLLHEVASTLKRHSHPPPLTLSSGLHRSSKGSFSLVPDSTVARQHRPLPSTPESPNHTQTSIPSRLRYNKPLPPTPDMPEFYHPSISSSYISRMYRPLPPVPIIDPSSEPPPLPPKSRGRSKSIQGGVIHSGGQAKPRPNNQDWTASTLSVGRTSWPPATGRSTESLPLTSRCNNEVSPGLAFSNMTNLLSPSSPTTPWIPDLQRPTTKDESGLTEESEPPVRGSFRRSAPQEEFNNTRRSALGSRKNSEKPLHHQLEKASSWPHRRDPARTSESSSEQVVLGQVPNKQKGWNRQGLRRPSILPESSSDLRNPAAGRLPGSSDSVVFREKKPKEGMGGFSRRCSKLISSQLLYQEYSDVVLNKEIQSQQRLDSLAEPHGLSSPRHRRKALVSSDSYLQRLSMASSGSLWQEIPVVRNSTVLLSMTHEDQKLQEAKFELIVSEASYLRSLNIAVDHFQHSAQLRGTLSNQDHQWLFSRLQDVRDVSTTFLSDLEENFENNIFSFQVCDVVLNHAADFHRVYLPYVTNQTYQERTFQSLMNSNSSFREVLEKLESDPICQRLSLKSFLILPFQRITRLKLLLQNILKRTQPGSSEEAEATKAHHALEKLIRDCNSNVQRMRRTEELIYLSQKIEFECKIFPLISQSRWLVKSGELTALEFSVSPGLRRKLTTRPVHLHLFNDCLLLSRPREGSRFLVFDHAPFSSIRGEKCEMKLHGPHKNLFRLFLLHNAQGTQVEFLFRTETQSEKLRWISALAMPREELDLLECYDSPQVQCLRAYKPRENDELALEKADVVMVTQQSSDGWLEGVRLSDGEQGWFPVQQVEFISNPEVRAQNLKEAHRVKTAKLQLVEQQV | null | null | actin cytoskeleton organization [GO:0030036]; hematopoietic stem cell homeostasis [GO:0061484]; intracellular signal transduction [GO:0035556]; myeloid dendritic cell chemotaxis [GO:0002408]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein import [GO:1904591]; positive regulation of stress fiber assembly [GO:0051496] | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; podosome [GO:0002102] | guanyl-nucleotide exchange factor activity [GO:0005085]; lipid binding [GO:0008289] | PF15441;PF00169;PF00621;PF00018; | 1.20.900.10;2.30.29.30;2.30.30.40; | null | PTM: Activation of SRC induces tyrosine phosphorylation of ARHGEF5. {ECO:0000269|PubMed:21525037}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12774}. Cytoplasm {ECO:0000250|UniProtKB:Q12774}. Cell projection, podosome {ECO:0000269|PubMed:21525037}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor which activates Rho GTPases (PubMed:19713215, PubMed:21525037). Strongly activates RHOA (PubMed:19713215, PubMed:21525037). Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (PubMed:19713215). Involved in regulation of cell shape and actin cytoskeletal organization (PubMed:21525037). Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (By similarity). Required for SRC-induced podosome formation (PubMed:21525037). Involved in positive regulation of immature dendritic cell migration (PubMed:19713215). {ECO:0000250|UniProtKB:Q12774, ECO:0000269|PubMed:19713215, ECO:0000269|PubMed:21525037}. | Mus musculus (Mouse) |
E9Q7E2 | ARID2_MOUSE | MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSSVFGEEWREKTDRDFVKFWKDIVDDNEVRDLISDRNKAHEDTPGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEESNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFRTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVTSTLEVLYMLTEMGDVACTKIAKVEKSIDVLVCLVSMDAQMFGPDALAAVKLIEHPSSSHQVLSEIRPQAIEQVQTQTHIASGPASRAVVAQHAAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSTSSGQAHIHVIGVKRRALPLPIQMYYQQQPISTPVVRVDAVADLSPTPSPAGIPHGPQAAGNHFQRTPVTNQSSNLTATQMSFPVQGIHTVAQTVSRIPPNPSVHTHQQQNSPVTVIQNKAPIPCEVVKATVIQNSVPQTAVPVSISVGGAPAQNSVGQNHSAGPQPVTVVNSQTLLHHPSVMPQPSPLHTVVPGQVPSGTPVTVIQQTVPQSRMFGRVQSIPACTSTVSQGQQLITTSPQPMHTSSQQTAAGSQPQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQVVTIAGVPSPQPSRVGFQNIAPKPLPSQQVSPSVVQQPIQQPQQPAQQSVVIVSQPAQQGQAYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPPTNNQVPTAMSSSSTLQSQGPPPTVSQMLSVKRQQQQQHSPAAPAQQVQVQVQQPQQVQVQVQPQQPSAGVGQPAPNESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVANNQAAGFGVQGQTPAQQLLVGQQNVQLVQSAMPPAGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFATATVSQGNAAQLIAPAGLSMSGAQASAGLQVQTLPAGQSACTTAPLPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGTTNTSNGDTSESELQVGSLLNGRKYSDSSLPPSNSGKLQSETSQCSLISNGPSLELGENGAPGKQNSEPVDMQDVKGDLKKALVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPVEPQGTSGATQQDTAKGDQLERVSNGPVLTLGGSPSTSSMQEAPSVATPPLSGTDLPNGPLASSLNSDVPQQRPSVVVSPHSTAPVIQGHQVIAVPHSGPRVTPSALSSDARSTNGTAECKTVKRPAEDNDRDTVPGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAAQQKQQHPPTYMQSVAPQNTPMPPSPAVQVQGQPSSSQPSPVSASSQHADPVRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQVANQKSSTKQPTVGGTGSAPRAQKAIASHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEML | null | null | cardiac muscle cell proliferation [GO:0060038]; chromatin remodeling [GO:0006338]; circulatory system development [GO:0072359]; coronary artery morphogenesis [GO:0060982]; embryonic organ development [GO:0048568]; heart morphogenesis [GO:0003007]; homeostatic process [GO:0042592]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; nucleosome disassembly [GO:0006337]; positive regulation of cell differentiation [GO:0045597]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; kinetochore [GO:0000776]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF01388;PF02257; | 1.10.150.60;1.10.10.10; | RFX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00858}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000250|UniProtKB:Q68CP9, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. | Mus musculus (Mouse) |
E9Q7F2 | RN169_MOUSE | MAAAGPSTRASSAAAAAALSRRGRRGRCDEMAAAKAGAPGPASSPALLVLRSAPRPEESGCTGCLETPGEVAALPCSHSRCRGCASRAAGPGCRRCRPRGSGWARRRARDDGQAAAELMGERARRGQPEPCRPRRDGGAAASGPRPEPEPLAEPEFIFRTPIKLSKPGELSEEYGCLRKLRGEKLQEEKDCDDQIHKLLQEDSEMGKRKADEQKKRDEAVVLKTSLEQCPARLSDSENEEPSRGQMMQTHRSAFVSKNSSCSLAFLAGKLNTKVQRSQSCSDTVQDRVRSRLRTAPPNRAKITTITPGSTPIIGVLLSTQNNRCLSAPDLTIEKRLPFGSLSSLASLHKPERSISPESNDSISEELNHFKPIVCSPCTPPKRLPDGRVLSPLIIKSTPRNLTRSLQKQTSYEASPRILKKWEQIFQERQIKKTLSKATLTSLAPEAGEEFPGSDTIHSSKERPSLAFNTRLSRVQVLSECAGPTSTALECFPSVNQTKVEQDCVRKRSREFSLETCHSSEHGGASSGPSLEREQCEESGSTVDATLVKTCISTVMKTAAVNSLLPKNDVLGGVLKTKQQLKTLNHFDLGNGILVNSLGEEPIPSLRRGRKRRCKTKHLEQNGVKKLRPPSSDMDLAPKDPGLLEVGRKLQQEEEDQQLALQSHRMFDSERRTMSRRKGSVDQYLLRSSSLAGAK | 2.3.2.27 | null | DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; negative regulation of double-strand break repair [GO:2000780]; protein ubiquitination [GO:0016567] | cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]; ubiquitin modification-dependent histone binding [GO:0061649]; ubiquitin-protein transferase activity [GO:0004842] | null | 3.30.40.10; | RNF169 family | PTM: Phosphorylated by DYRK1A; phosphorylation increases RNF169 ability to block accumulation of TP53BP1 at the DSB sites. {ECO:0000250|UniProtKB:Q8NCN4}. | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8NCN4}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NCN4}. Note=Localizes to sites of double-strand breaks (DSBs) following DNA damage. Recruited to DSBs via recognition of RNF168-dependent ubiquitin products. {ECO:0000250|UniProtKB:Q8NCN4}. | 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: Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization. Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000250|UniProtKB:Q8NCN4}. | Mus musculus (Mouse) |
E9Q7G0 | NUMA1_MOUSE | MTLHATRAATLLSWVNSLHVADPVETVLQLQDCSIFIKIINTIHDTKEGQQILQQPLPERLDFVCSFLQKNRKHPSSTQCLVSVQKVIEGSEMELAKMIMLFLYQSTMSSRNLRDWEQFEYGVQAELAVILKFMLDHEESLNLTEDLESFLEKVPYTHASTLSEELSPPSHQTKRKIRFLEIQRIASSSSENNFLSGSPSSPMGDILQTPQFQMRRLKKQLADERSNRDDLELELSESLKLLTEKDAQIAMMQQRIDHLALLNEKQAASSQEPSELEELRGKNESLTVRLHETLKQCQNLKTEKSQMDRKISQLSEENGDLSFKVREFANHLQQLQGAFNDLIEEHSKASQEWAEKQARLENELSTALQDKKCLEEKNEILQGKLSQLEDQATRLQESPAPEKGEVLGDALQLDTLKQEAAKLATDNTQLQTRVETLECERGKQEAQLLAERSRFEDEKQQLASLIADLQSSVSNLSQAKEELEQASQAQGAQLTAQLTSMTGLNATLQQRDQELASLKEQAKKEQAQMLQTMQEQEQAAQGLRQQVEQLSSSLKLKEQQLEEAAKEQEATRQDHAQQLAIVAEAREASLRERDTARQQLETVEKEKDAKLESLQQQLQAANDARDNAQTSVTQAQQEKAELSQKIGELHACIEASHQEQRQVQARVTELEAQLKAEQQKTTEREKVVQEKAQLQEQLRALEESLKITKGSLEEEKRRAADALKEQQCRATEMEAESRSLMEQREREQKELEQEKAGRKGLEARIQQLEEAHQAETEALRHELAEATASQHRAESECERLIREVESRQKRFEARQQEEARYGAMFQEQLMALKGEKTGQEVQEEAVEIHSEGQPGQQQSQLAQLHASLAKAIQQVQEKEVRAQKLVDDLSALQEKMAATNKEVACLKTLVLKAGEQQETASLELLKEPPRAANRASDQLGEQQGRPFSSTHAAVKAMEREAEQMGGELERLRAALIKSQGQQQEERGQQEREVARLTQERGQAQADLAQEKAAKAELEMRLQNTLNEQRVEFAALQEALAHALTEKEGTDQELAKLRGQEAAQRTELKELQQTLEQLKIQLVKKEKEHPAGGASGEDASGPGTQSETAGKTDAPGPELQALRAEISKLEQQCQQQQQQVEGLTHSLKSERACRAEQDKALETLQGQLEEKARELGHNQAASASAQRELQALRAKAQDHSKAEEEWKAQVARGQQEAERKSSLISSLEEEVSILNRQVLEKEGESKELKRLVVAESEKSQKLEERLRLLQVETASNSARAAERSSALREEVQSLREEVEKQRVVSENSRQELASQAERAEELGQELKAWQEKFFQKEQALSALQLEHTSTQALVSELLPAKHLCQQLQAEQAAAEKRFREELEQSKQAAGGLQAELMRAQRELGELGSLRQKIVEQERAAQQLRAEKASYAEQLSMLKKAHGLLAEENRGLGERANLGRQFLEVELDQAREKYVQELAAVRTDAETHLAEMRQEAQSTSRELEVMTAKYEGAKVKVLEERQRFQEERQKLTAQVEELSKKLTEHDQASKVQQQKLKAFQAQRGESQQEVQRLQTQLNELQAQLSQKEQAAEHYKLQMEKAKTHYDAKKQQNQKLQEQLQDLEELQKENKELRSEAERLGRELQQAGLKTKEAEQTCRHLTAQVRSLEAQVAHADQQLRDLGKFQVATDALKSREPQVKPQLDLSIDSLDLSLEEGTPCSVASKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPTPARGQAPLETSLDSLGDAFPDSGRKTRSARRRTTQIINITMTKKLELEEPDSANSSFYSTQSAPASQANLRATSSTQSLARLGSPDDGNSALLSLPGYRPTTRSSARRSQARMSSGAPQGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPTLSLATITDEEMKTGDPRETLRRASMQPAQIAEGVGITTRQQRKRVSSETHQGPGTPESKKATSCFPRPMTPRDRHEGRKQSSTADTQKKAAPVLKQADRRQSMAFSILNTPKKLGNSLLRRGASKKTPAKVSPNPRSGTRRSPRIATTTTGTATVATTPRAKGKVKH | null | null | anastral spindle assembly [GO:0055048]; astral microtubule organization [GO:0030953]; cell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; meiotic cell cycle [GO:0051321]; microtubule bundle formation [GO:0001578]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of chromosome segregation [GO:0051984]; positive regulation of chromosome separation [GO:1905820]; positive regulation of hair follicle development [GO:0051798]; positive regulation of intracellular transport [GO:0032388]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of microtubule polymerization [GO:0031116]; positive regulation of mitotic spindle elongation [GO:1902846]; positive regulation of protein localization to cell cortex [GO:1904778]; positive regulation of protein localization to spindle pole body [GO:1902365]; positive regulation of spindle assembly [GO:1905832]; regulation of metaphase plate congression [GO:0090235]; regulation of mitotic spindle organization [GO:0060236] | cell cortex region [GO:0099738]; centrosome [GO:0005813]; chromosome [GO:0005694]; cortical microtubule [GO:0055028]; cytoplasmic microtubule bundle [GO:1905720]; cytosol [GO:0005829]; dendrite [GO:0030425]; lateral cell cortex [GO:0097575]; lateral plasma membrane [GO:0016328]; microtubule bundle [GO:0097427]; microtubule minus-end [GO:0036449]; microtubule plus-end [GO:0035371]; mitotic spindle astral microtubule [GO:0061673]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; neuronal cell body [GO:0043025]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]; spindle pole centrosome [GO:0031616] | disordered domain specific binding [GO:0097718]; dynein complex binding [GO:0070840]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; microtubule plus-end binding [GO:0051010]; phosphatidylinositol binding [GO:0035091]; tubulin binding [GO:0015631] | PF21670; | null | null | PTM: Phosphorylation and dephosphorylation on Thr-2037 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase. In metaphase, phosphorylation on Thr-2037 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning. In anaphase, dephosphorylated on Thr-2037 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation. Probably also phosphorylated on Thr-1997 and Ser-2069 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase. Phosphorylated on Ser-1751, Ser-1754, Ser-1771 and Ser-1816 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization. {ECO:0000250|UniProtKB:Q14980}.; PTM: ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles. {ECO:0000250|UniProtKB:Q14980}.; PTM: O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. {ECO:0000250|UniProtKB:Q14980}.; PTM: Ubiquitinated with 'Lys-63'-linked polyubiquitin chains. Deubiquitination by the BRISC complex is important for the incorporation of NUMA1 into mitotic spindle poles and normal spindle pole function, probably by modulating interactions between NUMA1, dynein-dynactin complex and importin-beta. {ECO:0000250|UniProtKB:Q14980}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19255246}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14980}. Nucleus matrix {ECO:0000250|UniProtKB:Q14980}. Chromosome {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:26766442}. Cell membrane {ECO:0000250|UniProtKB:Q14980}; Lipid-anchor {ECO:0000250|UniProtKB:Q14980}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14980}. Lateral cell membrane {ECO:0000269|PubMed:26766442}. Note=Mitotic cell cycle-dependent shuttling protein that relocalizes from the interphase nucleus to the spindle poles and cell cortex (PubMed:19255246, PubMed:24109598, PubMed:26765568). The localization to the spindle poles is regulated by AAAS (By similarity). In interphase, resides in the nuclear matrix (PubMed:19255246). In prophase, restricted to the interchromatin or condensed chromosome space. In prometaphase, after nuclear envelope disassembly, forms aggregates both in the spindle midzone and at duplicated centrosomes and astral microtubules (MTs) of the bipolar spindle apparatus. Translocates from the spindle midzone towards the spindle poles along spindle fibers in a MT- and dynein-dynactin-dependent manner until the anaphase onset (By similarity). In metaphase, recruited to the polar cortical region in a GPSM2- and GNAI1-dependent manner (PubMed:24109598). Excluded from the metaphase equatorial cortical region in a RanGTP-dependent manner. Phosphorylation on Thr-2037 by CDK1 results in its localization at spindle poles in metaphase, but not at the cell cortex (By similarity). In anaphase, recruited and anchored at the cell membrane of the polar cortical region in a EPB41-, EPB41L2-, phosphatidylinositol-dependent and GPSM2- and G(i) alpha proteins-independent manner (PubMed:24109598). Excluded from the anaphase equatorial region of the cell cortex in a RACGAP1- and KIF23-dependent and RanGTP-independent manner. Associated with astral MTs emanating from the spindle poles during anaphase. Nonphosphorylated Thr-2037 localizes at the cell cortex, weakly during metaphase and more prominently during anaphase in a phosphatase PPP2CA-dependent manner. As mitosis progresses it reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. Localizes to the tips of cortical MTs in prometaphase (By similarity). Localizes along MTs and specifically to both MT plus and minus ends (PubMed:26765568). Accumulates also at MT tips near the cell periphery. Colocalizes with GPSM2 at mitotic spindle poles during mitosis. Colocalizes with SPAG5 at mitotic spindle at prometaphase and at mitotic spindle poles at metaphase and anaphase. Colocalizes with ABRO1 at mitotic spindle poles. Colocalized with TNKS from prophase through to anaphase in mitosis. Colocalizes with tubulin alpha. CCSAP is essential for its centrosomal localization (By similarity). In horizontally retinal progenitor dividing cells, localized to the lateral cortical region (PubMed:26766442). {ECO:0000250|UniProtKB:Q14980, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568, ECO:0000269|PubMed:26766442}. | null | null | null | null | null | FUNCTION: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:19255246, PubMed:24109598, PubMed:26765568). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:26765568). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:24109598, PubMed:26765568). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation. Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (By similarity). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:26765568). Plays a role in mitotic MT aster assembly. Involved in anastral spindle assembly. Positively regulates TNKS protein localization to spindle poles in mitosis. Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (By similarity). Required for epidermal differentiation and hair follicle morphogenesis (PubMed:26765568). {ECO:0000250|UniProtKB:Q14980, ECO:0000269|PubMed:19255246, ECO:0000269|PubMed:24109598, ECO:0000269|PubMed:26765568}. | Mus musculus (Mouse) |
E9Q7R9 | CFA43_MOUSE | MSQDPERDDVTASATASASASAPASASAHYSGSSLSVRWVQGFPSQNVHFVNDQTICYPSGNFVIFINLETKKKTVLQCINGIVGVMATNVPSEVVAFSDRRFKPVIYIYSFPSLTRKNKLKGDILLDYTLLCFSYCGTYLASYSSLPEFELALWNWEASAILCKKSNPGMDVSQMSFNPMNWHQMCLSSSSAMSVWTIERSNQEHHFRIRSVKLPLEDATFLNEPDMLFPTTLPKDLIYGPVLPLSAIAGLVGEEAETFRPKDDIYPLLHPTMHCWTPSSDLYVGCEEGHLLMINTETLKVTVLQKAEEFPLPDGAPLINPLTLVYQKDGILASGIDGVIYSFIIKDSKYQVKTFLEFDGPVTHLVFSPSYKMLLIQTDKGSVYIYTFGAEMPLDKLLDACDGKVQAVSFITPGTKYFLTLTSSGEVSTVSLEDCNCTSRIFLKTQATALACSPSSPTAAVGTVDGYVYFLNILDVESPQMIHQAFLSQSPVKIVTYDQRGIFLLVGTEEGNIFVIDARPSKSFQIFGFTETGKDILQISTVSVMESDVVEVLVLYPLPDMGRSRLEYFTLPVMLPEVVPENFSDERGRLKDDLTHKYLYEVEHTLSSAVLGFTGSKIFGFCSQVPYICSYVMPVKEHTGVLVLKPHQKVQSKQYGSGTIYLSSHGLWLMTIAKCGILCIRDMFSMETFVRCRSHSHQGRGIQNMKMSLDGQHILVNGKDDNTLVCLKWKRLGANIASEIFEHSRPLVLHLSQTVESESVYLALSRESTNEQQEETTESQKHLNSDSSEEEAVIDHKMIPWIQQKMEEAIKKEVRIFSPRRKEIKRGIKELAQVIAMMMEENEKVDIIAKLDEQEFCLDADELERLHDECEEEVAKIRKDVEMHNLAQSYLTELIKEECWNSMAVKGRALKCFHIPYVVDNFPMKERTEEELQELSKVMQQKKTEIECLKLRKEIVEVQATTTIAKKHHEEEEEEEEDEERTIKTTSLPNYLLGSLSTDFGADTSLLTSQLDLHSREEKINQIILLKDIIYNIKRNFNSEFDAAYKQKEIEIARVKEKNVRIAEIISDLELEETVWQPVFEDSEKPERALVVEDDEISFKKYIAPWQRAKIKEVVSTYEMERLQQARISDERQRGLMDMMGGVLEVKKEDILRMVIPQPPFMAKADALWSEDERKQFKEYEKKVKELNEERDKYRKSLEAELKKLQNSIQESTQNFDDHLKRLFERRVKAEMVINQEELKINNIIFSLLLDEELSSREQFLNNYLLKKQEEKTKTAEAIQKAREDLDVFKEHHDMLVAEDKILDRSFKKEFSDILGHQVDVLYKLFKRRPRVHKQKTQADVTSLVPYGERPGSAKLNKENLAQLMKSMDELDNINNMPEGLDPSVWEHFCSTRRAKVENEYKVKQKAACLLEMTTFLRKRMEEDDVVHHEIEKVFHELIRLQDEKVRFQVNLTVQILLKQGQVELENFQLMLEYSDAILINKNIIEDLNSVIRTQGQKKVASMMESKEVHKGIYQIEWEHKKMEMEMEDLNQRAWDIEMLFFSRDRQKYLNEPNYENVIAIQIGIMEQTISVIDKTHKKNVENCKKLLKKLGKYSNQKDVANYTLSCNLREELVAVSERQDICNEIGSKLTCEKIARERYDNQLKQQKLLNISKQQAEQISILQAEVERLRMKTFPALIPM | null | null | brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium assembly [GO:0060271]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; motile cilium assembly [GO:0044458]; mucociliary clearance [GO:0120197]; regulation of cilium beat frequency [GO:0003356]; sperm axoneme assembly [GO:0007288] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; extracellular region [GO:0005576] | null | null | 2.130.10.10; | CFAP43 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:31884020}. | null | null | null | null | null | FUNCTION: Flagellar protein involved in sperm flagellum axoneme organization and function (PubMed:28552195, PubMed:29449551, PubMed:31884020). Involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract (PubMed:31884020). {ECO:0000269|PubMed:28552195, ECO:0000269|PubMed:29449551}. | Mus musculus (Mouse) |
E9Q7X6 | HEG1_MOUSE | MATPRAPRWPPPSLLLLLLLPLLLLPPAAPGARGSLPSPAHRTLLPVAGPLSPPGAGHTAPGPGVATRRGRSGRVPRGVSAAAARNRWLESNNPEPHIGCSPSYQSQEDHSGSRKGVTAQNARMSHSSSEGPENPPLLPETSAEWSNMASSHRADIAGLRRGPSPEITTAPTAHSSLLSLESLPESPSSSRSQRRITPSQTESGTSLGFLERTRELPEEGTVHTQVAGTWVSRQASHPALEPGEPTVLSQKRNSSGQEHSGPPFSWSQSHPPPSDHPSSSGSIKNGNNFTALQNPSVTQTKSMLITDTYTNGVPRTLRSLPVGVDPADETEGFPEHSRLGITSMSVRSSPSVKDSRTNSGLTEHLGDGEGTELSTENGYGLPSIHWQSDAPSFGGRQLASSSEAGDGRAMPLTEAVFRSDPSIGGGESTGRWILTKKKTSTDAAESSALHPEAGGAGGLTQSSHAAQQPRGGGEDSGMGGRSYAESSSSSSSTSSSESLDSSAPLREHSLTGLSYTREHGSDAGQRTSSDHTDHGYVPSTFTKGERTLLSITDNTSYSEASESSTSSVKISDSPSQAQPKQSSMSSDDDEPAQSSTESPVLHTSNLPTYTSTVNMPNTLVLDTGTKPVEDPSDSRVPSTQPSPSQPQPFSSALPSTRSPGSTSETTTSSPSPSPISLLVSTLAPYSVSQTTFPHPSSTLVPHRPREPRVTSVQMSTAISAIALIPSNQTANPKNQSTPQQEKPITEAKSPSLVSPPTDSTKAVTVSLPPGAPWSPALTGFSTGPALPATSTSLAQMSPALTSAMPQTTHSPVTSPSTLSHVEALTSGAVVVHTTPKKPHLPTNPEILVPHISTEGAITTEGNREHTDPTTQPIPLTTSTTSAGERTTELGRAEESSPSHFLTPSSPQTTDVSTAEMLTSRYITFAAQSTSQSPTALPPLTPVNSCTVNPCLHDGKCIVDLTGRGYRCVCPPAWQGENCSVDVNECLSSPCPPLATCNNTQGSFTCRCPVGYQLEKGICNLVRTFVTEFKLKKTFLNTTAENHSNTQELENEIAQTLNVCFSTLPGYIRTTAHVSREPSTVFISLKTTFALASNVTLFDLADRIQKYVNSCRSSAEVCQLLGSQRRVFRAGSLCKRKSPECDKETSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGVALIVTCCRKSKNDISKLIFKSGDFQMSPYTDVPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTNVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF | null | null | cardiac atrium morphogenesis [GO:0003209]; cardiac muscle tissue growth [GO:0055017]; cell-cell junction organization [GO:0045216]; endothelial cell development [GO:0001885]; endothelial cell morphogenesis [GO:0001886]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; lung development [GO:0030324]; lymph circulation [GO:0003017]; lymph vessel development [GO:0001945]; multicellular organism growth [GO:0035264]; negative regulation of membrane permeability [GO:1905709]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of Rho-dependent protein serine/threonine kinase activity [GO:2000299]; pericardium development [GO:0060039]; positive regulation of fibroblast growth factor production [GO:0090271]; post-embryonic development [GO:0009791]; protein localization to cell junction [GO:1902414]; regulation of body fluid levels [GO:0050878]; vasculature development [GO:0001944]; vasculogenesis [GO:0001570]; venous blood vessel morphogenesis [GO:0048845]; ventricular septum development [GO:0003281]; ventricular trabecula myocardium morphogenesis [GO:0003222] | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897] | calcium ion binding [GO:0005509] | PF00008;PF07645; | 2.10.25.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:19151727}. | null | null | null | null | null | FUNCTION: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May be acting by stabilizing endothelial cell junctions. {ECO:0000269|PubMed:19151727}. | Mus musculus (Mouse) |
E9Q7X7 | NRX2A_MOUSE | MALGSRWQPPPQLPPLLLLLALAAGVRGLEFGGGPGQWARYARWAGAASTGELSFSLRTNATRALLLYLDDGGDCDFLELLLVDGRLRLRFTLSCAEPATLQLDTPVADDRWHMVLLTRDARRTALAVDGEARAAEVRSKRREMQVASDLFVGGIPPDVRLSALTLSTVKYEPPFRGLLANLKLGERPPALLGSQGLRGAAADPLCAPARNPCANGGLCTVLAPGEVGCDCSHTGFGGKFCSEEEHPMEGPAHLTLNSEVGSLLFSEGGAGRGGAGDVHQPTKGKEEFVATFKGNEFFCYDLSHNPIQSSTDEITLAFRTLQRNGLMLHTGKSADYVNLSLKSGAVWLVINLGSGAFEALVEPVNGKFNDNAWHDVRVTRNLRQHAGIGHAMVNKLHYLVTISVDGILTTTGYTQEDYTMLGSDDFFYIGGSPNTADLPGSPVSNNFMGCLKDVVYKNNDFKLELSRLAKEGDPKMKLQGDLSFRCEDVAALDPVTFESPEAFVALPRWSAKRTGSISLDFRTTEPNGLLLFSQGRRAGAGVGSHSSTQRADYFAMELLDGYLYLLLDMGSGGIKLRASSRKVNDGEWCHVDFQRDGRKGSISVNSRSTPFLATGESEVLDLESELYLGGLPEGGRVDLPLPPEVWTAALRAGYVGCVRDLFIDGRSRDLRGLAEAQGAVGVAPFCSRETLKQCASAPCRNGGICREGWNRFVCDCIGTGFLGRVCEREATVLSYDGSMYMKIMLPTAMHTEAEDVSLRFMSQRAYGLMMATTSRESADTLRLELDGGQMRLTVNLDCLRVGCAPSKGPETLFAGHKLNDNEWHTVRVVRRGKSLQLSVDNVTVEGQMAGAHTRLEFHNIETGIMTERRFISVVPSNFIGHLSGLVFNGQPYMDQCKDGDITYCELNARFGLRAIVADPVTFKSRSSYLALATLQAYASMHLFFQFKTTAPDGLLLFNSGNGNDFIVIELVKGYIHYVFDLGNGPSLMKGNSDKPVNDNQWHNVVVSRDPGNVHTLKIDSRTVTQHSNGARNLDLKGELYIGGLSKNMFSNLPKLVASRDGFQGCLASVDLNGRLPDLIADALHRIGQVERGCDGPSTTCTEESCANQGVCLQQWDGFTCDCTMTSYGGPVCNDPGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTMRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPSSGGPCQAERDDSDCEEPVEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPRPNLRTDGATGAPGVLFAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGVPTAFEPRRPPPLRPGVTSAPGFPRLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV | null | null | adult behavior [GO:0030534]; cell adhesion [GO:0007155]; chemical synaptic transmission [GO:0007268]; gephyrin clustering involved in postsynaptic density assembly [GO:0097116]; neuroligin clustering involved in postsynaptic membrane assembly [GO:0097118]; neurotransmitter secretion [GO:0007269]; postsynaptic density protein 95 clustering [GO:0097119]; postsynaptic membrane assembly [GO:0097104]; signal transduction [GO:0007165]; social behavior [GO:0035176]; synapse assembly [GO:0007416]; vocal learning [GO:0042297]; vocalization behavior [GO:0071625] | cell projection [GO:0042995]; glutamatergic synapse [GO:0098978]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991] | calcium channel regulator activity [GO:0005246]; cell adhesion molecule binding [GO:0050839]; metal ion binding [GO:0046872]; neuroligin family protein binding [GO:0097109]; transmembrane signaling receptor activity [GO:0004888] | PF02210; | 2.60.120.200;2.10.25.10; | null | PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins. {ECO:0000269|PubMed:30100184}. | SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9CS84}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling. {ECO:0000250|UniProtKB:Q63374}. | Mus musculus (Mouse) |
E9Q816 | CP2W1_MOUSE | MALLLLGVWGILLLLGLWGLLQGCTRSPSLAPRWPPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRPPAQTLCVVPRS | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q6VVX0}; | aflatoxin metabolic process [GO:0046222]; organic acid metabolic process [GO:0006082]; phospholipid metabolic process [GO:0006644]; retinoic acid catabolic process [GO:0034653]; xenobiotic metabolic process [GO:0006805] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | all-trans retinal binding [GO:0005503]; all-trans-retinol binding [GO:1904768]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; retinoic acid 4-hydroxylase activity [GO:0008401]; retinoic acid binding [GO:0001972] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8TAV3}. Cell membrane {ECO:0000250|UniProtKB:Q8TAV3}. Microsome membrane {ECO:0000250|UniProtKB:Q8TAV3}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced [NADPH--hemoprotein reductase] = 1-[8-hydroxy-(9Z)-octadecenoyl]-sn-glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50328, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132285; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50329; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced [NADPH--hemoprotein reductase] = 1-[11-hydroxy-(9Z)-octadecenoyl]-sn-glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50332, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132286; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50333; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced [NADPH--hemoprotein reductase] = 1-[(9S,10R)-epoxy-octadecanoyl]-sn-glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50324, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132278; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50325; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced [NADPH--hemoprotein reductase] = 1-[(9R,10S)-epoxy-octadecanoyl]-sn-glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50320, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132280; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50321; Evidence={ECO:0000250|UniProtKB:Q8TAV3}; | null | null | null | null | FUNCTION: A cytochrome P450 monooxygenase that may play a role in retinoid and phospholipid metabolism. Catalyzes the hydroxylation of saturated carbon hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may regulate atRA clearance. Other retinoids such as all-trans retinol and all-trans retinal are potential endogenous substrates. Catalyzes both epoxidation of double bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl chain of 1-acylphospholipids/2-lysophospholipids. Can metabolize various lysophospholipids classes including lysophosphatidylcholines (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines (LPEs) and lysophosphatidic acids (LPAs). Has low or no activity toward 2-acylphospholipids/1-lysophospholipids, diacylphospholipids and free fatty acids. May play a role in tumorigenesis by activating procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines. 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). {ECO:0000250|UniProtKB:Q8TAV3}. | Mus musculus (Mouse) |
E9Q876 | ABCAC_MOUSE | MASQFHQLRILVWKNWLGVKRQPLWTLVLILWPVIIFIILAITRTKFPPTAKPTCYLAPRNLPSAGFFPFLQTLLCDTDSKCKDTPYGPRDLLRRKGIDGPLFKESEILKKPSNPKRDSNLSLRSTQVPERSHTSLATVPPRPSYDLEGTGTENFNGSQLLTRILGLEKLLKQNSTPEDIRRELCESYPGYTADYAFSWVTLGKNVFNKFCLSNMTLLESSLQELKYQVSQMSSDPDNQKRVFRGLVQVLSFFSQVQQQREVWQLLSSLPDVFQNGTSLSSLFGVLQKANRVLLVVQKVYPRVQTDEGFSTLQKSVKHLLNTLDSPMQGDNSTHAWSDDDEQTLSPSSLAAQLLILENFEDAILNISSNSPYSPYLACVRNMTDNLAKGSPDNLKLLQSTIHFRKSFLQNGSSEDSFPPFLEILKSKLSQLRNLTELLCESETFSSIKKSCQFSNMSFERLCEDHAFHVQLIEAAELGTDLTTGLLYHDNIISAKLRGLLTGDPSKINLNVDWLLEQALQMNYLENITRLIPTVEAMLHVNTSADASEKPGQLREMFKNIDLLKEDLRAIGMSNTSIDKLLAIPIPDNRAEIISRVFWLHSCDTNVTNPKLEDAMKEFCKLPLPERSHQSYLIGLTLLHYLDIYNFTYKVFFPRKDQKPMERMMELFIKLREILNQLASGTHPLLDKMRSLRQMHLPRSVPLTQAMYRNTRMNSPAGSFSTISQALCSQGITTEYLTAMLPSSQKPKGNHTKDFLTYKLTKEEIASKYGIPLNATPFCFSLYKDIINMPAGPVIWAFLKPMLLGKILYSPYNPTTKAIMEKSNVTLRQLAELREKSQEWMDKSPIFMNSFHLLNQTIPMLQNTLRNPFVQVFVKFSVGLDAVELLKQIDDLDVLRLKLVNNIDIIDQLNTLSSLTVNISSCVLYDRIQASDTVEEMETVAEQLYKSNELFGSVIFKLPSNGSLHRGFDPEKVSLPPIVRYTIRMSLKTAQTTRSIRTKIWAPGPHNSPSHNQIYGRAFIYLQDSIERAIIELQTGRNSQEVAVQVQAVPYPCFMKDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESIGFLLVTIAILIVILKFGNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLSPTAFSYASQYIARYEEQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAWYVRNVFPGTYGMAAPWYFPILPSYWKERFGCAEVKHEKSNGLMFTNIMMQNTNPSASKTSPDCAFPSNIEPEPKDLQVGVALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKSPNLDTNAICDTVAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKVSGAYLSLLRALDKGMGKLNIGCYGISDTTVEEVFLNLTKDSQKSSNMSLEHLTQRKVGNPSANGTSTPDDLSVSSSNFTDRDDKVLTRSEKLEGFGLLLKKIMAILIKRFHHTRRNWKGLIAQVILPIVFVATAMGLGTLRDSSNSYPEIMISPSIYGTSEQTAFYANFDPSTSGLVSALWNFPGIDNVCLNTSDLQCLKKDDLGKWNTSGEAIDNFGVCSCSDNVQECPKFNYHPPHRRTYSSQVIYNLTGKHMENYLITTANHFVQKRYGGWSFGMKLTNDLRFDVTAVPDNRTLAKVWYDPEGYHSLPAYLNSLNNFLLRVNMSEYDAARHGIIMYSHPYPGVQDQEQATISSLIDILVALSILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGVIAIFKLPAFYSGNNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSIVSLSVVYFLSKEKPNDPTLELISETLKRIFLIFPQFCFGYGLIELSQQQAVLDFLKAYGVEYPSETFEMDKLGAMFVALVSQGTMFFLLRLLINEWLIKKLRLFFRKFTSSPIMETVDEDEDVRAERFRVESGAAEFDLVQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIKSRFGRGFTVKVHLKNNKVSMETLTKFMQLHFPKTYLKDQHLSMLEYHVPVTAGGVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQKSYENVDTSSQGSTISVDSQEDQLDS | 7.6.2.1 | null | ceramide metabolic process [GO:0006672]; ceramide transport [GO:0035627]; cholesterol efflux [GO:0033344]; corneocyte desquamation [GO:0003336]; establishment of localization in cell [GO:0051649]; establishment of skin barrier [GO:0061436]; intracellular protein transport [GO:0006886]; keratinization [GO:0031424]; keratinocyte differentiation [GO:0030216]; lipid homeostasis [GO:0055088]; lipid transport [GO:0006869]; lung alveolus development [GO:0048286]; phospholipid efflux [GO:0033700]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of intracellular lipid transport [GO:0032379]; positive regulation of protein localization to cell surface [GO:2000010]; protein localization to plasma membrane [GO:0072659]; regulated exocytosis [GO:0045055]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of keratinocyte differentiation [GO:0045616]; surfactant homeostasis [GO:0043129] | cytosol [GO:0005829]; epidermal lamellar body membrane [GO:0097234]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658] | ABC-type transporter activity [GO:0140359]; apolipoprotein A-I receptor binding [GO:0034191]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319] | PF12698;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCA family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q86UK0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86UK0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86UK0}. Note=Localizes in the limiting membrane of the lamellar granules (LGs). Trafficks from the Golgi apparatus to the lamellar granules (LGs) at the cell periphery in the uppermost granular layer keratinocytes where ABCA12-positive LGs fuse with the keratinocyte-cell membrane to secrete their lipid content to the extracellular space of the stratum corneum. Co-localizes through the Golgi apparatus to the cell periphery with glucosylceramide. {ECO:0000250|UniProtKB:Q86UK0}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:Q86UK0}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-glucosylceramide(in) + H2O = ADP + beta-D-glucosylceramide(out) + H(+) + phosphate; Xref=Rhea:RHEA:66660, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83264, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q86UK0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66661; Evidence={ECO:0000250|UniProtKB:Q86UK0}; | null | null | null | null | FUNCTION: Transports lipids such as glucosylceramides from the outer to the inner leaflet of lamellar granules (LGs) membrane, whereby the lipids are finally transported to the keratinocyte periphery via the trans-Golgi network and LGs and released to the apical surface of the granular keratinocytes to form lipid lamellae in the stratum corneum of the epidermis, which is essential for skin barrier function (PubMed:18802465, PubMed:18957418, PubMed:20489143, PubMed:24293640, PubMed:27551807). In the meantime, participates in the transport of the lamellar granules-associated proteolytic enzymes, in turn regulates desquamation and keratinocyte differentiation (PubMed:20489143, PubMed:27551807). Furthermore, is essential for the regulation of cellular cholesterol homeostasis by regulating ABCA1-dependent cholesterol efflux from macrophages through interaction with NR1H2 and ABCA1 (PubMed:18802465, PubMed:23931754). Plays pleiotropic roles in regulating glucose stimulated insulin secretion from beta cells, regulating the morphology and fusion of insulin granules, lipid raft abundance and the actin cytoskeleton (PubMed:32072744). Also involved in lung surfactant biogenesis (PubMed:18632686). {ECO:0000269|PubMed:18632686, ECO:0000269|PubMed:18802465, ECO:0000269|PubMed:18957418, ECO:0000269|PubMed:20489143, ECO:0000269|PubMed:23931754, ECO:0000269|PubMed:24293640, ECO:0000269|PubMed:27551807, ECO:0000269|PubMed:32072744}. | Mus musculus (Mouse) |
E9Q8I9 | FRY_MOUSE | MASQQDSGFFEISIKYLLKSWSNASPVGNGYIKPPVPPASGTHREKGPPAMLPINVDPDSKPGEYVLKSLFVNFTTQAERKIRIIMAEPLEKPLTKSLQRGEDPQFDQVISSMSSLSEYCLPSILRTLFDWYKRQNGIEDESHEYRPRTSNKSKSDEQQRDYLMERRDLAIDFIFSLVLIEVLKQIPLHPVIDSLIHDIINLAFKHFKYKEGYLGPNTGNMHIVADLYAEVIGVLAQAKFPAVKKKFMAELKELRHKEQSPYVVQSIISLIMGMKFFRIKMYPVEDFEASLQFMQECAHYFLEVKDKDIKHALAGLFVEILVPVAAAVKNEVNVPCLRNFVESLYDTTLELSSRKKHSLALYPLVTCLLCVSQKQLFLNRWHVFLNNCLSNLKNKDPKMARVALESLYRLLWVYMIRIKCESNTATQSRLITITTTLFPKGSRGVVPRDMPLNIFVKIIQFIAQERLDFAMKEIIFDFLCVGKPAKAFSLNPERMNIGLRAFLVIADSLQQKDGEPPMPVTGAVLPSGNTLRVKKTYLSKTLTEEEAKMIGMSLYYSQVRKAVGNILRHLDKEVGRCMMLTNVQMLNKEPEDMITGERKPKIDLFRTCVAAIPRLLPDGMSKLELIDLLARLSIHMDDELRHIAQNSLQGLLVDFSDWREDVLFGFTNFLLREVNDMHHTLLDSSLKLLLQLLTQWKLVIQTQGRAYEQANKIRNSELIPNGSSHRMQSERGPHCSVLHAVEGFALVLLCSFQVATRKLSVLILKEIRALFLALGQPEDDDRPMIDVMDQLSSSILESFIHVAVSDSATLPPTHNVDLQWLVEWNAVLVNSHYDVKSPSHVWIFAQSVKDPWVLCLFSFLRQENLPKHCPTALSYAWPYAFTRLQSVMPLVDPNSPVNAKKTSTASSGDNYVTLWRNYLILCFGVAKPSIMSPGHLRASTPEIMATTPDGTVSYDNKAIGTPSVGVLLKQLVPLMRLESIEITESLVLGFGRTNSLVFRELVEELHPLMKEALERRPENKKRRERRDLLRLQLLRIFELLADAGVISDSTNGALERDTLALGALFLEYVDLTRMLLEAENDKEVEILKDIRAHFSAMVANLIQCVPVHHRRFLFPQQSLRHHLFILFSQWAGPFSIMFTPLDRYSDRNHQITRYQYCALKAMSAVLCCGPVFDNVGLSPDGYLYKWLDNILACQDLRVHQLGCEVVMLLLELNPDQINLFNWAIDRCYTGSYQLASGCFKAIATVCGNRNYPFDIVTLLNLVLFKASDTNREIYEVSMQLMQILEAKLFVHSKKVAEQRPGSILYGTHGPLPPLYSVSLALLSCELARMYPELTLPLFSEVSQRFPTTHPNGRQIMLTYLLPWLHNIELVDSRLLLPGSSPSSPEDEVKDREGEVTASHGLKGNGWGSPEATSLVLNNLMYMTAKYGDEVPGAEMENAWNALANNEKWSNNLRVTLQFLISLCGVSSDTILLPYIKKVATYLCRNNTIQTMEELLFELQQTEPVNPIVQHCDNPPFYRFTASSKASAAASGTTSSSNTVVAGQDSFPDPEESKILKESDDRFSNVIRAHTRLESRYSNSSGGSYDEDKNDPISPYTGWLLSITEAKQPQPLPMPCSGGCWAPLVDYLPETITPRGPLHRCNIAVIFMTEMVVDHSVREDWALHLPLLLHAVFLGLDHYRPEVFEHSKKLLLHLLIALSCNSNFHAIASVLLQTREMGEAKTLTMQPAYQPEYLYTGGFDFLREDQSSPVPDSGLNSSSTSSSISLGGSSGNLPQMTQEVEDVEAATETDEKASKLIEFLTTRAFGPLWCHEDITPKNQNSKSAEQLSNFLRHVVSVFKDSRSGFHLEQHLSEVALQTALASSSRHYAGRSFQIFRALKQPLSAHALSDLLSRLVEVIGEHGDEIQGYVMEALLTLEAAVDNLSDCLKNSDLFTVLSRSSSPDLSSSSKLTASRKSTGQLNVNPGTPGSGGGGGGSGNTTTAERSRHQRSFSVPKKFGVVDRSSDPPRSATLDRIQACTQQGLSSKTRSNSSLKESLTDPSHVSHPTNLLATIFWVTVALMESDFEFEYLMALRLLNRLLAHMPLEKAENREKLEKLQAQLKWADFPGLQQLLLKGFTSLTTTDLTLQLFSLLTSVSKVPMVDSSQAIGFPLNVLCLLPQLIQHFENPNQFCKDIAERIAQVCLEEKNPKLSNLAHVMTLYKTHSYTRDCATWVNVVCRYLHEAYADITLNMVTYLAELLEKGLPSMQQPLLQVIYSLLSYMDLSVVPVKQFNMEVLKTIEKYVQSIHWREALNILKLVVSRSASLVLPSYQHSDLSKIELHRVWTSASKELPGKTLDFHFDISETPIIGRRYDELQNSSGRDGKPRAMAVTRSASSTSSGSNSNVLVPVSWKRPQYSQKRTKEKLVHVLSLCGQEVGLSKNPSVIFSSCGDLDLPEHQTSLVSSEDGPREQENMDDTNSEQQFRVFRDFDFLDVELEDGEGESMDNFNWGVRRRSLDSLDKCDMQILEERQLSRSTPSLNKMSHEDSDESSEEDLTASQILEHSDLIMNLSPSEEANPMELLTSACDSAPADPHSFNTRMANFEASLPDINNLQISEGSKAEAVPEEEDTTVHEDDLSSSINELPAAFECSDSFSLDMTEAEEKGNRGLDQYTLASFGEGDRGVSPPPSPFFSAILAAFQPAACDDAEEAWRSHINQLMCDSDGSCAVYTFHVFSSLFKNIQKRFCFLTCDAASYLGDNLRGIGSKFVSSSQMLTSCSECPTLFVDAETLLSCGLLDKLKFSVLELQEYLDTYNNRKEATLSWLANCKATFAGGSRDGVITCQPGDSEEKQLELCQRLYKLHFQLLLLYQSYCKLIGQVHEVSSVPELLNMSRELSDLKRNLKEATAAIATDPLYIEGAWSEPTFTSTEAAIQSMLECLKNNELGKALRQIKECRSLWPNDIFGSSSDDEVQTLLNIYFRHQTLGQTGTYALVGSNHSLTEICTKLMELNMEIRDMIRRAQNYRVLTAFLPDSSVSGTSL | null | null | cell morphogenesis [GO:0000902]; negative regulation of tubulin deacetylation [GO:1904428]; neuron projection development [GO:0031175] | cell cortex [GO:0005938]; centrosome [GO:0005813]; site of polarized growth [GO:0030427]; spindle pole [GO:0000922] | enzyme inhibitor activity [GO:0004857] | PF19421;PF14225;PF14228;PF14222; | null | Furry protein family | PTM: Phosphorylated by AURKA, CDK1 and PLK1. {ECO:0000269|PubMed:22753416}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Distributed diffusely throughout the cytoplasm in interphase. Localizes to the separating centrosomes in prophase, to the spindle poles and spindle microtubules in prometaphase to metaphase, to spindle microtubules in anaphase and to the distal sections of the midbody in cytokinesis. Colocalizes with PLK1 to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269|PubMed:22753416}. | Mus musculus (Mouse) |
E9Q8Q6 | CC141_MOUSE | MSCKESPHVGASTTTVSSVAVHAGDSKIVIAVVKCGKWVRLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLREADRTAEANKAQSQVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEAFLQNPHEFESTEALQSLLLLHDRHAKELLERSLDLLNKSQQLTDFIEKFKCEGSTMNSELIQGAQSSCLKIDSLLELLQDRRRQLDKYLQQQRQELSQVLQLCLWDQQENQVSSWFQKAIRDLQEQSLGASLSDNRELICKHEDLIVKAKEWDSAVEKLKSQALGILLSKDLAGKEHLQLSNQKLNRLQEEFGRLMVERKAWLSMANDFFTSANKSFDVLGKVEAYLKLLKSEGLSLPVLAAKHEELHREIKDSTATALQKGRTLISQVDSCRSRVTGIHEMMGYIQNRVDCLTEQCTAHEEFARKRQQLATSVDDYLRKVEMSIQEIRPILATTLDVASSPSESEKILNKYLELDIQVKETAHALEAAAKIMTEKNELELNEVALLPLKVKWLEEELSTLGRSISCRSRILQTYVAFRKSSEEAEEQLQSLKEFYLTEIPWKDEDDAVVKCQSNSAERKWQLFLKKSFLTQDLSLEFLNLINMAKENEILNVKNEMHIMENIMEKQTNGREELSHLRVAWYLKAIEGKPAREQWEMFKEKLTKTTHSVKLLHEVLMPVSALDLGGSLQSTSDLRRRWIAMKPQLQQLHEDVQQITKEWEVLSSQGAPLKEKAEQLKDLVHLHRRQRERIQEYEEILYKTVQFHQVKEELVHLIKPRELELLAQPMELASSEEVQMQLGRSQERRAHVDHLHQLALTLGVDIISSVQQPNCSNISAKNLQQQLEALELESRSWSAQAKEHERVLSCSLEYCTARDEISELKESFKDIKKKFNNLKFNYSKKNEKSRNLKTLQYQIQQVDTYAEKIQALRKKMEKVNNKTSDSFLSYPSNKANMLSEAMEDLKKNVDDFDKVVTDYKMNLDLTEHLQEVIEECNFWYEDASATVVRVGKYSMECQTREAVDILHRQFNKFITPSVPQQEERIQEVIDLAQRLYGLEEGQKYAEKIVTRHKEILESITELCGSLVELKEKLMQGEVPKMNSDLEDFHDNCIDLLKGPGKDDQKTFSEERNEGQVQGADVLAVNGTREDGLPMDLRRTSSDKEDSAQGLILPEDTLSGEESECISSDDISLPPLPVSPESPLAPSDMEVEELTSSSALALHISGYRMHPGTGGLGKAQESALPSPIAFADGGHSKKDTFTSHFERPYPQLKAESSLASRGSAEMSTKLHINVKCPASMPHEVHDKALQQCSQARESTLEMQEKVHADSNVTKTQDRLHAALDVSPGLGSQPDTSESHQRRVGPQGNKKNSSAENSVVSLAGQAPHFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTWFKKGQKLCADGHLQVLHKDTKHSVFIPKVCEADAGLYVAQAQNSSGTLSSKAILHVTGNHGPPITRLNWIMLCIIYVSVSVIYWLLTR | null | null | brain development [GO:0007420]; centrosome localization [GO:0051642]; cerebral cortex radially oriented cell migration [GO:0021799] | centrosome [GO:0005813]; cytoplasm [GO:0005737] | null | PF07679; | 1.20.58.60;2.60.40.10; | null | PTM: Ubiquitinated and degradated by the CDC20-APC/C pathway. During brain development, CDC20-APC/C complex degrades CCDC141 after centrosome translocation into the dilated area. CCDC141 is restabilized in the dilation until the centrosome enters the dilation, at which point it is once again immediately destabilized by CDC20-APC/C complex. The oscillatory regulation of CCDC141 protein is needed for proper cortical migration. {ECO:0000269|PubMed:34298015}.; PTM: Phosphorylation at Thr-91 by PLK1 affects CCDC141 degradation. {ECO:0000269|PubMed:34298015}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20956536}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:34298015}. Note=Co-localized with DISC1 at/around the centrosome. Localizes to the centrosome, at least in part, in a DISC1-dependent manner (PubMed:20956536). Accumulates and oscillates at the dilation in cortical neurons during migration (PubMed:34298015). CAMDI protein level is stabilized at the G1 phase and destabilized at the G2 /M phase (PubMed:34298015). {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:34298015}. | null | null | null | null | null | FUNCTION: Plays a critical role in cortical radial and GnRH neurons migration during brain development (PubMed:20956536, PubMed:27014940). Regulates cortical radial migration by negatively controlling the activity of histone deacetylase 6 (HDAC6) and promotes centrosome maturation (PubMed:27737934). CAMDI is required for dilation formation of cortical neurons during radial migration (PubMed:34298015). Plays a critical role in learning and memory performance through regulation of AMPA-selective glutamate receptors (AMPARs) cell surface expression in competition with KIBRA (PubMed:27014940). {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:27014940, ECO:0000269|PubMed:27737934, ECO:0000269|PubMed:34298015}. | Mus musculus (Mouse) |
E9Q8Q8 | SACA6_MOUSE | MTSQRSLSSPQTRRPSVMGLISLVGSIVLLFLLIFRASTWACLFCFTTYEERLRVCQLFVGREETKINLCRNELEGAFEDLKDMKINYDERSYLHDEFTQMTVSLQEKAARRREPFWLAFKDAAAKLKRTIEHLKKAPACIPPCGLQEVARLFHCSGCFSKLCDLPLDCPVQDMLVNRGDQALFSCIVAFELPESEITYSWKFVGGVRTKDVTYFRDMPGAHGYLARIRPVQPKHGGTFSCVILHDQRPLARLYFYLNVTGPPPPEDTELQVTFREVMNRTPAEPEMIQPWSPSLGELLTNPQALTLGNLFLLAATAALGSASVTLLVWLFFRWYLSGN | null | null | fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342] | acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; membrane [GO:0016020] | null | null | null | SPACA6 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:32393636}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Sperm protein required for fusion of sperm with the egg membrane during fertilization. {ECO:0000269|PubMed:24275887, ECO:0000269|PubMed:32210282, ECO:0000269|PubMed:32393636}. | Mus musculus (Mouse) |
E9Q8T2 | PRD15_MOUSE | MCPPTIWEKGGQVGARWSLRAPEVSAMAEDGSEEIMFIWCEDCSQYHDSECPELGPVVMVKDSFVLSRARSSLPSNLEIRRLDDGAEGVFAVTQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPALEPGHQNLTAYQHGSDVYFTTSKDIPAGTELRVWYAAFYAKKMDKPMLKQACSSVQAAGTPEPSVSVEPERGQWVCKVCSNTFLELQLLNEHLLGHLEQAKSLPAGGQQHEAASEKEPDAPRMEPPTAAESKSIQSVMVTKEPKKKPRRGRKPKASKVEQPLVIIKDKEPSEHVAEIITEIPPDEPVSATPDERIMELVLGKLAAPTNEASSVPKFPHHPSSTIALKRGLVLSSRHGVRRKLVRQLGEHKRIHQCGTCSKVFQNSSNLSRHVRSHGECAHGDKLFKCEECSKLFSRKESLKQHVSYKHSRNEVDGEYRYRCGSCGKTFRMESALEFHNCRTDDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMFYRKDVMLDHQRRHLDGVRRVKREDLEASGESLVRYKKEPSGCPVCGKVFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLRDHIHVHFKDIALMDDHQREEFIGKIGISSEENDDNSDESADSEPHKYSCKRCQLTFGRGKEYLKHIMEVHKEKGHGCSICHRRFALKATYHAHMVIHRENLPDPNVQKYIHPCEICGRIFNSIGNLERHKLIHTGVKSHACEQCGKSFARKDMLKEHMRVHDNIREYLCAECGKGMKTKHALRHHMKLHKGIKEYECKECHRKFAQKVNMLKHYKRHTGIKDFMCELCGKTFSERNTMETHKLIHTVGKQWTCSVCDKKYVTEYMLQKHVQLTHDKVEAQSCQLCGTKVSTRASMSRHMRRKHPEVLAVRIDDLDHLPETTTIDASSIGIVQPALGLEQEELAEGKHGKAAKRSHKRKQKPEEEAGAPVPEDTTFSEYPEKEPEFTGSVGDETNSAVQSIQQVVVTLGDPNVTAPSSSVGLTNITVTPITTAAGTQFTNLQPVAVGHLTNPDRQLQLDNSILTVTFDTVSGSAMLHNRQNDVQIHPQPEATNPQSVAHFINLTTLVNSITPLGNQLSEQHPLTWRAVPQTDVLQPPQAPAAPQQAVQPQVQNEQQQMYSY | 2.1.1.- | null | cell fate commitment [GO:0045165]; methylation [GO:0032259]; negative regulation of MAPK cascade [GO:0043409]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of stem cell division [GO:2000035]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF21549;PF00096;PF13894; | 3.30.160.60;2.170.270.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28740264}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding transcriptional regulator. Plays a role as a molecular node in a transcriptional network regulating embryonic development and cell fate decision. Stimulates the expression of upstream key transcriptional activators and repressors of the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are essential for naive pluripotency and self-renewal maintenance of embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1 transcription activation through recognition and direct binding of a specific DNA sequence in their promoter regions. Also plays a role in induced pluripotent stem cells (iPSCs) reprogramming. Involved in early embryo development. {ECO:0000269|PubMed:28740264}. | Mus musculus (Mouse) |
E9Q8T7 | DYH1_MOUSE | MEECNKEGPSSSSQGPGYCPVKVPESHDLEKILQESNYHPERNPLNPDPKTPPLPLTDLRQPRKSPLTGTDKKYPLMKQRGFYSDILSPGTLDKLGNVCCGPYMSQNLIRQADLDKFTPKVDSFVIPEDFQERVEQQIIGATTRLLTQTDFPLQSYEPKVQVPFQVLPGQCPRKIEIERRKQQYLRLDIEQLLTSEGIDSNKLMPRHPDLQHPQTIEQGRDPLFPIYLPLKVFDNEEFDCRTPTEWLNMGLEPGSQNRKPVPGKALLPTDDDLGHEDPKNQELDYRWCEVGVLDYDEEKKLYLVQKTDKRGLVRDEMGMPILNGGITPAGRPPLLATQYWVPRIQLLFCAEDPRVFTQRVVQANALRKYTEALLMYNLYVDCMPTEGRRVINEQSLSKIKQWALSTPRMRKGQSVLEHLSCLAREVNLDYERSMNKINFDQIVSSNPETFSYVTLPEKEEEKVPNQGLVSVPEYPFREQKEDFTFVSLLTRPEVITALSKVRAECNKVTSMSLFHSSLSKYSRLEEFEQIQSQTFSQVQMFLKDSWISTLKVAMRGSLRDMSKGWYNLYETNWEVYLMSKLRKLMELIKYMLQDTLRFLVQDSLGSFTQFIGDACCSVLECVDDMDWGEDLVNSPYKPRKNPLFIVDLVLDNSGVHYSTPLEHFEMILLNLFDKGILATHAVPQLEKLVMEDIFISGDPLLESVGLHEPLVEELRANITNAMHKAMMPLQAYAKEYRKYLELNNNDISTFLKTYQTQCPSAEEVREVVITHLKEKEILDNSLPSSIIIGPFYINVDNVKQSLSKKRKALATSMLDILAKNLHKEVDSICEEFRSISRKIYEKPNSIEELAELRDWMKGIPEKLVFLEERIVKVMSDYEVMDEFFYNLTTDDFNDKWAANNWPSKILGQIDMVRQQHVEDEEKFRKIQLMDQNNFQEKLEGLQLVVAGFSIHVEIARAHEIANEVRRVKKQLKDCQQLAMLYNNRERIFGLPITNYDKLSRMVKEFQPYLDLWTTASDWLRWSESWMNDPLSAIDAEQLEKNVIESFKTMHKCVKQFKDIPACQEVALDIRTRIEEFKPYIPLIQGLRNPGMRNRHWEVLSNEININVRPKANLTFARCLEMNLQDHIESISKVAEVAGKEYAIEQALDKMEKEWSSILFNVLPYKETDTYILKSPDEASQLLDDHIVMTQSMSFSPYKKPFEQRINSWETKLKLTQEVLEEWLNCQRAWLYLEPIFSSEDITRQLPVESKRYQTMERIWRKIMKNAYENREVINVCSDQRLLDSLRDCNKLLDLVQKGLSEYLETKRTAFPRFYFLSDDELLEILSQTKDPTAVQPHLRKCFENIARLLFQEDLEITHMYSAEGEEVKLSFSIYPSSNVEDWLLEVERSMKASVHDIIEMAIKAYPTMLRTEWVLNWPGQVTIAGCQTYWTMEVAEALEAGNISSKLFPQLSKQLSDLVALVRGKLSRMQRMVLSALIVIEVHAKDVVSKLIDENVVSVHDFEWISQLRYYWTKDDLYIRAVNAEFIYGYEYLGNSGRLVITPLTDRCYLTLTGALHLKFGGAPAGPAGTGKTETTKDLGKALAIQTVVFNCSDQLDFMAMGKFFKGLASAGAWACFDEFNRIDIEVLSVVAQQITTIQKAQQQRVERFMFEGVEIPLVPSCAVFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAMIAEISLYSFGFNEANVLAKKITTTFKLSSEQLSSQDHYDFGMRAVKTVISAAGNLKRENPTMNEELICLRAIRDVNVPKFLQEDLKLFSGIVSDLFPTIKEEETDYGILDQAIRRSCEKNNLKDVEGFLIKCIQLYETTVVRHGLMLVGPTGSGKSNCYRVLAAAMTLLKGKPSISGGVYEAVNYYVLNPKSITMGQLYGEFDLLTHEWTDGIFSSLIRAGAIASDTNKKWYMFDGPVDAVWIENMNTVLDDNKKLCLSSGEIIKLTEAMTMMFEVQDLAVASPATVSRCGMVYLEPSILGLMPFVECWLKRLPAIIKPYEEQFKSLFTKYLENSINFVRNTVKEVIASTNSNLTMSLLKLLDCFFRPFLPREGLKKIPSEKLSHIPELIEPWFIFSLVWSVGATGDHTSRISFSQWLRLKMRLEQVKLGFPEDGLVYDYRLDDAGISSTEDDDEEEDENKQVSWVKWMDYSAPFTMMPDTNYCNIIVPTMDTVQMSYLLGMLLTNHKPVLCIGPTGTGKTLTVSNKLLKYLPLEYISHFLTFSARTSANQTQDLIDSKLDKRRKGVFGPPLGRNFIFFIDDLNMPALETYGAQPPIELLRQWMDHGGWYDRKVIGAFKNLVDINFVCAMGPPGGGRNAITPRLTRHFNYLSFIEMDEVSKKRIFSIILECWMDGLLGEKSYREPVPGAPNIDDLTEPLVDATINVYGIITSQLLPTPAKSHYTFNLRDLSKVFQGMLMAEPSKVEDKVQLLRLWYHENCRVFRDRLVNEEDRSWFDELLEAQMEEFGVAFNKVCPFQPILYGDFMSPGSDVKSYELITSESKMMQVIEEYMEDYNQINTAKLRLVLFVDAMSHICRISRTLRQALGNALLLGVGGSGRSSLTRLASHMAEYECFQIELSKNYGMSEWREDVKKVLLKAGLQNLPITFLFSDTQIKNESFLEDINNVLNSGDIPNIYSADEQDQIINTMRPYIQEQGLQPTKANLMAAYTGRVRSNIHMVLCMSPIGEVFRARLRQFPSLVNCCTIDWFNEWPAEALKSVATTFLSEIPELECSEEVIQGLIQVCVFIHQSVASKCVEYLAELARHNYVTPKSYLELLNIFSILIGQKKMELKTAKNRMKSGLDKLLRTSEDVAKMQEELEIMRPLLEEAAKDTMLTMEQIKVDTAIAEETRKSVQAEEIKANEKANKAQAIADDAQKDLDEALPALDAALASLRNLNKNDVTEVRAMQRPPPGVKLVIEAVCIMKGIKPKKVPGEKPGSKVDDYWEPGKGLLQDPGRFLESLFKFDKDNIGEAVIKAIQPYIDNEEFQPAAIAKVSKACTSICQWVRAMHKYHFVAKAVEPKRQALREAQDDLEVTQRILEEAKHHLHEVEDGIATMQAKYRECVAKKEELEMKCEQCEQRLGRADKLINGLADEKVRWQETVENLENMLDNIFGDVLVAAGFVAYLGPFTGQYRTTLYEYWVNQLTVHHVPHTSKPTLITTLGNPVKIRSWQIAGLPNDTLSVENGVINQFSQRWTHFIDPQGQANKWIKNMERESGLDVFKLSDRDFLRSMENAIRFGKPCLLENVGEELDPALEPVLLKQTYKQQGNIVLKLGDTVIPYHEDFRMYITTKLPNPHYSPEISTKLTLINFTLSPSGLEDQLLGQVVAEERPDLEEAKNQLIVSNAKMRQELKDIEDQILYRLSSSEGNPVDDMELIKVLEASKMKAAEIQAKVRIAEQTEKDIDLTRMEYIPVAVRTQILFFCVSDLANVDPMYQYSLEWFLNIFLSGIANSERADNLKKRIVNINRYLTFSLYSNVCRSLFEKHKLMFAFLLCVRIMMNEGKINQAEWRYLLSGGSIQTMFENPAPQWLSDRAWRDILALSNLPTFATFSNDFVMYLSEFQAIFDSAEPHRELLPGIWNAYLDEFQKLLILRCLRGDKVTNAMQDFVATHLEPRFIEPQTANLSAVFKESNSTTPLIFVLSPGTDPAADLYKFAEEMKFSKKFSAISLGQGQGPRAEAMMRNSIERGKWVFFQNCHLAPSWMPALERLIEHINPDKVHRDFRLWLTSLPSNKFPVSILQNGSKMTIEPPRGVKANLLKSYNSLSDDFLHSCQKVVEFKSLLLSLCLFHGNALERRKFGPLGFNIPYEFTDGDLRICISQLKMFLDEYEDIPYKVLKYTAGEINYGGRVTDDWDRRCVMNILEDFYNPAVLSSEHSYSNSGIYHQIPPTYDLNGYLSYIKSLPLNDMPEIFGLHDNANITFAQNETFALFNAILQLQPKSSSMGGQSREELVEDVAENILLQVPGPIELQEVTKKFPVLYEESMNTVLVQEVIRYNKLLEVITQTLSDMLKAIKGLVVMSLELELMSISLYNNTVPELWKSKAYPSLKPLASWIMDLLLRLDFMHSWINDGIPPVFWISGFFFPQAFLTGTLQNFARKFVISIDTITFDFKVLPEASSEIKERPQTGCYIHGLFLEGARWDSMNFQLAESRPKELYTEMAVIWLLPEANRKVQNQDFYLCPIYKTLTRAGTLSTTGHSTNYVIAVEIPSNQPQRHWIKRGVALICALDY | null | null | cilium movement involved in cell motility [GO:0060294]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; flagellated sperm motility [GO:0030317]; inner dynein arm assembly [GO:0036159]; sperm axoneme assembly [GO:0007288] | extracellular region [GO:0005576]; inner dynein arm [GO:0036156]; microtubule [GO:0005874]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; dynein intermediate chain binding [GO:0045505]; dynein light intermediate chain binding [GO:0051959]; microtubule motor activity [GO:0003777]; minus-end-directed microtubule motor activity [GO:0008569] | PF12774;PF12775;PF12780;PF12781;PF17857;PF18198;PF08393;PF17852;PF18199;PF03028;PF12777; | 1.10.287.2620;1.10.472.130;1.10.8.1220;1.10.8.710;1.20.1270.280;1.20.58.1120;1.20.920.20;1.20.920.30;3.10.490.20;6.10.140.1060;1.20.140.100;3.20.180.20;3.40.50.300;1.10.8.720; | Dynein heavy chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9P2D7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11371505}. | null | null | null | null | null | FUNCTION: Force generating protein of cilia required for sperm flagellum motility (PubMed:11371505). Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (By similarity). {ECO:0000250|UniProtKB:Q9P2D7, ECO:0000269|PubMed:11371505}. | Mus musculus (Mouse) |
E9Q912 | GDS1_MOUSE | MDNLSDTLKKLKITAADRTEGSLEGCLDCLLQALAQNNAETSEKIQGSGILQLFANLLTPQASCTAKVADIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCGRTDPASEKLMTVFCGMLMNYSNENDSLQAQLISMGVIPTLVKLLGIHCHNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSNKEDDVAELKTASDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDGNCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVVNKAKMLSAGVTETVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNAKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGPAEKDLASAQLVQILHRLLADERSAPEIKYNSMVLICALMGSESLYKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVES | null | null | angiotensin-activated signaling pathway involved in heart process [GO:0086098]; CAAX-box protein maturation [GO:0080120]; cardiac muscle hypertrophy [GO:0003300]; myosin filament assembly [GO:0031034]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; protein localization to nucleus [GO:0034504]; regulation of ERK5 cascade [GO:0070376]; regulation of matrix metallopeptidase secretion [GO:1904464]; regulation of mitochondrion organization [GO:0010821]; vascular associated smooth muscle contraction [GO:0014829] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | GTPase regulator activity [GO:0030695]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF00514; | 1.25.10.10; | null | PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52306}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P52306}. Mitochondrion {ECO:0000250|UniProtKB:P52306}. Nucleus {ECO:0000250|UniProtKB:P52306}. Note=Nuclear import is dependent on complexing with a GTPase containing a C-terminal polybasic region. {ECO:0000250|UniProtKB:P52306}. | null | null | null | null | null | FUNCTION: Acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP. Additionally, appears to chaperone the processing and/or trafficking of small GTPases containing a C-terminal polybasic region independently of GEF activity. Targets include RAP1A/RAP1B, RHOA, RHOB, RHOC, RAC1 and KRAS. Regulates mitochondrial dynamics by controlling RHOT function to promote mitochondrial fission during high calcium conditions. Able to promote the Ca(2+) release from the endoplasmic reticulum via both inositol trisphosphate (Ins3P) and ryanodine sensitive receptors leading to a enhanced mitochondrial Ca(2+) uptake. {ECO:0000250|UniProtKB:P52306}.; FUNCTION: [Isoform 1]: Acts as a GEF (guanine nucleotide exchange factor) for unprenylated RHOA. Chaperones the entry and passage of small GTPases through the prenylation pathway. Recognizes the last amino acid in the GTPase C-terminal CAAX motif with a preference for 'Leu' over 'Met', indicating involvement in the geranylgeranylation pathway. May also recognize prenylated GTPases. {ECO:0000250|UniProtKB:P52306}.; FUNCTION: [Isoform 3]: Acts as a GEF (guanine nucleotide exchange factor) for prenylated RHOA. Acts as a GEF for RHOC. Chaperones the downstream trafficking and/or processing of small newly prenylated GTPases. Escorts RAC1 to the nucleus. {ECO:0000250|UniProtKB:P52306}. | Mus musculus (Mouse) |
E9Q956 | MCMD2_MOUSE | METLQMKEAALVYLDRSGGLQKFIDDCKSYNDSKQSYAVYRFSILIDPCDVVELDADLGNHILHHPLKAARVFQSVCFVAVKTLSLIGQLQTETQINIVLKLTHLPALPSYTLDLCEFPLNYASQRFYMMQGIVIAMTTITKYTQGARFLCSDGVCPLSKGFQYVRVHVPGATESATVRNDFLCSLCSSSLQEDRKFRVLGDKQIVEIITTKMFHAFQGDSKNQPFRFQSLGIFLRDELVNKMKIGNEYKIIGIPVCVKTSQTALCVEANNITPHTAKVPLGISDNFRRLLSLTSSSCWKFTAMLANVFASQIVAPGTYNLLKLCLLMSLVQTRDCNREREDCLDILVITSDTLLVDRLLNFSMNLVSRGIRHPVCTEVFPTVSRNKYGTGAVSIQAGSALLAKGGICFIGDLTSHKKDKLEQLQSALESRSVTVFIPGKKFGDDFDQQMTFPIQCSFWSFVDMDSSSRRNVQKTSTLIGQMDCSLIPANLAEAFGLLINCSEASPCHPLLPTVQHTLKKAVEPEGLLYLASKQFTTEDFEKLLAFAKSLNMEFSLEAERMIHGYYLASRRIRTDSIHGSKLSASALKYLVSLSEAHARLSLRTTVLREDALIAALLLEISLTLRYGATPFCVAPNALFPFELYNEEYLEQRDLYLTQCQQQLQQFIATCGPGTTVFSSDE | null | null | double-strand break repair involved in meiotic recombination [GO:1990918]; double-strand break repair via break-induced replication [GO:0000727]; late meiotic recombination nodule assembly [GO:0042140]; meiotic recombination nodule assembly [GO:0007146]; oogenesis [GO:0048477]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; single-stranded DNA helicase activity [GO:0017116] | PF17855; | 3.40.50.300; | null | null | null | null | null | null | null | null | FUNCTION: Plays an important role in meiotic recombination and associated DNA double-strand break repair. {ECO:0000269|PubMed:27760146, ECO:0000269|PubMed:27986806}. | Mus musculus (Mouse) |
E9Q9A9 | OAS2_MOUSE | MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK | 2.7.7.84 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29728}; | defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; interleukin-27-mediated signaling pathway [GO:0070106]; negative regulation of viral genome replication [GO:0045071]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of lactation [GO:1903487]; response to bacterium [GO:0009617]; response to virus [GO:0009615]; RNA catabolic process [GO:0006401]; type I interferon-mediated signaling pathway [GO:0060337] | cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471] | 2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872] | PF01909;PF10421;PF18144; | 1.10.1410.20;3.30.460.10; | 2-5A synthase family | PTM: Myristoylation is not essential for its activity. {ECO:0000250|UniProtKB:P29728}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000250|UniProtKB:P29728}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}. | CATALYTIC ACTIVITY: Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence={ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for ATP {ECO:0000269|PubMed:15865429}; Note=kcat is 6.4 sec(-1) for ATP. {ECO:0000269|PubMed:15865429}; | null | null | null | FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179, ECO:0000303|PubMed:21142819}. | Mus musculus (Mouse) |
E9Q9D5 | RBL2A_MOUSE | MAGDRNRHCELEQEKYDTHENVKIICLGDSAVGKSKLMERFLMDGFQPQQLSTYALTLYKHTATVDGKTILVDFWDTAGQERFQSMHASYYHKAHACIMVFDVQRKITYKNLGTWYAELREFRPEIPCILVANKIDADIQMTQKNFSFAKKFSLPLYFVSAADGTNVVKLFNDAIRLAVAYKESSQDFMDEVLQELENFKLEQKEEDTSGQEQSDTTKSPSPS | null | null | cilium assembly [GO:0060271]; flagellated sperm motility [GO:0030317]; intracellular protein transport [GO:0006886]; photoreceptor cell morphogenesis [GO:0008594]; regulation of exocytosis [GO:0017157]; single fertilization [GO:0007338] | endomembrane system [GO:0012505]; intraciliary transport particle B [GO:0030992]; sperm midpiece [GO:0097225] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | null | null | null | null | null | null | FUNCTION: Plays an essential role in male fertility, sperm intra-flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail. {ECO:0000269|PubMed:23055941}. | Mus musculus (Mouse) |
E9Q9F6 | CTSRD_MOUSE | MLVLMLAAAVATMVRAHTLCRVHTVRTGKVFKSNIQLQGDPLFYAFPNTFVLKNVCKADISVYLGQKVFLTIDNFESSLLPLTVPKSLAVGVPSITSAHFVSGSLVLFVISGKGYSYDYYENTWRKLEGISEPVSHISGDVCCFKGSFCLELSNNLFAYLRGGQIPGTNIYFSDNGGFSFQLMNTDKLSHLTGTLGGIFHLHSMSQVGVLMVENNLGTFHYMEYPLNHSMGIAFSYKNLLEVIMKPYQRGFMVLWNQKSILVSSNSGQIVEHVRLIDQKIFTDLDVEHANINIYSVASNAYELAFLVAEDHLYYGSQSYMGTYVIKLPHQPLWSTHTSIYFEDIGILQVLTPVADPHFAAYDFDKCTVNVQSSLMDEKLALQPCNVELLESTMINTMFTIDMNSKLKLSALMIPRKGENPTPLVMVSNPHALGFKANLNEFGNTFDGNSKYKLDIELKQQHHWGNSDFNFTASIKRHAISSVTVDIADKTLSCVDLKPLSTLISVGCDMTKKIVVQNKISACTMGILNPVQLQKNYTYTIEKEAYDPINHNGEAQDDLIVFYEYKDLGCPRLVYYDKPWKPVVELWKNGIVEEIMNAEYVISEINGLVTYSYSLTAATANCRSQPQNWSTFESDIENEEPFLWNRENYVSCHEDNKDNPLLWPNVEYQVLGGQTNNKIIFGQRNGIYTFHLSVVDPYYSYCNLNTIFSVYVHGALPVTKFQPLLTILLMVTTTLLTAWLAYAIPKQLRSEKGQRLLGFCYQILQLCLGVCFCTWLRGKLRQWLRPRRVKDQNRGKVRVAQKHPET | null | null | flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240]; spermatogenesis [GO:0007283] | CatSper complex [GO:0036128]; sperm principal piece [GO:0097228] | null | PF15020; | null | CATSPERD family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353}; Single-pass type I membrane protein {ECO:0000255}. Note=Specifically located in the principal piece of sperm tail. {ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353}. | null | null | null | null | null | FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:21224844). Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane (PubMed:21224844). {ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353}. | Mus musculus (Mouse) |
E9Q9F7 | CC146_MOUSE | MEYNSKDAEEETEDEEEGLKEAEGEEQEKEEVTATSETDDDQEDLPSVLVPTVNIREERLINLAETPAFLCLHELHSKGKLPGTRMAELKAKYTLLHDTVVSTQESEVQLLENAKRFTEQIQQQQVCLQQAEDFPNVFTTEVCKLREQLLKYQNEYTAAQEREYNIQYRLTSLTEEKSIILKEFEKIPKPGEIEKKTRLLKESTEELRKEVIQRRLEIKNLREDVVLKQKQLVREQKELEELMEYQVGLKDDVVHHQSVPVQITKEIEKMTRKKVETEKKNIVLESELKELSDSLKKLENKVNTLAEERDDIMKEVEGKRTLLEVKEREYGQLLKLLELTKENEASSLAERGILDINLRNCLIDKQNYHDELSRKQREKERDFRNLKKTELLLKVSLDALTQAQAMNQRLLLEMEAIPKEYLTLPERRKELHKEVDLARRNLAQQKSLSEAEAKLVEQQIAQENKLLKEQESLRELVFNLGRMTQIKIDEKEQKAKDFLKAQRRYSEIVKEIKSKDLEIRLYKKRKHEIHRRLREFASLYDTIRNERNKFVNLLHKAHQKVNEIKERLKMSLNELEILRNSAVSQERKLQNAMLKHSNNVTIKESIQNDVCKITAKLQEMKEKKEAQLTSMDRLASMITVIEEEMVQLRKKYEKAVQRRNESGVQLIEREEEVCIFYEKVNVQEKIKLHQDVEIHILEEKIRFLKLRIAEKQRQISVTRKLVPIKKSLDADLAVIQIQFSQCTDRIKDLEKLFVNPDSKGRVRFIKGKDLTEEEMIKKLDMLELQIAKKEEKLLEKDFIYEQVSQLTNRLKGKTQACKKDTLLLAKKMNSYQQKIKVVTQEMMALVAELSMKQALTIELQKEVREKEEFIFSCSARIEKGLPLNREIEKDWLKVLRDEEMYAFATAEMSREYMETDYRQLPNGVYTTAEQRPNAYMPEADTELPLPKPYGAMAPFKPSEPGANRRHIRKPVVKPIEI | null | null | manchette assembly [GO:1905198]; sperm axoneme assembly [GO:0007288]; sperm flagellum assembly [GO:0120316]; spermatid development [GO:0007286] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoskeleton [GO:0005856]; sperm connecting piece [GO:0097224] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IYE0}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:38038747}. Note=In sperm cells, localized to only one centriole identified as the mother centriole by co-staining with CEP164 (By similarity). Localizes to the sperm connecting piece and flagellum during spermiogenesis and to the flagellum in spermatozoa from cauda of the epididymis (PubMed:38038747). {ECO:0000250|UniProtKB:Q8IYE0, ECO:0000269|PubMed:38038747}. | null | null | null | null | null | FUNCTION: Essential for sperm flagellum biogenesis and male fertility. {ECO:0000269|PubMed:38038747}. | Mus musculus (Mouse) |
E9Q9K5 | TRDN_MOUSE | MTEITAEGNASTTTTVIDNKNGCIPKSPGKVLKRSVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSEGDEDDEDADEDIDKGEIEEPPLKRKEIHQEKAEKEEKPEKKIQTKASHREREKGKEKLKGEKPEKTATHKEKLEKKERPETKMMAKEDKKIKTKEKTEEKAKKEMKVGKQEKVKPTAAKAKETPKTPPKARKKDDKEMPAVHEQKDQYAFCRYMIDMFVHGDLKPGQSPVMPPPSLTPSKPALSTTALEEKEKEEKKKMEKKDTSDTKKKEKEVKKKSEETTIDGKGKEPGKPPETKQMTAKLTTQAAARKDEKKEESKKMRKPTEEQPKGKKQEKKEKHIEPAKTPKKEHPGPSEKLKKAKAEQAKEEIAAASTKKALHGKKEEKAKTVEQEVKKEKSGKSSSDLKDKEVKKEKSGKSSSDLKDKEPQLKNEEKSKPQVKKEAKLASSDKGQTRKQNITRPEQVIPHVKPEKAEHQEKGHPSIKKDKPKPSSKGAPEVPDSGKKKIEKSEKESKVPTREENLQVYNVTKAEKPGKIPKDSKEAPASKKDKEDSKEAPTSKKDKEDSKDVPHSKKDKEVTDDVSSPKKQTRPISFFQCVYLNGYNGYGFQFPVTPVQQPGENPGKTNSPGQKQQEQ | null | null | cytoplasmic microtubule organization [GO:0031122]; endoplasmic reticulum membrane organization [GO:0090158]; establishment of localization in cell [GO:0051649]; heart contraction [GO:0060047]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of release of sequestered calcium ion into cytosol [GO:0051280]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to bacterium [GO:0009617] | calcium channel complex [GO:0034704]; cytosol [GO:0005829]; junctional membrane complex [GO:0030314]; junctional sarcoplasmic reticulum membrane [GO:0014701]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; sarcoplasmic reticulum [GO:0016529] | signaling receptor binding [GO:0005102] | PF05279; | null | null | PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19383796}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11707337}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28820}. | null | null | null | null | null | FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength (PubMed:19843516). Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:19383796, ECO:0000269|PubMed:19843516, ECO:0000269|PubMed:22768324}. | Mus musculus (Mouse) |
E9Q9M8 | PWP2B_MOUSE | MEPRAGCRLPVRVEQVVNGALVVTVSCGERSFAGILLDCTKKSGLFGLSPSTLLPLADNSSAVSCHGQAPEEGTGEVMQLETGPLHPHHKDPEKDQPPKTAVSEPPPPLIPPVPAGNLPPFPPYFEGAPFPHPLWLRNTYQQWVPQPPPRTIKRTRRRLSRNRDPGRLILSTIRLRPRQVLCEKCKSTVSPQEASPSPLNTPKPRRRLGSGPDSEHRKPEEPEDSAVIATAAPRRSKREKREEDRVAGERVPRSPVIKISYSTPQGKGEVVKIPSRVHGSVEPFCPQQSLQNGSQDSEVSRDVEPRGGGDRPPSGSSASIPKLKLTRPVPPISDLPPPKIRLKPHRLGDGEHEPLYRAELVEELNGCPRGPLVSSPALFADGSSHGLEDLSSGSSGEDDDLKRFPQGKHGRDGLAFLVDCPGRRTDCTSESVCSTDSLDELKSSGSEVTSPDTGDLSSGDSASVPSSSADTRQTVPPLTVRLHTQSVSRCVTEDGRTVAVGDIVWGKIHGFPWWPARVLDISLGQKEDGEPSWQEAKVSWFGSPTTSFLSISKLSPFSEFFKLRFNRKKKGMYRKAITEAANATQHVAPEIRELLTQFEM | null | null | chromatin remodeling [GO:0006338]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of cold-induced thermogenesis [GO:0120161] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | NuRD complex binding [GO:0120325] | PF00855; | 2.30.30.140; | null | PTM: Deubiquitinated by BRCC3; leading to its stabilization. {ECO:0000269|PubMed:34180153}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34180153}. | null | null | null | null | null | FUNCTION: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (By similarity). Plays a role in facilitating transcriptional elongation through regulation of histone acetylation (PubMed:30228260). Negatively regulates brown adipocyte thermogenesis by interacting with and stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone deacetylation at the promoter leading to the repression of UCP1 expression (PubMed:34180153). {ECO:0000250|UniProtKB:Q6NUJ5, ECO:0000269|PubMed:30228260, ECO:0000269|PubMed:34180153}. | Mus musculus (Mouse) |
E9Q9R9 | DLG5_MOUSE | MEPQRRELLAQCQQSLAQAMTEVEAVLGLLEAAGALSPGERRQLDEEAGGAKAELLLQLLLAKEQDHFQDLRAALEKTQPHLLPILYLNGVVGPPQSTEGAGSTYSVLSIMPSDSESSSSLSSVGTTGKAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMECQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRKSLGGKVVTPLHINLSGQKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFPQSSSWSGQNIFENIKDSDRMLSCRAHGPEVQAHNKRNLLQHNNSTQTDIFYTDRLEDRKELGHSGGSSSFLHKPFSGSSSPVSPQACPSTSERSLNSFRSDTSAERGYGLVDMRSQRPLLSFETEVGPCGAVEVPLDKIDPEGSNSGGTWPKAVLGSTSGPEKLSVYKKPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGLTHSPQPSKRVGSLTPPKPPRRSDSIKFQHRLETSSESEATLVGSSPSTSPPSAPPPSMDPSEPTHASPPRKARVRIASSYHSEGDGDTSYLPAKKPCDEDLTSQKVDELGQKRRRPKSAPSFRPKISPVVIPAQCLEEQECVPAIGELSPEGQEWSPYSPGHASRHGNPLLYPNRPSVGTVPRSMTPGTTVGSILRNPIYTVRSHRVLPCGSPPVPRDAGSQSLSPSVQHQGRLSLDLSHRACSDYSEMRASQGSNSLPSSARLGSSSNLQFKAERIKIPLTPRYPRSVMGSDRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAVNPSSHGERRKDRPFVEEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQYNPHIHQLNSHSRSSSHLDPAATPHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASSTRSVGDTTKKTPDPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKVQYRHEEFTRVKGLPGDSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQEFSRRLSMSEVKDDNTAKTLSAAARRSFFRRKHKHKRSGSKDGKDLLALDTFSNDSIPLFEDSVSLAYQRVQKVDCTSLRPVLLLGPLLDVVKEMLVNEAPGKFCRCPLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEYSRYFTGVVQGGALSSICTQILAMVSQEQSKVLWIPACPP | null | null | apical protein localization [GO:0045176]; epithelial to mesenchymal transition [GO:0001837]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; maintenance of cell polarity [GO:0030011]; metanephric collecting duct development [GO:0072205]; midbrain development [GO:0030901]; negative regulation of cell migration [GO:0030336]; negative regulation of hippo signaling [GO:0035331]; negative regulation of T cell proliferation [GO:0042130]; neuroepithelial cell differentiation [GO:0060563]; polarized epithelial cell differentiation [GO:0030859]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of hippo signaling [GO:0035332]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of synapse assembly [GO:0051965]; postsynapse organization [GO:0099173]; protein localization to adherens junction [GO:0071896]; protein-containing complex assembly [GO:0065003]; regulation of apoptotic process [GO:0042981]; zonula adherens assembly [GO:0045186] | adherens junction [GO:0005912]; cell junction [GO:0030054]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | beta-catenin binding [GO:0008013]; cytoskeletal protein binding [GO:0008092] | PF16610;PF00625;PF00595;PF04822; | 2.30.42.10;1.10.533.10;3.40.50.300;2.30.30.40; | MAGUK family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q8TDM6}. Cell membrane {ECO:0000250|UniProtKB:Q8TDM6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDM6}. Postsynaptic density {ECO:0000269|PubMed:25232112}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localized at sites of cell-cell contact. {ECO:0000250|UniProtKB:Q8TDM6}. | null | null | null | null | null | FUNCTION: Acts as a regulator of the Hippo signaling pathway. Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714). Positively regulates the Hippo signaling by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (By similarity). Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin (PubMed:25232112). Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (PubMed:25644602). {ECO:0000250|UniProtKB:Q8TDM6, ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:25644602, ECO:0000269|PubMed:28087714}. | Mus musculus (Mouse) |
E9Q9U0 | U17PB_MOUSE | MVVALSFPEADPAMSPPSAPELHQDEAQVVEELAANGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSAFHKRKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQNDLKKGSINMPEGRIHEVLDAKYQLKKSGEKKHNKSPCTEDAGEPCENREKRSSKETSLGEGKVLQEQDHQKAGQKQENTKLTPQEQNHEKGGQNLRNTEGELDRLSGAIVVYQPICTAN | 3.4.19.12 | null | proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF00443; | 3.90.70.10; | Peptidase C19 family, USP17 subfamily | PTM: Ubiquitinated. {ECO:0000269|PubMed:14583620}. | null | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:14583620}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. {ECO:0000269|PubMed:14583620}. | Mus musculus (Mouse) |
E9Q9W4 | S27A6_MOUSE | MLLSWLTGLGAGLLSLHFLQKLLFPYFWDDFWYLLKVVRYGIQMEMYKLRGELVTVLDKFLSHTRKQPRKAFIIYEGDVYTYEDVDKRSNRIAHALLNHSSLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFDSLLHCINTCEPTAVVVGGDLLGSIEEILPSLPKHVRVWGMKDSVPEGIDSLQEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQLQVLKGSVGLWAFGCTADDIIYITLPLYHSSGSLLGIGGCVELGATCVLKKKFSASQFWNDCKKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGLSSDVWRQFLDRFGNIKMCELYGATEGNIVFMNHTGKIGSVGRANFFYSLFFSFELIKYDFQKDEPWRNGQGWCSCVRKGEPGLLISRVNKKNPFFGYAGSDTHTKSKLLFDVFRKGDVYFNTGDLMFQDQENFVYFWDRLGDTFRWKGENVATTEVADVLGRLDFIQEANVYGVRVPGYEGKAGMTSVILKPNKSLDLEKMYNQVVTSLPAYACPLFLRIQDKMETTGTFKLKKLQLVEEGFDPLKISDPLYFMDNLKKSYVPLTEEIYNQIMSEEVKL | 6.2.1.-; 6.2.1.15; 6.2.1.3 | null | long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | arachidonate-CoA ligase activity [GO:0047676]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; nucleotide binding [GO:0000166]; oleate transmembrane transporter activity [GO:1901480]; very long-chain fatty acid-CoA ligase activity [GO:0031957] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Y2P4}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:15699031}; Multi-pass membrane protein {ECO:0000255}. Note=In heart is exclusively located on the sarcolemma in areas juxtaposed with small blood vessels where it colocalizes CD36. {ECO:0000250|UniProtKB:Q9Y2P4}. | CATALYTIC ACTIVITY: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256, ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in); Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000269|PubMed:15699031}; | null | null | null | null | FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (By similarity). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:15699031). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation such as the heart (By similarity). {ECO:0000250|UniProtKB:Q9Y2P4, ECO:0000269|PubMed:15699031}. | Mus musculus (Mouse) |
E9Q9W7 | PDZD7_MOUSE | MARGFTVGFDPLGLGELSSGSLSSVSSRGHLGSDSGSTATRYLLRKQQRLLNGPSRGIRASSPMGRVILINSPIEANSDESDIIHAVRVEKSPSGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVRLLTSSSCLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCSSTPSDRSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSYASSAPCSSGSLPSDRMDVCLGPEEPTSHGPGWGRADTAMQTEPDLDSRVETWCSVRPTVILRDTAIRSDGPSSTRHLDSALSESPKTALLLALSRPRTPITRSQSHLTLWEEKKQRKKEKSGSSGEKGALQRSKTLMNLFFKGGRQGRPAGDGHREAWTLDSRSPTKVRPRLDLEKAGSVGPVQKFVTWRLRRDRERGRALLSARSGSPSGQAPTVNEQVQAWESRRPLIQDLARRLLTDDEVLAVTRHCSRYVHEGGVEDLVRPLLAILDRPTKLLLLRDIRSVVAPTDLGRFDSMVMPVELEAFEALKSRAVGPSALRPTRQDTPPKRHLITPVPDSRGGFYLLPVNSSEDEDGEIREKLGVLKVSLGASAPHHKGIPPLQDVPVDAFSLRRGACAPPPQPPPVAPRPPRPNWLLTEPLSREDTQQNQSQTPAQSCSRSRSRSRSRSHSRGQGKSPGRRRSPSPAPIATAATANGRYHRPRKARPLLPRLLDGQVAKVGARQGPLENGRIAEEAVGNVSTGALRTITLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLCGDLQAGFELVAVDGESLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPGLLPLASDLRVVKDQSLAPDCPSALGPVDDARILTQLPPPEARQLQQSLSSALKVPQSIPKLSPILKDPHDPS | null | null | auditory receptor cell development [GO:0060117]; auditory receptor cell stereocilium organization [GO:0060088]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; establishment of localization in cell [GO:0051649]; establishment of protein localization [GO:0045184]; inner ear receptor cell differentiation [GO:0060113]; sensory perception of sound [GO:0007605] | cilium [GO:0005929]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stereocilia ankle link [GO:0002141]; stereocilia ankle link complex [GO:0002142]; stereocilium [GO:0032420]; stereocilium tip [GO:0032426]; USH2 complex [GO:1990696] | identical protein binding [GO:0042802] | PF00595; | 1.20.1160.20;2.30.42.10; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9H5P4}. Nucleus {ECO:0000250|UniProtKB:Q9H5P4}. Cell projection, stereocilium {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. Note=Localizes at the ankle region of the stereocilia. {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. | null | null | null | null | null | FUNCTION: In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links (PubMed:24334608). Blocks inhibition of adenylate cyclase activity mediated by ADGRV1 (PubMed:24962568). {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:24962568}. | Mus musculus (Mouse) |
E9QA28 | CEA16_MOUSE | MKMPLTWYSWFLLSAWILNTGAEISITPEPAQPAEGDNVTLVVHGLSGELLAYNWYAGPTLSLTFLVASYIVSTGDETPGPAHTGREAVRPDGSLDIHGALPGHTGTYILQTLNRQFQTEVGYGHMQVYEILAPPTVMANDTALVERRDTLRLVCSSPSPAEVRWFFNGDALPVAVRLGMSPDGRMLTRHGVRREEAGAYQCEVWNPVSVSRSEPLNLTVYFGPERVAILQDSTTRTGCTIKVDFNMSLTLWCVARSCPEPEYVWAFNGKALKNGQDHLNISSMTAAHEGTYTCIAKNSKTLLSGSASVVVKLSAAAVAMMIVPVPTKPTEGQDVTLTVQGYPKDLLVYAWYRGPASEPNRLLSQLPSGNWIAGPAHTGREVGFANCSLLVQKLNLTDAGRYTLKTVTLQGKTDTLEVELQVAPLE | null | null | sensory perception of sound [GO:0007605] | extracellular space [GO:0005615]; stereocilium tip [GO:0032426] | identical protein binding [GO:0042802] | PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, CEA family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21368133}. Note=Localizes at the tip of cochlear outer hair cells and to the tectorial membrane. {ECO:0000269|PubMed:21368133}. | null | null | null | null | null | FUNCTION: Required for proper hearing, plays a role in maintaining the integrity of the tectorial membrane. {ECO:0000269|PubMed:25080593}. | Mus musculus (Mouse) |
E9QA62 | LMOD3_MOUSE | MSGHSRNSEQEDTLSEELDEDELLANLSPEELKELQSEMEVMAPDPHLPVGMIQKDQTDKAPTGNFNHKSLVDYMYLQKASRRMLEDERVPVSFVQSEKNTQNQREVGDKGIKNMPQFLKEKLNSEILAKKRESNGSNNVQEAEDDDEDEEEEEEDDEDEEEEEEDEEDDEGEEDEDGEQANREKNDAKEQIHNNPGTYQQLATKTAHEQKDTSETKEKGEKKIAKLDPKKLALDTSFLKVSARPSGNQTDLDGSLRRVRQNDPDMKELNLNNIENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSVTTLNIESNFITGKGIVAIMRCLQFNETLTELRFHNQRHMLGHHAEMEISRLLKANTTLLKMGYHFELPGPRMVVTNLLTRNQDKRRQKRQEEQQQQQLKEQRKLIAMLENGLGLPPGMWERLGGPMPDPRMQEFFQPASGRPLDAQEVPFGSRKEMIKNPPQPPQCKTDPDSFRVVKLKRIQRKSRMPEAREAQEKTNLKDVIKTLKPVPRNRPPPLVEITPRDQLLNDIRHSNVAYLKPVQLPKELE | null | null | actin filament organization [GO:0007015]; actin nucleation [GO:0045010]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; positive regulation of skeletal muscle fiber development [GO:0048743]; skeletal muscle fiber development [GO:0048741]; skeletal muscle thin filament assembly [GO:0030240]; striated muscle contraction [GO:0006941] | A band [GO:0031672]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865] | actin monomer binding [GO:0003785]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | PTM: Ubiquitinated, leading to its degradation. Interaction with KLHL40 negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:24960163}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:24960163}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VAK6}. Note=Highly expressed in nonstriated areas of developing myotubes, where it shows a granular cytoplasmic pattern. In sarcomeres, highly expressed in the M band region and, at lower levels, along actin thin filaments. Not detected in Z-disks. In sarcomeres, may be located near, but not at, actin thin filament pointed end. {ECO:0000250|UniProtKB:Q0VAK6}. | null | null | null | null | null | FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25774500, PubMed:26035871). Increases the rate of actin polymerization (By similarity). {ECO:0000250|UniProtKB:Q0VAK6, ECO:0000269|PubMed:26035871}. | Mus musculus (Mouse) |
E9QAG8 | ZN431_MOUSE | MVDALTYDDVYVNFTQEEWALLNPSQKSLYKDVMLETYRNLNAVGYNWEDSNIEEHCESSRRHGRHERNHTGEKPYEGIQYGEAFVHHSSLQMRKIIHTGEKRYKCNQCDKAYSRHSILQIHKRTHSGEKPYECNQCGKAFTQHSHLKIHMVTHTGEKPYKCDQCGKAFAFHSTLQVHKRTHTGEKPYECNQCSKAFAHHCHLRVHKRIHTGEKPYKCDQCGKAFVGQNDLKRHERVHTGEKPYKCNECGKAFVCNASLRTHKTTHTGVKPYECKQCTKSFASHGQLQKHERIHTGEKPYKCDQCGKAFASHDKFQKHERIHIGEKPYKCKQCTKSFASHDKLQKHERIHTGEKPYECKQCTKSFASHNKLQKHERIHTGEKPYKCDQCNKAFVYESYLQVHKKTHTGEKPYKCNECGKAFARHSHLKVHKITHTGEKPYKCNQCGKALAYHSTLQVHQRTHTGEKPYECEQCGKAFANQSYFQVHKRIHTGEKPYKCDQCGKAFVGSSDLKRHERVHTGRETLQM | null | null | cell differentiation [GO:0030154]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01352;PF00096;PF13894;PF13465; | 6.10.140.140;3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1. {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}. | Mus musculus (Mouse) |
E9QAM5 | HELZ2_MOUSE | MASVGCSLRSASTSATNGPSLAGLCAKVDLYLGCSRCTQCLNESTYILREVEHTCPREILLARFKQAAESKIWRKVGRRPSFPTPMRYQVCHYYRPGLGCRRHWNRCTFARSPEEALVWTFELKNNLPRLKLKEAVQGTRAPDRLQTPADTIRAEFGGHFQLLCAICFTCCPPCLCPVDPRGHCPKHQICPTLLIHVIVEGLKRQFVEVRPLPQRRHPLNYCMYVGRGVPCRHGASRCEYAHSAVEMAVWKAEQLDGLQRGDLLTYPLFGENKWKASPNPNPPVTKLYCHACLVTCNSQEAFENHCSSLEHAQMVAFDQAVPWKHRAPPMGLSKFDLCPRPDLCEHGEVCIKAHSKQELQEWVQRAQDMELREQAAWQDGLVPYQARLLAEYQRSSKEVSVMAETIRGVSVTCHPPPVHQAQEKIQHQWVFTIHSEDPLLHVALLNQEPGAAFSLVAPSLPPHQLYAQGKHFCVQSSPAQYKVGVLVQAVAFGSFEQWVVFDFGRRPVLLQKLKLQLGQTHSQGLNGKPAPSHPQELECWHTGNRHVVLEVDWTPEQEALMAKYKLPSLALEFNQIVPDWGPISRSNYRQRMHKFLYEEEAAQQQLVAKLAMKGQVSLKTALETPALGMLFAPPGALYAKVPFHSSLLPDTDQGFLLSRAVSTALVAPVPAPNSTVYQVRLEARASSDHALWLLLPARCCMALGLQAQDSPILEVQFQIDPMTFRFWHQAVDALLEEHLVVPDLPACTLPHPWPTPPSFRGNHKQKLAVGLIAGRRPEGTKHIPPLLIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNSAADIYIREYFHDYVSSGHPEATPLRVMYADRPPRQTDPTTLQYCCLTEDRQAFRPPTGPELVHHRLVVTTTSQARELQVPAGFFSHIFIDEAAQMLECEALIPLSYALSLTRVVLAGDHMQVTPRLFSVPRDKSARHTLLHRLFLYYQQEAHKIAQQSRIIFHENYRSTAAIINFVSHHFYLAKGNPIQASGKVPRHPQHYPLMFCHVAGSPEQDMSMTSWLNSAEVTQVVEKVREIYNTWPHCWGPREQRHICAVSHGAQVSALRQELRRRNLGEVSVGSFEILPGREFRVVVLSSVHNRNSLLSPGAPTSEFFTEPRVLNTVMTRAQSQLVAVGDAVALCSSGACRNLWRSFIRECIEHHSAFPEELSLEQIEQGVAQRQNWASLTLKARGPETEQKSMAQGPQRLIAEGTMVTVKAETRAEAAAKAQTAAVAAEDTASGNSASRDAAAEVSTLEGGMSEEDSESDFWPSDWELNADDAILKELLDESQQVTVTVREDGLLDTVVCSAPQKAREYTNLPSSVLWKFLRSNSKQFRRCSFLQETFERALATPLDDMASSPIQVRGRLNCGMAFTGDEVLVQILGPAGDDRCVPGSLQGRVMGVLKRRRHELAFVCRMDEWDPRIMIPINGSVTKIFVAEMKDPQQVPIHRLIQGQVQRVRHETLKPEDRSTRLFWVRIVLWRERFYYPLGIVLEVLPKAITWEQGLYILDLEHGLKAHTPDPASVSKALQRYRSELNTAAGHREDYRHFLTFTVDPQGACNLDDALSVRDLGPVYEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNREPVLMLPASLCQDALSLLPGQDRLAISLFLTMEKGGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRHPGAGLELPAHLDSVEACVVAACYFSWMLRRQRLSAACYYEPPDEDSVLGFRTAHIMVQEYMIQFNSHVAEFLVSNKHTQTLTPLRWQPTPSRQQLDSVFKKYRGLVPLSLHLCHHSNTDYTPNKQLHLLTSLWKQVQLAAGTQDYSQMVDLIAADDMHPSLAPACLDLRRALGRSVFGRSSQGKQQPAVHHSLQVDWYTWATSPIRRYLDVVLQRLILLALGHRGSTYSNRDIDGLCLDFSRQYASAQSYQRRAYSLHLAIQLKSQPQNKLGFVVDVEMGARCFKVLFPINRETLPDPCPIHYHSLQLAEHPQELVSQTGVRLVWRRRMYSVQASKLPLPLLGTSLDPHTQTVDAALWMKLLMLLKEQRWPEIAALIQEQDKRFHPREKVKIHQSRCGHFVEVVYELGSGDTLQVQLGSSLQRGFLAPTLKLWTVVPGFSLCLEHMERPGDCFSSHVHQALQDQYLQVGEYSGAWGPRCALESLTNAVTENDSIVLHDVHISWDTSQGQLQGTFQLEAAFLQEKCINIHFGCCYLCIRLEGLPLPLDSSLPGPSGLGPFLNIDPNTYTWVAHGLSGDWDHELAGGDWDQENVDDRQEAPKQVYFLIHHMTMEKVPEEVLRPSARFTVEVLSKQLPDLRKEEAVRQLKTASPLVISIALGLPIPEIRWPISGPRRLVSELRWPIPGPRRPVSEPHRPMSGPCGPISEPCRSIPEPCRGNWPRQHSFHKASTSRFLERQNYNIPAGHHKLNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVYWFHRSNQEQMPTDSSPSGEEQLGGPCVLYCGPSNKSVDVLGGLLLRRKTEMKPLRVYGEQAEATEFPLPGVSNRSLFGKTSQEGRPNQSLRSITLHHRIRQAPNPYAAEIRKFDAQLREGKIFSKEDLRVYRRVLGKARKHELERHSVILCTCSCAASKSLKILNVRQILIDEAGMATEPETLIPLVCFSKTVEKVVLLGDHKQLRPVVKSEQLQSLGMDRSLFERYHRDAIMLDTQYRMHKDICSFPSVEFYGGKLKTWSDLRRLPSILGHTGKPSCSVIFGSVQGHEQKLLVSTEDGNENSRANPEEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGLMQRGVTGVTVTSITKSQGSEWRYVIVSTVRTCPRSDVDQRPTKSWLKKFLGFVVDPHQVNVAITRAQEALCIIGDHLLLRCCPLWHRLLDFCEAQHSLVSAEKVRVQRKSALSS | 3.1.13.1; 3.6.4.13 | null | regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; P granule [GO:0043186] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exoribonuclease II activity [GO:0008859]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF13086;PF13087;PF00773; | 3.40.50.300; | DNA2/NAM7 helicase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYK8}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000250|UniProtKB:Q9BYK8}; 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:Q9BYK8}; | null | null | null | null | FUNCTION: Can degrade highly structured RNAs through its concerted ATP-dependent RNA helicase and 3' to 5' exoribonuclease activities (By similarity). Shows a strong preference for pyrimidine over purine residues for its nuclease activity (By similarity). Acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA (PubMed:23525231). {ECO:0000250|UniProtKB:Q9BYK8, ECO:0000269|PubMed:23525231}. | Mus musculus (Mouse) |
E9QAT4 | SC16A_MOUSE | MQPPPQAVPSGVAGPPPAGNPRSMFWANSPYRKPANNAPVAPITRPLQPVTDPFAFNRQTLQNTPVGSSSKSSLPNLPGPALSVFSQWPGLPVTPTNAGDSSTGLHEPLSGTLSQPRADASLFPPASTPSSLPGLEVSRNAEADPSSGHEVQMLPHSAHYIPGVGPEQPLGGQMNDSGSGPDQPMNRHAPHDGAVTHAASPFLPQPQMPGQWGPAQGGPQPSYQHHSPYLEGPVQNMGLQAASLPHFPPPSSLHQGPGHESHAPQTFTPASLASGEGNEIVHQQSKNHPLSSFPPKHTFEQNSRIGNMWASPELKQNPGVNKEHLLDPAHVNPFTQGNSPENQAHHPPVAATNHALQEAASGALSMFFQGEETENEENLSSEKAGLDKRLNLDSFSSTSRLGHPPPPGASGVYQAFPRGPSSEAAQEGDAQPYFSQSVGVRLDKQSTVPPANDAWGDVPGTGTRCASGPQCENVENLEFVQNQEVLPRETLSVDPFPLSDQIRYGPLPGPAASRPATVGLTRGGGLNLEAPDTPLHPTRPDSVSSSYSSHSHRSPPGSARPQELVGTFIQQEVGKLEDDTSGSFFKQIDSSPVGGETDEVTGSQNCCSSLSQPSTPSPPKPTGVFQTSANSSFEPVKSHLVGVKPVEADRANMVVEVRGTQYCPKKRRAAVAPPDATSGNLEQPPDNMETPCAPQACPLPLSTTGEAGQLVSNTAGTPLDTVRPVPDKRPSARAQGPVKCESPATTLWAQNELPDFGGNVLLAPAAPALYVPVKPKPSEVVHHPEKGMSGQKAWKQGSVPPLQNQDPPGASENLENPPKVGEEEALPVQASSGYASLLSSPPTESLHNQPVLIAQPDQSYNLAQPINFSVSLLNPNEKNQSWGDAVVGERSIVSNNWALGGDPEERAALSGVPASAVTGASLPSSIPQNCAPQGSGSSEMIASQSASWLVQQLSPQTPQSPHPNAEKGPSEFVSSPAGNTSVMLVPPASSTLVPNSNKAKHSSNQEEAVGALDFTLNRTLENPVRMYSPSPSDGPASQQPLPNHPRQSGPGLHNQDHFYQQVTKDAQDQHRLERAQPELVPPRPQNSPQVPQASCPEPSNPESPPTQGQSESLAQPPASPASVNTGQLLPQPPQASSASVTSTNSSQAAVRSEQLWLHPPPPNTFGPAPQDLASYYYYRPLYDAYQSQYPSPYPSDPGTASLYYQDMYGLYEPRYRPYDSSASAYAENHRYSEPERPSSRASHYSDQLAPRQGYPEGYYNSKSGWSSHSDYYANYYSGQYDYGDPSRWDRYYGSRLRDPRTWDRRYWYDSEHDPYRKDHYAYSDRPEKCDDHWRYDPRFTGSFDDDAEIHRDPYGEEADRRSIHSEHSARSLRSTHSLPSRRSSLSSHSHQSQIYRSHHVTGGSFEAPHAPGSFHGDYAYGTYASNFSGAHGFPEYSYPADTSWPAVEQVPSRPTSPEKFTVPHVCARFGPGGQLLKVIPNLPSEGQPALVEIHSLETLLQHTPEQEEMRSFPGPLGKDDTHKVDVINFAQNKATKCLQNESLIDKESASLLWKFIILLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNEAVEQVEEEESGEAQLSFLTDSQTVTTSVLEKETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRFANSLPINDPLQTVYQLMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASKGLLDAAHFCYLMAQVGFGVYTKKTTKLVLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAHTCSLPNFQVFKFIYLCRLAEMGLATQAFHYCEVIAKSVLTQPGAYSPVLISQLTQMASQLRLFDPQLKEKPEEESFVEPAWLVQLQHVERQIQEGTVLWSQDGTEPQQCRITSGSEVEQSDGPGLNQQAGPQADNPLLMPSTEPLMHGVQLLPTAPQTLPDGQPAHLSRVPMFPVPMSRGPLELSPAYGPPGSALGFPESSRSDPAVLHPGQALPPTTLSLQESGLPPQEAKSPDPEMVPRGSPVRHSPPELSQEEFGESFADPGSSRTAQDLETSPVWDLGSSSLTRAPSLTSDSEGKKPAQAVKKEPKEPKKTESWFSRWLPGKKRTEAYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSFPRVPQVAPTGPAGPPTASVNVFSRKAGGSRARYVDVLNPSGTQRSEPALAPADFFAPLAPLPIPSNLFVPNPDAEEPQPADGTGCRGQAPAGTQSKAESTLEPKVGSSTVSAPGPELLPSKPDGSQGGEAPGDHCPTGAPHGGSVPFYNPAQLVQASVTSGNSRPGRIGQRKYAALN | null | null | autophagy [GO:0006914]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum organization [GO:0007029]; Golgi organization [GO:0007030]; Golgi to plasma membrane transport [GO:0006893]; protein exit from endoplasmic reticulum [GO:0032527]; protein localization to endoplasmic reticulum exit site [GO:0070973]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; response to endoplasmic reticulum stress [GO:0034976] | cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471] | null | PF12932;PF12931; | 1.25.40.1030; | SEC16 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15027}. Microsome membrane {ECO:0000250|UniProtKB:O15027}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882). Recruited to microsomal membrane in SAR1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:25201882}. | null | null | null | null | null | FUNCTION: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17428803). Mediates the recruitment of MIA3/TANGO to ERES. Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (By similarity). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in adipocytes (PubMed:27354378). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:27354378}. | Mus musculus (Mouse) |
E9QAU8 | ARK2C_MOUSE | MVLVHVGYLVLPVFGSVRNRGAPFQRSQHPHATSCRHFHLGPPQPQQLAPDFPLAHPVQSQPGLSAHMAPAHQHSGTLHQSLTPLPTLQFQDVTGPSFLPQALHQQYLLQQQLLEAQHRRLVSHPRRNQDRVSVHPHRLHPSFDFGHQLQTPQPRYLAEGTDWDLSVDAGLSPAQFQVRPIPQHYQHYLATPRMHHFPRNSSSTQMVVHEIRNYPYPQLHFLALQGLNPSRHTSAVRESYEELLQLEDRLGNVTRGAVQNTIERFTFPHKYKKRRPQDSKGKKDEGEESDTDEKCTICLSMLEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLGADS | 2.3.2.27 | null | axonogenesis [GO:0007409]; forelimb morphogenesis [GO:0035136]; innervation [GO:0060384]; limb development [GO:0060173]; motor neuron axon guidance [GO:0008045]; muscle structure development [GO:0061061]; positive regulation of BMP signaling pathway [GO:0030513]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209] | nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF13639; | 3.30.40.10; | Arkadia family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23610558}. | 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; Evidence={ECO:0000269|PubMed:23610558}; | null | null | null | null | FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of motor axon elongation (PubMed:23610558). Required for efficient motor axon extension in the dorsal forelimb by enhancing the transcriptional responses of the SMAD1/SMAD5/SMAD8 effectors, which are activated downstream of BMP (PubMed:23610558). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD6, SMAD7, SKI and SNON isoform of SKIL (PubMed:23610558). {ECO:0000269|PubMed:23610558}. | Mus musculus (Mouse) |
E9QBI7 | OMA1_DANRE | MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRWHFLGAGTGLLFIASLFFFTHLDESPITGRTRLLVFSRKNFRELAQFNADAFMEEFKDSLIASSDPRHKVVEQVVQILAQRNQDIAEISAVPWTVHVVDSPTMNAFVLPNGEIFVFTGMLNAVTDIHQLTFILGHEMAHALIGHAAEQASLSHVVELLSLVLLTAIWAVCPRDSLAALGHWIQGKLVQFLFDRPFSRKLEAEADQVGLQMAAKACADVRAGPVFWEQMEIFDQLSGQPTMPEWLSTHPSHQNRVRQLDRLIPEALELRARCNCPELPKTDPRVVFNEAVRLVLEGKKEQMLEKEEKNGKTQTGDMFP | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O75844}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844}; | diet induced thermogenesis [GO:0002024]; energy homeostasis [GO:0097009]; glucose metabolic process [GO:0006006]; HRI-mediated signaling [GO:0140468]; integrated stress response signaling [GO:0140467]; lipid metabolic process [GO:0006629]; mitochondrial protein processing [GO:0034982]; mitochondrial respiratory chain complex assembly [GO:0033108]; negative regulation of mitochondrial fusion [GO:0010637]; positive regulation of apoptotic process [GO:0043065]; protein autoprocessing [GO:0016540]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; regulation of cristae formation [GO:1903850]; zymogen activation [GO:0031638] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01435; | 3.30.2010.10; | Peptidase M48 family | PTM: Autocatalytically cleaved in response to mitochondrial depolarization both at the N-terminus and C-terminus to generate the short active form (S-OMA1). The S-OMA1 form is unstable. {ECO:0000250|UniProtKB:Q9D8H7}.; PTM: May form a redox-dependent disulfide bond (By similarity). Exists in a semi-oxidized state and is activated by prolonged hypoxia (By similarity). {ECO:0000250|UniProtKB:P36163, ECO:0000250|UniProtKB:Q96E52}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}. | null | null | null | null | null | FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as opa1 and dele1 (By similarity). Involved in the fusion of the mitochondrial inner membranes by mediating cleavage of opa1 at S1 position, generating the soluble opa1 (S-opa1), which cooperates with the membrane form (L-opa1) to coordinate the fusion of mitochondrial inner membranes (By similarity). Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of opa1, leading to excess production of soluble opa1 (S-opa1) and negative regulation of mitochondrial fusion (By similarity). Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of dele1 to generate the processed form of dele1 (S-DELE1), which translocates to the cytosol and activates eif2ak1/hri to trigger the ISR (By similarity). Required for the stability of the respiratory supercomplexes (PubMed:26365306). {ECO:0000250|UniProtKB:Q96E52, ECO:0000250|UniProtKB:Q9D8H7, ECO:0000269|PubMed:26365306}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QDC5 | HWA_DANRE | MSQLGSAVPSSNLPEGLPVSSLALLILVLIPCVLLLLLLNCLFVGYKLFRMTRRKRDRYGSEMSLMHSSYSTRQRITRFSDEPPVAPNRKTNYVSVSEPMLAPPITSSLTSSAERRATGQRAMFLRPDGATYAGSESLRVPHWRTSAPVLVQSSDSDMERVNTVPPNSPVLRVTPNGFSVPMTSLRRSSTMELESTSLDKIHVECESASIIPQENSCYVVSSSSSARGSGLDSDFGASAGVSLRILSMDSDGFPGSAWASALEWDYYDPSYVTQNHVPKHRPQAPPITTKQYWV | null | null | dorsal/ventral pattern formation [GO:0009953]; embryonic axis specification [GO:0000578]; positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification [GO:2000055]; protein destabilization [GO:0031648]; regulation of canonical Wnt signaling pathway [GO:0060828] | plasma membrane [GO:0005886] | null | null | null | Huluwa family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30467143}; Single-pass membrane protein {ECO:0000255}. Note=Enriched on the plasma membrane of blastomeres only in a small region in which the dorsal organizer will form. {ECO:0000269|PubMed:30467143}. | null | null | null | null | null | FUNCTION: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1) (PubMed:30467143). Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2) (PubMed:30467143). Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression (PubMed:30467143). {ECO:0000269|PubMed:30467143}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QG68 | UBP45_DANRE | MRLKDPFSLKTADMTKRSNKPKKPRDEDSSDEVGGLTCQHVSRAVDLSSVKKAVTGSLWSVCSDCLKERNVLEGETAGAHDILVCLKCGFQGCNQAEVQHSTKHQQAHHSDSHCITISLTTWKAWCFECKEELSTHCNKKALAQTLDFLQKQSAKATSGTSSKLIKLREEPAEYVDTQRGKSPVNSTLIPVKGINNLGNTCFFNAVMQNLSQTHMLNDLIQDVKEKGHKMKISPSTETNLGSLTVTLPSPEPLTSAMFLFLQSMKESGKGPVSPKILFNQLCQKAPRFKGYQQQDSQELLHYLLDSMRVEETKRIKAGILKAFNNPTEKTADEETKRQVKAYGKEGVKLNFVDRIFVGELTSTIMCEECEHISTVKEAFIDISLPIIEERISKPTNPARLGKSGREQDSLTSHDDSLAAHSQANRNSRRLSGQKLQSRHSSTSHDDRGPDTVSSRQEEDLCVAGRGLSSYRTDTMGSQSDCSEKESNLQDSSNDADSEASESEWSPRIPSVSSHSSTSDKTSITTTLSTTTHNPSLKSNPSSTPLPSIRPQQGGAVEQLVSAVSKLGLVHTSTDTLPISHSQEELSETRDRDRQHHQGAFQVLCHSYTPSSKECSVQSCLHQFTSIELLMGNNKLLCENCTDRRQRQMKRSDKKAEKVYTSARKQMLISALPPVVTLHLKRFHQAGMNLRKVNRHVDFPLLLDLAPFCSATCKNLGSGERVLYSLYGIVEHSGSMRGGHYAAYVKVRTPQRKPEQRRNQSGSREACSAPQGQWVYVSDTTVQTVPESRVLNSQAYLLFYEELL | 3.4.19.12 | null | cell migration [GO:0016477]; neural retina development [GO:0003407]; photoreceptor cell maintenance [GO:0045494]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917] | cysteine-type deubiquitinase activity [GO:0004843]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Photoreceptor inner segment {ECO:0000269|PubMed:30573563}. Cytoplasm {ECO:0000250|UniProtKB:Q70EL2}. Nucleus {ECO:0000250|UniProtKB:Q70EL2}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q70EL2}; | null | null | null | null | FUNCTION: Catalyzes the deubiquitination of SPDL1 (By similarity). Plays a role in the repair of UV-induced DNA damage via deubiquitination of ERCC1, promoting its recruitment to DNA damage sites (By similarity). May be involved in the maintenance of photoreceptor function (PubMed:30573563). May play a role in normal retinal development (PubMed:27613029). {ECO:0000250|UniProtKB:Q70EL2, ECO:0000269|PubMed:27613029, ECO:0000269|PubMed:30573563}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QI36 | HARS1_DANRE | MADKAQLQEAIKTQGEVVRKLKSEKASKEQIDEEVARLLQLKAQLGGDEGKHVFVLKTAKGTRDYNPKQMAIREKVFNIIINCFKRHGAETIDSPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKITNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGQYDAMIPDAECLKLVYEILSELDLGDFRIKVNDRRILDGMFAICGVPDEKFRTICSTVDKLDKLAWEEVKKEMVNEKGLSEEVADRIRDYVSMQGGKDLAERLLQDPKLSQSKQACAGITDMKLLFSYLELFQITDKVVFDLSLARGLDYYTGVIYEAILTQANPAPASTPAEQNGAEDAGVSVGSVAGGGRYDGLVGMFDPKGRKVPCVGVSIGIERVFSIMEQKAELSSEKVRTTETQVLVASAQKNLLEERLKLTAELWNAGIKAEVLYKKNPKLLSQLQHCEDTGIPLVAILGEQELKDGVVKLRNVASREEVDVPRAELVDEVKKRTS | 6.1.1.21 | null | histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial translation [GO:0032543]; nematode larval development [GO:0002119]; regulation of vasculature development [GO:1901342]; sprouting angiogenesis [GO:0002040] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF03129;PF13393;PF00458; | 3.40.50.800;1.10.287.10; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:28934368}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:28934368}. | CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21; Evidence={ECO:0000250|UniProtKB:P12081}; | null | null | null | null | FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA. {ECO:0000250|UniProtKB:P12081}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QJ30 | KL40B_DANRE | MALPIDPMEEPRMYQQTLLQDGLYDLLESDMMVDCVLKIKDKEFPCHRLVLAACSSYFRAFFKSGVEESKQREIVLEDVEPGVMGIILKYLYTSNINVTEQNVQDIFALSNMLQIPSIFTVCVSFLQKRLSLSNCLAIFRLGLMLDCPRLAISARNFACERFQFITRDEEFLQLTPSELAAVLASDSLNVETEQDVFEALIKWVGHDQENRIGDLPDLLDCIRLRLVPRDYFVKNVEKHEWLSSNPEITKKLQLVKDAHAGKLPELKKTKNKKSPSEEGQKKGDEEEVEEEEEQEERLPGILNDNLRFGMFLRELIFLINDSASVAYDPTGNDCYVASVSTQIPKNHCSLVTKENQIFVAGGLFFDEQSKDEQIYSYFLQFDPASSDWMGMPPIPSPRFLFGMGEAENFIFVIGGREMKEGENILNTVMVYDRQFLKWAESDPLPYLVYGHGVVSHNEMIYVIGGKGENKECLNRVCAYDIKTHQWKDLAPLNTARSLFGVTIHKNNIYVVAGVTDSGLTGSAEVYDIKTNKWSEFVEFPQDRSSLSLVSVSGVLYAVGGFAMFPKEDSDDLMPLEMNDIWRYDESERTWSGILRENRYASGATVLGVRLNTLRLTKM | null | null | muscle structure development [GO:0061061]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; skeletal muscle fiber development [GO:0048741]; skeletal muscle fiber differentiation [GO:0098528]; swimming [GO:0036268] | A band [GO:0031672]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; I band [GO:0031674] | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | KLHL40 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}. | null | null | null | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (By similarity). Required for skeletal muscle development (PubMed:23746549). {ECO:0000250|UniProtKB:Q9D783, ECO:0000269|PubMed:23746549}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QJ73 | CXR32_DANRE | MDNSTTAAEVSAPTDYDYNSTSYDDDNPYAAPCSLTETWNFLGRFAPVAYILVFILALVGNILVLCVIRRYRQSRHSPCSFSLTDTFLLHLAVSDLLLAATLPFFAVEWISEWVFGKVMCKITGALFSLNVYCGVLFLACISFDRYLAIVHAINISWRRKTCHAQLACAFIWVICLGLSMVDMHFRDLVEIPGMNRMVCQIVYSEQYSKQWQIGMQLVSMVLGFILPLLVMLYCYLHIFKALCHATRRQKRRSLRLIISLVIVFVISWAPYNALRMTDSLQMLGVIVKSCALNNVLDVGILVTESLGLAHCALNPLLYGLVGVKFRRELAQMCKAALGPQGCLGLVGWANGRGSSTRRPTGSFSSVETENTSYFSVMA | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemokine-mediated signaling pathway [GO:0070098]; immune response [GO:0006955]; innate immune response [GO:0045087]; leukocyte migration involved in immune response [GO:0002522]; macrophage activation involved in immune response [GO:0002281]; macrophage chemotaxis [GO:0048246]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; response to bacterium [GO:0009617] | external side of plasma membrane [GO:0009897] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25573892}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor for the C-X-C chemokines cxcl11.1 and cxcl11.6 (PubMed:25573892). Promotes macrophage chemotaxis to sites of bacterial infection (PubMed:20424185, PubMed:25573892). {ECO:0000269|PubMed:20424185, ECO:0000269|PubMed:25573892}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
E9QY26 | CP51B_ASPFU | MGLIAFILDGICKHCSTQSTWVLVGIGLLSILAVSVIINVLQQLLFKNPHEPPVVFHWFPFIGSTISYGIDPYKFFFDCRAKYGDIFTFILLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKFVKYGLTSDALRSYVPLITDEVESFVKNSPAFQGHKGVFDVCKTIAEITIYTASRSLQGKEVRSKFDSTFAELYHNLDMGFAPINFMLPWAPLPHNRKRDAAQRKLTETYMEIIKARRQAGSKKDSEDMVWNLMSCVYKNGTPVPDEEIAHMMIALLMAGQHSSSSTASWIVLRLATRPDIMEELYQEQIRVLGSDLPPLTYDNLQKLDLHAKVIKETLRLHAPIHSIIRAVKNPMAVDGTSYVIPTSHNVLSSPGVTARSEEHFPNPLEWNPHRWDENIAASAEDDEKVDYGYGLVSKGTNSPYLPFGAGRHRCIGEQFAYLQLGTITAVLVRLFRFRNLPGVDGIPDTDYSSLFSKPLGRSFVEFEKRESATKA | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:26269599}; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; ergosterol biosynthetic process [GO:0006696]; methylation [GO:0032259] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:28461309, ECO:0000269|PubMed:29439966}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:28461309, ECO:0000269|PubMed:29439966}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, 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:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, 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:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:29439966}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:29439966}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, 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:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:29439966}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:29439966}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, 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:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, 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:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000305|PubMed:26269599}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000305|PubMed:26269599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000305|PubMed:26269599}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 uM for eburicol {ECO:0000269|PubMed:26269599}; KM=3.78 uM for obtusifoliol {ECO:0000269|PubMed:26269599}; | PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:28461309}. | null | null | FUNCTION: Sterol 14alpha-demethylase, encoded by cyp51A and cyp51B, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:18191972, PubMed:26269599, PubMed:26459890, PubMed:29439966, PubMed:9184358). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (PubMed:18191972, PubMed:26459890, PubMed:29439966). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (PubMed:18191972, PubMed:26269599, PubMed:26459890, PubMed:28461309, PubMed:29439966). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10614, ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:26459890, ECO:0000269|PubMed:28461309, ECO:0000269|PubMed:29439966, ECO:0000269|PubMed:9184358}.; FUNCTION: As a target of azole drugs, plays a crucial role in azole susceptibility. {ECO:0000269|PubMed:12543662, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:28461309, ECO:0000269|PubMed:29894182}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9QYP0 | SIDA_ASPFU | MESVERKSESSYLGMRNMQPEQRLSLDPPRLRSTPQDELHDLLCVGFGPASLAIAIALHDALDPRLNKSASNIHAQPKICFLERQKQFAWHSGMLVPGSKMQISFIKDLATLRDPRSSFTFLNYLHQKGRLIHFTNLSTFLPARLEFEDYMRWCAQQFSDVVAYGEEVVEVIPGKSDPSSSVVDFFTVRSRNVETGEISARRTRKVVIAIGGTAKMPSGLPQDPRIIHSSKYCTTLPALLKDKSKPYNIAVLGSGQSAAEIFHDLQKRYPNSRTTLIMRDSAMRPSDDSPFVNEIFNPERVDKFYSQSAAERQRSLLADKATNYSVVRLELIEEIYNDMYLQRVKNPDETQWQHRILPERKITRVEHHGPQSRMRIHLKSSKPESEGAANDVKETLEVDALMVATGYNRNAHERLLSKVQHLRPTGQDQWKPHRDYRVEMDPSKVSSEAGIWLQGCNERTHGLSDSLLSVLAVRGGEMVQSIFGEQLERAAVQGHQLRAML | 1.14.13.196 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22928747}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22928747}; | cellular response to iron ion starvation [GO:0010106]; ergosterol biosynthetic process [GO:0006696]; ferrichrome biosynthetic process [GO:0031169]; intracellular iron ion homeostasis [GO:0006879]; secondary metabolite biosynthetic process [GO:0044550]; siderophore biosynthetic process [GO:0019290]; siderophore-dependent iron import into cell [GO:0033214] | null | iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP+ binding [GO:0070401]; ornithine N5-monooxygenase activity [GO:0031172] | PF13434; | 3.50.50.60; | Lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78275; EC=1.14.13.196; Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894}; CATALYTIC ACTIVITY: Reaction=L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+); Xref=Rhea:RHEA:41512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:46911, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78275; EC=1.14.13.196; Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 mM for L-ornithine (in the presence of 1 mM NADH) {ECO:0000269|PubMed:20614882}; KM=1.7 mM for L-ornithine (in the presence of 1 mM NADPH) {ECO:0000269|PubMed:20614882}; KM=0.49 mM for L-ornithine (at 37 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=0.58 mM for L-ornithine (at 25 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=0.94 mM for NADPH (in the presence of 15 mM L-ornithine) {ECO:0000269|PubMed:20614882}; KM=0.9 mM for NADH (in the presence of 15 mM L-ornithine) {ECO:0000269|PubMed:20614882}; KM=4.6 uM for NADPH (at 37 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=2.6 uM for NADPH (at 25 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=18 uM for O(2) (at 37 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=16 uM for O(2) (at 25 degrees Celsius) {ECO:0000269|PubMed:20650894}; Note=kcat is 29 min(-1) with L-ornithine as substrate and 75 min(-1) with NADPH as substrate. {ECO:0000269|PubMed:20614882}; | PATHWAY: Siderophore biosynthesis; ferrichrome biosynthesis. {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:16113265, ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22465572}. | null | null | FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:15504822, PubMed:16113265, PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265, PubMed:20614882, PubMed:20650894, PubMed:22465572). SidA is highly specific for its substrate, only hydrolyzing l-ornithine, and has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate (PubMed:20614882, PubMed:22465572). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265). {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:16113265, ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:21622789, ECO:0000269|PubMed:22106303, ECO:0000269|PubMed:22465572}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9R5S0 | RHBA_ASPFU | MPAAPKQRKIAIVGSRSVGKSSLTVRFVEHHFVESYYPTIENTFSRIIKYNGQDFATEIVDTAGQDEYSILNSKHFIGIHGYIIVYSVASRQSFDMVRVIRDKILNHLGADHVPLVVVGNKSDLKSEQRQVSLDEGRQLGEEFQCAFTEASARLDYNVTKAFDLMIGEIEKSQNPSQPAGGSKCILM | 3.6.5.- | null | asexual sporulation resulting in formation of a cellular spore [GO:0043936]; cellular response to nitrogen starvation [GO:0006995]; negative regulation of asexual sporulation resulting in formation of a cellular spore [GO:0043944]; small GTPase-mediated signal transduction [GO:0007264] | plasma membrane [GO:0005886] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rheb family | PTM: Farnesylation is important for efficiently activating mTORC1-mediated signaling. {ECO:0000250|UniProtKB:Q15382}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q15382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q15382}; | null | null | null | null | FUNCTION: Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12135576, PubMed:12704156). Plays a role in virulence (PubMed:11446528, PubMed:12704156, PubMed:16205968). {ECO:0000269|PubMed:11446528, ECO:0000269|PubMed:12135576, ECO:0000269|PubMed:12704156, ECO:0000269|PubMed:16205968}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9RAH5 | GLIT_ASPFU | MSIGKLLSNGALLVDVLIIGAGPAGLSTATGLARQLHTAVVFDSGVYRNAKTQHMHNVLGWDHRNPAELRAAGRADLTTRYSTIQFQNSTIEAIRQVETNQLFEARDNEGHSWYGRKVVLATGVRDIPLDIEGYSECWANGIYHCLFCDGYEERGQETVGVLALGPIANPARALHLARMALRLSESVTIYTNGNEQLAKEIQQAAEESPVGASGLKFEARPIRRFEKGDVAKTVIVHLGESESKTEGFLVYNPQTEVNGPFAKQLALNMTEGGDILTTPPFYETSVPGVFAVGDCATPLKAVTPAVSMGSLAAGGLVAQLQAQALPEFRLDQEL | 1.8.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24446392}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:24446392}; | cell redox homeostasis [GO:0045454]; cellular response to mycotoxin [GO:0036146]; gliotoxin biosynthetic process [GO:2001310]; mycotoxin biosynthetic process [GO:0043386] | null | flavin adenine dinucleotide binding [GO:0050660]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791] | PF07992; | 3.50.50.60; | Class-II pyridine nucleotide-disulfide oxidoreductase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20548963}. | null | null | FUNCTION: Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:23434416, PubMed:24039048). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). GliT is required for self-protection against gliotoxin (PubMed:20548963, PubMed:26150413). GliT plays a role in preventing dysregulation of the methyl/methionine cycle to control intracellular S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) homeostasis during gliotoxin biosynthesis and exposure (PubMed:26150413). {ECO:0000269|PubMed:17154540, ECO:0000269|PubMed:20548963, ECO:0000269|PubMed:21513890, ECO:0000269|PubMed:21612254, ECO:0000269|PubMed:21749092, ECO:0000269|PubMed:22903976, ECO:0000269|PubMed:22936680, ECO:0000269|PubMed:23434416, ECO:0000269|PubMed:24039048, ECO:0000269|PubMed:25062268, ECO:0000269|PubMed:26150413}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9RBG1 | ABCC_ASPFU | MSLLGTINPNINPERTVAGRGTQEEEGEIARVEHNHHNNAASVSTDETVLERSKEIGDEDVAVEEVTRLARQLTRQSTRFSTSGNVENPFLETKEDSTLNPLSPNFKAKNWMKNLLALSSRDPERYPKRVAGVAFKNLSVHGYGSPTDYQKDVFNSVLEVGTLVRRIMGTGKQKIQILRDFDGLVKSGEMLVVLGRPGSGCSTFLKTISGEMNGIYMDEKSYLNYQGISSKQMRKQFRGEAIYTAETDVHFPQLTVGDTLKFAALARAPRNRLPGVSREQYAVHMRDVVMAMLGLTHTMNTRVGNDFVRGVSGGERKRVSIAEATLSGSPLQCWDNSTRGLDSANALEFCKTLNLMTKYAGATVAVAIYQASQSAYDVFDKVTVLYEGRQIYFGRTDEAKEFFTNMGFECPERQTTADFLTSLTSPAERVVKPGFEGKVPQTPDEFVRAWKSSEAYAKLMREIEEYDREFPIGGESLNQFIESRRAMQAKNQRVKSPYTISVWQQIELCMIRGFQRLKGDSSLTMSQLIGNFIMALVIGSVFYNLPDDTSSFYARGALLFFAVLLNAFSSALEILTLYAQRPIVEKQARYAMYHPFAEAIASMLCDMPYKITNAIIFNLTLYFMTNLRREPGAFFVFLLFSFVTTLTMSMLFRTMAASSRTLSQALVPAAILILGLVIYTGFTIPTRNMLGWSRWMNYIDPIAYGFESLMVNEFHNRQFLCPDSAFVPSSGAYDSQPLAYRVCSTVGSVSGSRYVQGDDYLNQSFQYYKSHQWRNLGIMFGFMFFFMFTYLTATEYISESKSKGEVLLFRRGHAQPTGSHDVEKSPEVSSAAKTDEASSKEATGAIQRQEAIFQWKDVCYDIKIKGEPRRILDHVDGWVKPGTCTALMGVSGAGKTTLLDVLATRVTMGVVSGEMLVDGRPRDQSFQRKTGYVQQQDLHLHTTTVREALRFSALLRQPAHVPRQEKIDYVEEVIKLLGMESYADAVVGVPGEGLNVEQRKRLTIGVELAAKPQLLLFLDEPTSGLDSQTSWSILDLIDTLTKHGQAILCTIHQPSAMLFQRFDRLLFLAKGGKTVYFGEIGEKSSTLASYFERNGAPKLPPDANPAEWMLEVIGAAPGSHSDIDWPAVWRDSPERRAVHEHLDELKRTLSQKPIDPSKADPGSYDEFAAPFTIQLWECLLRVFSQYWRTPVYIYSKTALCVLTALYIGFSFFNAQNSAQGLQNQMFSIFMLMTIFGNLVQQIMPNFCTQRSLYEVRERPSKTYSWKAFMAANIIVELPWNTLMAFLIFVCWYYPIGLYRNAEPTDSVHERGALMFLLIWSFLLFTSTFAHMMIAGIELAETGGNLANLLFSLCLIFCGVLAPPQSLPGFWIFMYRVSPFTYLVSAMLSTGVSGTNAVCEPVEFLHFDPPSNMTCKDYMADYISTRGGYLENPSATSDCTFCTISSTDTFLSAVSSHYSDAWRNFGIMWAYIIFNIFAAVFIYWLARVPKGKRTKGST | null | null | xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF19055;PF00005;PF14510;PF06422; | 3.40.50.300; | ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24123268}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46081, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:32209680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917; Evidence={ECO:0000269|PubMed:32209680}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out) + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504; Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate + voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913; Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680}; | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), tebuconazole (TEBZ), and voriconazole (VRC) (Probable) (PubMed:22509997, PubMed:23580559, PubMed:24123268, PubMed:28264842, PubMed:32209680). Is also able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters (PubMed:32209680). Required for normal pathogenesis in a Galleria mellonella (greater wax moth) infection model (PubMed:24123268). {ECO:0000269|PubMed:22509997, ECO:0000269|PubMed:23580559, ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:28264842, ECO:0000269|PubMed:32209680, ECO:0000305|PubMed:16622700}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9RBR0 | ABR2_ASPFU | MWYQSASLLGVAAVAQAATVHYSLDLTWETGSPNGVSREMIFVNGQFPGPAIILNEGDEAIIDVTNHLPFNTSIHFHGIEQKNTPWADGVVGLSQWAIQPGQSYTYQWRADTYGTYWYHAHDKAEIMDGLYGPVHIRPRPNRDSPFSMISDDPADIRAMKQAERNGKLVMLSDWDHLTGQEYMKAMEETGYDIFCSDSVLINGRGSVFCHDPEELTQMVPPPELAILNSSLTDKGCLPFVPPIQGNWEHHPDKVPPGLNEGCHPSTTQETIFTVDAAHQWASFHFISAASLKVLVVSIDEHPMYVYEVDGRYIEPQLAHSVKLYNGERYSVMVKLDKEPANYKMRAANDGGNQIVSGFATVTYEGGETSQRPSQPYIDYGSRNTSADVIPLDTNHLPPYPAISPASEPDDFHILMLGRTNSSWEWSLDGAAFLPSNLAALPPAILSPQAPEFADALKITTRNDTWVDIVFQLVVSETTPIQPPHPLHKHSNKGFLLGTGHGKFNWTSIKEAKEASPESFLETPVYRDTFTTSPQGETWTAIRYHVENPGPFLLHCHMTTHLQSGMGLILMDGVDVWPEVYADMITPM | 1.10.3.- | null | melanin biosynthetic process [GO:0042438]; pigment biosynthetic process [GO:0046148] | cell surface [GO:0009986] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:26972005}. | null | null | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203}. | null | null | FUNCTION: Laccase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21573171, PubMed:21747802, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622). {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078, ECO:0000269|PubMed:21573171, ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666, ECO:0000269|PubMed:25684622, ECO:0000269|PubMed:26972005}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
E9RCK4 | VEA_ASPFU | MATRPPLMPPANETESSVSRISREGKKITYKLSVMQQPERARACGAGAKSSADRRPVDPPPVVELRIFESDPNDDLHKTDITFAYNANFFLFATLETARPMAQGRLTGPPTCPVLTGVPVAGVAYLDRPQQAGYFIFPDLSVRHEGRYRLSFHLYEEIKDIKDADKDTPMPDLNSSTNLTKPSAPKAHLNFRLEVKSVPFTVYSAKKFPGLATSTSLSRIIAEQGCRVRIRRDVRMRRRGEKRTDDYDFDDERAFATRSDRYTTPDMYAANSAERARSTSISTTADTSFPYGSDAQRRPSAGDYGFQGAQPYQRSMPAASAAPAPAPVHSPATSAQTSSYQSHLSFGATQSQYPAPQLPPTPQSATPTNTYSPHPSYSHSRNPSNGTEYDATSSGYPYPQPRLPADRPSYSKAALPPLRLEPPKAPNMQTSTDSRSSDANAYPTLSQPPVPRAPTPANHVTSLPPLKVLSGEYSHPSQPNAQSPHHDLGSGKRLLWETNHTLSKRSHEETFGSDERPLHNGMRPDMDQYPSMGRKQPDYGRLPFYTDSRDEMAYKRANGRMVMKILPALP | null | null | asexual sporulation resulting in formation of a cellular spore [GO:0043936]; conidiophore development [GO:0070787]; negative regulation of conidiophore development [GO:0070794]; negative regulation of sexual sporulation resulting in formation of a cellular spore [GO:0043942]; positive regulation of asexual sporulation resulting in formation of a cellular spore [GO:0043945]; positive regulation of gliotoxin biosynthetic process [GO:1900691]; spore germination [GO:0009847] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF11754; | 2.60.40.3960; | Velvet family, VeA subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTV4}. Cytoplasm {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}. | null | null | null | null | null | FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex hat acts as a global regulator for secondary metabolite gene expression (By similarity). Controls the expression of hundreds of genes, including those comprising more than a dozen known secondary metabolite gene clusters (PubMed:24116213). Controls the expression of the gliotoxin gene cluster (PubMed:23087369). Controls the expression of the fumagillin, fumitremorgin G, fumigaclavine C and glionitrin gene clusters (PubMed:24116213). The regulation of the fumagillin gene cluster and fumagillin production is performed through direct control of the expression of fumR (PubMed:24116213). Negatively regulates conidiation (PubMed:22970834, PubMed:23087369). Required for normal protease activity (PubMed:23087369). {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:22970834, ECO:0000269|PubMed:23087369, ECO:0000269|PubMed:24116213}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
F0JAI6 | KEBAB_DROME | MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERSLYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKENQELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKGIKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQLQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKIEKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCIEAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP | null | null | null | kinetochore [GO:0000776]; perinuclear region of cytoplasm [GO:0048471]; spindle microtubule [GO:0005876] | kinetochore binding [GO:0043515]; microtubule binding [GO:0008017] | null | 1.10.418.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21912673}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21912673}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21912673}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21912673}. Note=During metaphase expressed in the kinetochores. During anaphase expression in the kinetochores progressively increases, and at late anaphase it is also expressed in the microtubules, specifically in the central spindle and centrosomal region. During telophase expression increases in the microtubules, and it is associated with residual spindle microtubules between chromosomes that have separated. At interphase it is expressed in the cytoplasm particularly around the nucleus. {ECO:0000269|PubMed:21912673}. | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
F0NDL2 | HELS_SULIR | MSLELEWMSIDDLKLPSNVIDIIKNRGIKKLNPPQTEAVKKGLLDGNRLLLTSPTGSGKTLIAEMGIISFLLKNGGKAIYVTPLRALTNEKYLTFKDWESIGFKVAMTSGDYDTDDAWLKNYDIIITTYEKLDSLWRHRPDWLNEANYFVLDELHYLNDPERGPVVESVTIRAKRRNLLALSATISNYKQIAKWLGAEPVATNWRPVPLMEGVMYPERKKKEYTILFRDNTTRKVHGDDAIIAYTLDSLSKNGQVLVFRNSRKMAESTALKIANYMNFVSLDEKAISEILNQLDDIEEGGSDEKELLKSLISKGVAYHHAGLSKALRDIIEESFRKRKIKVIVATPTLAAGVNLPARTVIIGDIYRFNRKIVGYYDEIPVMEYKQMSGRAGRPGFDQIGESIIVVRDKEDVDRVFKKYILSDVEPIESKLGSERAFYTFLLGILSAEGSLSEKQLEGFAYESLLAKSLVDVYFDRAIRWLSEHSFIREENNTFTLTNFGKRVADLYINPFTADIIRKGLEGHKASCEIAYLHLLAFTPDGPLVSVGRNEEEELIELLEDLECELLVEEPYEEDEYSLYLNALKVALIMKDWIDEVDEDTILGKYNIGSGDLRNIVETMDWLTYSAYHLSKELRLDDHSDKLRILNLRVTDGVKEELLELVQIGGVGRKRARLLYNNGIKGLGDVVMNPDRVRNLLGQKLGERVVQEAARLLNRFH | 5.6.2.3; 5.6.2.4 | null | DNA repair [GO:0006281] | null | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853] | PF00270;PF00271;PF21280; | 1.10.3380.30;1.10.150.20;3.40.50.300; | Helicase family, Hel308 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:29846688}; 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=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:29846688}; CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.; EC=5.6.2.3; Evidence={ECO:0000269|PubMed:29846688}; 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=5.6.2.3; Evidence={ECO:0000269|PubMed:29846688}; | null | null | null | null | FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:29846688}.; FUNCTION: Has predominantly 3'-5' helicase activity but also a weak 5'-3' helicase activity (PubMed:29846688). Has the ability to unwind replication forks, preferentially removing the lagging strand (PubMed:29846688). Hjc, Hjm (Hel308) and branch migration ATPase PINA coordinate HJ migration and cleavage of replication forks in a coordinated way (PubMed:29846688). {ECO:0000269|PubMed:29846688}. | Sulfolobus islandicus (strain REY15A) |
F0NHH1 | ALBA1_SULIR | MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK | 3.1.-.- | null | chromosome condensation [GO:0030261] | chromosome [GO:0005694]; cytoplasm [GO:0005737] | double-stranded DNA binding [GO:0003690]; nuclease activity [GO:0004518]; RNA binding [GO:0003723] | PF01918; | 3.30.110.20; | Histone-like Alba family | PTM: Acetylated (PubMed:29679495). Acetylation at Lys-16 by the Pat acetylase decreases DNA-binding affinity (By similarity). Deacetylation at Lys-16 by the CobB deacetylase increases DNA-binding affinity (By similarity). Acetylation at Ser-2 is involved in the regulation of the turnover of the protein (PubMed:29679495). {ECO:0000250|UniProtKB:P60849, ECO:0000269|PubMed:29679495}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01122}. Chromosome {ECO:0000255|HAMAP-Rule:MF_01122}. | null | null | null | null | null | FUNCTION: Binds double-stranded DNA tightly but without sequence specificity (By similarity). Involved in DNA compaction (By similarity). Possesses DNA endonuclease activity (By similarity). Prevents transcription after DNA binding (By similarity). Binds single-stranded DNA and RNA in vitro (By similarity). Binds rRNA and mRNA in vivo (By similarity). May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). Binds double-stranded RNA (dsRNA) and exhibits RNA chaperone activity (PubMed:32761152). Required for normal growth (PubMed:32761152). {ECO:0000250|UniProtKB:P60848, ECO:0000250|UniProtKB:P60849, ECO:0000269|PubMed:32761152}. | Sulfolobus islandicus (strain REY15A) |
F0NID4 | PINA_SULIR | MNDLMLDKSALLFGVSKYLEKGIITGNVLIHKSLLAELERESNDGLVSAEIALDEVKKLKDITERILVNFEIVGDDSKKGEANELSREYCLEKGCIIVTADETQKKICDAMGIQYNFLQPLKQGLSFESFFDDETMSLHIKEDTVPRAKKGKPGNWKFVNLSDKPMLSTDVRMIANEIINAVRLIKGSFVEIERRGSLIIQLGNYRVVITRPPLSDGWEITITRPVVRKRLEDYNLDERLIKRLEERAEGIIIAGAPGMGKTTFAQALAEYYMRLGKIVKTIESPRDMHLPPEITQYSKNYAEIGELHDILLLSRPDYTVYDEMRNDEDFKLYVDLRLAGVGMVGVVHATSPIDAIHRFVNRVDIGTIPNILDTIIFINSGNVSKVYTLEMTVKVPAGLKEADLARPVVEIKDLATGNTEYEIYVFGEQTMIVPVNRGITMSNMEFKISKIVNNIIPNATVKYEDGEYVIVIPKEEIGKYNRKLVQRLKRLEKKNNIKIKIKLSD | 3.6.4.12 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28238763}; Note=Ca(2+) stimulates ATPase activity more than Mn(2+) or Mg(2+). {ECO:0000269|PubMed:28238763}; | DNA recombination [GO:0006310]; DNA repair [GO:0006281] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; four-way junction helicase activity [GO:0009378]; hydrolase activity [GO:0016787] | PF00437; | 3.40.50.1010;3.40.50.300; | null | null | null | 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; Evidence={ECO:0000269|PubMed:28238763}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for ATPase activity. {ECO:0000269|PubMed:28238763}; | null | FUNCTION: Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner (PubMed:28238763). Stimulates cleavage by HJ resolvase Hjc (PubMed:28238763). Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way (PubMed:29846688). Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA (PubMed:29846688). Probably acts as an ATP-dependent pump that pulls DNA through the hexamer (By similarity). {ECO:0000250|UniProtKB:Q5M2B1, ECO:0000269|PubMed:28238763, ECO:0000269|PubMed:29846688}. | Sulfolobus islandicus (strain REY15A) |
F0T4D1 | KDTA_CHLP6 | MIKGRRTKLHTFLYDCFLIFAFMVGLPRILYKRFVHGKYTKSLGIRFGFKKPEVPGTGPVAWFHGASVGETALLLPLLKRFMKEYPEWRCVVTSCTESGHENAHRLFGPLGVTTFILPLDLSIIIKPVVRAISPSLLVFSEGDCWLNFIEEAKRLGATAVIINGKLSANSCKRFTILKRFGRNYFSPVDGFLLQDEQHKARFLQLGVDKEKIQVTGNIKTYTETLSENNQRDYWREKLQLAQDTELLVLGSVHPKDVEVWLPVVRELRRNLKVLWVPRHIERSKELEALLSKENISYGLWSKEATFAQHDAIIVDAIGWLKQLYSAADLAFVGGTFDDRIGGHNLLEPLQCGVPLIFGPHIQSQSDLAERLLSMGAGCCLDKTNIVKVITFLLDHPEERAAYIQKGAMFLHEEKVAFDRTWESFKRYIPCVKI | 2.4.99.12; 2.4.99.13; 2.4.99.14; 2.4.99.15 | null | lipid A biosynthetic process [GO:0009245]; lipopolysaccharide core region biosynthetic process [GO:0009244] | plasma membrane [GO:0005886] | Kdo transferase activity [GO:0043842] | PF04413; | 3.40.50.11720;3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 30 subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029}; CATALYTIC ACTIVITY: Reaction=alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28062, ChEBI:CHEBI:15378, ChEBI:CHEBI:60364, ChEBI:CHEBI:60365, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.13; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029}; CATALYTIC ACTIVITY: Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28154, ChEBI:CHEBI:15378, ChEBI:CHEBI:60365, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987, ChEBI:CHEBI:86234; EC=2.4.99.14; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029}; CATALYTIC ACTIVITY: Reaction=alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28158, ChEBI:CHEBI:15378, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987, ChEBI:CHEBI:86234, ChEBI:CHEBI:86236; EC=2.4.99.15; Evidence={ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7744029}; | null | PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. | null | null | FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of predominantly four 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo. {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:7523826, ECO:0000269|PubMed:7744029}. | Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci) |
F1C7I4 | MDHC_TAESO | MPGPLRVLITGAAGQIAYNLSNMVANGNLFGKDQKIILHLLDIPEAKTVLEGVVMELQDCAFTVLEGIVPTHCLKEAFTDIDVALMVGAMPRKQGMERRDLLSSNVKIFKDQGEALEKYAKKTVKVLVVGNPANTNCLIMSKYAPSIPKENFTALSRLDHNRAIYQVAAKVGVPSECVKNVCIWGNHSNKQFPDLAHAVVTKGGKQHPAKELINDEKWVKEVFTPCVQNRGAAVIGLRKLSSAASAAKAIVDQMHDWWFGTKEGEWVSMSVYSTGEHYGAPKDIYFSFPVTIKNGHYKVVDGLAMDEWGKGLFKITADELVDEREVALSSFK | 1.1.1.37 | null | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | L-malate dehydrogenase activity [GO:0030060]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19277715}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for L-malate (at pH 9.6) {ECO:0000269|PubMed:21439955}; KM=42 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:21439955}; KM=44 uM for oxaloacetate (at pH 8) {ECO:0000269|PubMed:21439955}; KM=167 uM for NADH (at pH 8) {ECO:0000269|PubMed:21439955}; KM=215 uM for L-malate (at pH 9.6) {ECO:0000269|PubMed:19277715}; KM=50 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:19277715}; KM=2.4 uM for oxaloacetate (at pH 7.6) {ECO:0000269|PubMed:19277715}; KM=48 uM for NADH (at pH 7.6) {ECO:0000269|PubMed:19277715}; Vmax=77.03 umol/min/mg enzyme toward L-malate (at pH 9.6) {ECO:0000269|PubMed:21439955}; Vmax=79.12 umol/min/mg enzyme toward NAD (at pH 9.6) {ECO:0000269|PubMed:21439955}; Vmax=450.3 umol/min/mg enzyme toward oxaloacetate (at pH 8) {ECO:0000269|PubMed:21439955}; Vmax=721.4 umol/min/mg enzyme toward NADH (at pH 8) {ECO:0000269|PubMed:21439955}; Vmax=87.8 umol/min/mg enzyme toward L-malate (at pH 9.6) {ECO:0000269|PubMed:19277715}; Vmax=104 umol/min/mg enzyme toward NAD (at pH 9.6) {ECO:0000269|PubMed:19277715}; Vmax=1490 umol/min/mg enzyme toward oxaloacetate (at pH 7.6) {ECO:0000269|PubMed:19277715}; Vmax=1714 umol/min/mg enzyme toward NADH (at pH 7.6) {ECO:0000269|PubMed:19277715}; Note=kcat is 47.4 sec(-1) for L-malate. kcat is 385.6 sec(-1) for NAD. kcat is 665.34 sec(-1) for oxaloacetate. kcat is 962.66 sec(-1) for NADH. {ECO:0000269|PubMed:21439955}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6 for oxaloacetate reduction and 9.6 for malate oxidation (PubMed:19277715, PubMed:21439955). Stable between pH 6.8-8.5 for the forward reaction (PubMed:19277715). {ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Has highest activity between 5-40 degrees Celsius. No activity at 60 degrees Celsius. {ECO:0000269|PubMed:21439955}; | FUNCTION: Malate dehydrogenase. Has no activity with NADPH as substrate. Does not show lactate dehydrogenase activity. {ECO:0000269|PubMed:21439955}. | Taenia solium (Pork tapeworm) |
F1CKI6 | 3CAR1_PICSI | MSVISIVPLASKPCLYKSFISSTHEPKALRRPISTVGLCRRAKSVTASMSMSSSTALSDDGVQRRIGNHHSNLWDDNFIQSLSSPYGASSYAERAERLIGEVKEIFNRISMANGELVSHVDDLLQHLSMVDNVERLGIDRHFQTEIKVSLDYVYSYWSEKGIGPGRDIVCADLNTTALGFRLLRLHGYTMFPDVFEQFKDQMGRIACSTNQTERQISSILNLFRASLIAFPWEKVMEEAEIFSTAYLKEALQTIPVSSLSREIQYVLDYRWHSDLPRLETRTYIDILRENATNETLDMKTEKLLELAKVEFNIFNSLQQNELKCVSRWWKESGSPDLTFIRHRQVEFYTLVSGIDMEPKRSTFRINFVKICHFVTILDDMYDTFGTIDELRLFTAAVKRWDKSATECLPEYMKGVYIDLYETVNELAREAYKSQGRDTLNYARQALEDYLGSYLKEAEWISTGYIPTFEEYLVNGKVSSAHRIATLQPILMLDVPFPPHVLQEIDFPSKFNDLAGSILRLRGDTRCYQNDRARGEEASCISCYMKDNPGSTEEDALNHINGMIEKQIKELNWELLKPDKNVPISSKKHAFNISRGLHHFYKYRDGYTVANSETRNLVIKTVLEPVPM | 4.2.3.107 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | gibberellin biosynthetic process [GO:0009686]; green leaf volatile biosynthetic process [GO:0010597]; monoterpene biosynthetic process [GO:0043693]; monoterpenoid biosynthetic process [GO:0016099]; response to jasmonic acid [GO:0009753] | chloroplast [GO:0009507] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (+)-car-3-ene + diphosphate; Xref=Rhea:RHEA:32539, ChEBI:CHEBI:7, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.107; Evidence={ECO:0000269|PubMed:21323772}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.88 uM for geranyl diphosphate {ECO:0000269|PubMed:21323772}; Vmax=32.1 pmol/sec/ug enzyme with geranyl diphosphate as substrate {ECO:0000269|PubMed:21323772}; Note=kcat is 2.21 sec(-1) with geranyl diphosphate as substrate. {ECO:0000269|PubMed:21323772}; | PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21323772}. | null | null | FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores (e.g. insect attack by white pine weevil P.strobi) and pathogens (PubMed:21323772, PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-car-3-ene (PubMed:21323772, PubMed:21385377). {ECO:0000269|PubMed:21323772, ECO:0000269|PubMed:21385377}. | Picea sitchensis (Sitka spruce) (Pinus sitchensis) |
F1CMX0 | KSHA1_RHORH | MSLGTSEQSEIREIVAGSAPARFARGWHCLGLAKDFKDGKPHSVHAFGTKLVVWADSNDEIRILDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGNGRCKNIPYARRVPPIAKTRAWHTLDQDGLLFVWHDPQGNPPPADVTIPRIAGATSDEWTDWVWYTTEVDTNCREIIDNIVDMAHFFYVHYSFPVYFKNVFEGHVASQFMRGQAREDTRPHANGQPKMIGSRSDASYFGPSFMIDDLVYEYEGYDVESVLINCHYPVSQDKFVLMYGMIVKKSDRLEGEKALQTAQQFGNFIAKGFEQDIEIWRNKTRIDNPLLCEEDGPVYQLRRWYEQFYVDVEDVAPEMTDRFEFEMDTTRPVAAWMKEVEANIARKAALDTETRSAPEQSTTAG | 1.14.15.30 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:25049233}; Note=Binds 1 Fe cation. {ECO:0000269|PubMed:25049233}; | cholesterol metabolic process [GO:0008203]; lipid catabolic process [GO:0016042] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; iron ion binding [GO:0005506] | PF19298;PF00355; | 2.102.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641; EC=1.14.15.30; Evidence={ECO:0000269|PubMed:25049233, ECO:0000305|PubMed:21642460}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=2 uM for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=2.2 uM for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=50 uM for ADD as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=110 uM for testosterone as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=400 uM for AD as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; Note=kcat is 2.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.4 sec(-1) for testosterone as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.3 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.1 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.9 sec(-1) for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.5 sec(-1) for AD as substrate (at pH 7.0 and 22 degrees Celsius). {ECO:0000269|PubMed:25049233}; | null | null | null | FUNCTION: May be involved in the degradation of cholic acid, a steroid acid found predominantly in the bile (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 23,24-bisnorcholesta-4-ene-22-oate, 3-oxo-23,24-bisnorcholaesta-1,4-dien-22-oate (1,4-BNC), 23,24-bisnorcholesta-1,4-diene-22-oate and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21642460, PubMed:25049233). KshA1 has the highest specificity for steroids possessing an isopropionyl side chain at C17 (PubMed:25049233). {ECO:0000269|PubMed:21642460, ECO:0000269|PubMed:25049233}. | Rhodococcus rhodochrous |
F1CMY8 | KSHA5_RHORH | MSIDTARSGSDDDVEIREIQAAAAPTRFARGWHCLGLLRDFQDGKPHSIEAFGTKLVVFADSKGQLNVLDAYCRHMGGDLSRGEVKGDSIACPFHDWRWNGKGKCTDIPYARRVPPIAKTRAWTTLERNGQLYVWNDPQGNPPPEDVTIPEIAGYGTDEWTDWSWKSLRIKGSHCREIVDNVVDMAHFFYIHYSFPRYFKNVFEGHTATQYMHSTGREDVISGTNYDDPNAELRSEATYFGPSYMIDWLESDANGQTIETILINCHYPVSNNEFVLQYGAIVKKLPGVSDEIAAGMAEQFAEGVQLGFEQDVEIWKNKAPIDNPLLSEEDGPVYQLRRWYQQFYVDVEDITEDMTKRFEFEIDTTRAVASWQKEVAENLAKQAEGSTATP | 1.14.15.30 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:25049233}; Note=Binds 1 Fe cation. {ECO:0000269|PubMed:25049233}; | cholesterol catabolic process [GO:0006707] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; iron ion binding [GO:0005506] | PF19298;PF00355; | 2.102.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641; EC=1.14.15.30; Evidence={ECO:0000269|PubMed:25049233, ECO:0000305|PubMed:21642460}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=0.5 uM for testosterone as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=0.8 uM for AD as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=1.2 uM for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=6.1 uM for 5alpha-androstan-3,17-dione as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=500 uM for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; Note=kcat is 1.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.8 sec(-1) for 5alpha-androstan-3,17-dione, AD and testosterone as substrates (at pH 7.0 and 22 degrees Celsius). kcat is 0.7 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.5 sec(-1) for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). {ECO:0000269|PubMed:25049233}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:25049233}. | null | null | FUNCTION: Probably involved in the degradation of cholesterol (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione, 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5alpha-androstane-17beta-ol-3-one (stanolon), 11beta-hydrocortisone, 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 23,24-bisnorcholesta-4-ene-22-oate, 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21642460, PubMed:25049233). KshA5 has the broadest substrate range without a clear substrate preference and is active with Delta-4, Delta-1,4, 5alpha-H and 5beta-H steroids, as well as with steroids having bulky aliphatic side chains and an isopropionyl side chain at C17. {ECO:0000269|PubMed:21642460, ECO:0000269|PubMed:25049233}. | Rhodococcus rhodochrous |
F1DBA9 | MPAC_PENBR | MNFHKGQPKEDLRVLFGPQCPDITDSITHIRDAISKDPTGLGFLTNILDELPSLWPTIAGAWPALKNVEGESQLLALGRLFEHESEDRVEASNLMMTPITVMRHIVDFWNLQDVATHPAFPSSSLSETEMPRIVDTQGFCVGLLAAIAVACSRNTQEFQYVASNAIRLSLCVGALVDLDEILCGSTTSLAVSAERVKQEIHDHGLRTKQLSLRGRFHHEAHREGIQHIMKLCTNDSRFKLPRSDALLTPLRSSQGGEIFQQEALLHTVALDSILCAKANWYDVVSALINSTEMTVDQSHLLSIGPEEFVPRSARSRSVARRELQSYAMQGFSNESPQPSTASLSNSVQTFDSRPQAAEASPIAITGMACRYPNADTLAQLWDLLELGRCTVKSPPESRFHMSDLQREPKGPFWGHFLERPDVFDHRFFNISAREAESMDPQQRVALQVAYEAMESAGYLGWQPNGLSRDIGCYVGVGSEDYTENVASRNANAFSITGTLQSFIAGRISHHFGWSGPSISLDTACSSAAVAIHLACKALQTNDCKIALAGGVNVLTNPRVYQNLSAASFLSPSGACKPFDASADGYCRGEGAGLFVLRPLQDAIDNGDPILGVIAGSAVNQGSNNSPITVPDAEAQRSLYNKAMSLAGVSPDEVTYVEAHGTGTQVGDPIELDSLRRTFGGPQRRNSLHIGSIKGNIGHTETSSGAAGLLKTILMLQQQRIPRQANFNQLNPKVKSLTPDRLVIASESTEWASTERVAMVSNYGASGSNAALIVKEHAPIRSEQNGTAPEYIQNVPILVSARSEESLRAYCGALRATLLSHPPSETLVQKLAYNLAMKQNRDLPLNLTFSTSSDATSLSARLEAISTGASADLIQKRPSNEPPVVLCFGGQNGLTATISKEVFDASALLRTHLEDCEEVGRTLGLPSLFPTIFSSAPITNIIHLHFILFSIQYASAKAWLDSGLRVSRIVGHSFGQLTALSVAGSLSVRDGIHLVTERARLIESSWGPESGIMLAVEGTDIEVQQLLDQTGHIADVACYNGPRQQVLAGTAESIAAIENAAARTPSASKLRLTRLQNSHAFHSRLVDSIVPAIMEVAGSLVYQTPIIPIEACSASGDWSTITAAEIVEHSRMPVYFRRAVERVAEKLQAPAVWLEAGSASPIIPMVRRVLESSSVANTYHKIDLGGSSGAQNLANVTSALWAQGVHVQFWPFDRAQHGSFKWMNLPPYQFAQNSHWVDFDPAAFSSAGPSSGKQSAGQEAGLLCQLSESPDERLYHVNIQDALYRACTQGHAVLNQTLCPASMYMEMVLRAAASIFPTGNASEPAMSHIEDLTISSPLVLDPQGDVFLRLTSDGAGPTRPWLFSIFSSESNDHTSVHAEGTVCLHQERSRALARFQSMDRLLDSARSKTIEADPASNGLKGSTVYAALESVTNYGDYFRGVKKVFANGREASGLVSMMPSASETNCDPILLDNFLQVAGIHVNCLSDRRSSEVFVCNAIGETFVINSLLKQKNGASPSTWKVYTSYVRPSKTEIACDIYVMDCQTDTLSAAMMGVRFTSVSIRSLTRALAKLNNNVLETAEAQSVVEPAIPAEKSVVTATPSAPAADGGGAKDLATVQEMLCELFGVSVAEVSPSVSLVDIGVDSLMSTEVLSEIKKRFQVDMSYTTLVDIPNIQGLVEHIFPGHSHAAPSQPVVETAPVQSVAPQAVSHVPTPANNGPPLVSVARQCFDTTHAAVSHTSDAHWTGFFHTTYPKQMTLLTAYILEAFRALGSPLEASEPNEVLIPISVLPRHEQLRKHLYKILESVGLVRQMPTGELVRTTTPIPLSQSHDLHTQIRAEYPPYALEHDLLQITAPRLADCLTGKADGVSLIFQDANTRRLVGDVYAQSPVFKSGNLYLARYLLDVVQSFGSSRTIKILEIGAGTGGTTKNLLEKLSTIPGLSTRLEYTFTDISPSLVAAGRKTFANYNFMRYETLNVENDPPSALSGQYDIVLSTNCVHATRNLRESCTNIRKLLRPDGILCLVELTRDIFWLDLVFGLLEGWWRFEDGREHALATEMMWDQTLRQSGFEWVDWTNNETVESNALRVIVASPTGNSSTATMSPSKLTKMETVVWGERDNLQLRADIYYPETVDTTRKQRPIALMIHGGGHVMLSRKDIRPAQTQTLLDAGFLPVSIDYRLCPEVSLAEGPMADARDALSWVRRVLPNIPLLRADIRPDGNQVVAIGWSTGGHLAMTLPFTAPAAGISAPNAVLAFYCPTNYEDPFWSNPNFPFGQTVASNEMEYDVWEGLQSMPIAGYNPALKERPLGGWMSTRDPRSRIALHMNWTGQTLPVLLKACTIKGNTEKCSPDDLSRPTEEEIQAVSPNYQIRVGRYNTPTFLIHGTSDDLVPCAQTESTHGALTASGVEAELRVVQEAAHLFDLYPASHAGQEAKAAVAEGYEFLRRHVQL | 2.3.1.- | null | fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; mycophenolic acid biosynthetic process [GO:0140722]; proteolysis [GO:0006508]; terpenoid biosynthetic process [GO:0016114] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177]; serine-type peptidase activity [GO:0008236] | PF00698;PF20434;PF18558;PF00109;PF02801;PF08242;PF00326;PF21089;PF00550;PF14765;PF16073; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.10.129.110;3.40.50.150; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A0B5KU17}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + 3 malonyl-CoA + S-adenosyl-L-methionine = 5-methylorsellinate + 3 CO2 + 4 CoA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:63056, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:146172; Evidence={ECO:0000269|PubMed:21398493}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63057; Evidence={ECO:0000269|PubMed:21398493}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21398490}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:21398490, PubMed:21398493). MpaC catalyzes the synthesis of 5-methylorsellinic acid (5MOA) via the condensation of 1 acetyl-CoA starter unit with 3 malonyl-CoA units and one methylation step (PubMed:21398493). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable) (PubMed:21398490, PubMed:22544261). {ECO:0000269|PubMed:21398490, ECO:0000269|PubMed:21398493, ECO:0000305|PubMed:21398490, ECO:0000305|PubMed:22544261}. | Penicillium brevicompactum |
F1LM81 | TM1L1_RAT | MAFGKSHRDPYATSLGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLSLSLIDMCMQNCGPSFQSLIVKKEFVKDTLVKLLNPRYTLPLETQNRILSFIKMWSQGFPGGVDVSEVKEVYLDLLKKGVQFPPLDGEPETKQEAGQISPSRPTSVPTAPALSSIIAPKNPTISLVPEQIGKLHSELDMVKMNVKVMTAILMENTPGSENHEDIELLRKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRLLEQKRNPTEANQTSSEPSAPSCDLLNLGPVAPVPVSSEGPLNSVNAQLSGLNVSSQSPVITNNLYPSLQPQMDLLASEDTEVPTLFPQRTSQNLASSHTYDNFPDHSSSVLLQPVSLHTAPAAPSSQRLPPLPSNHPVLKNSALQPPSYYEVMEFDPLAPTTEAIYEEIDASHKKGAQSHSEC | null | null | negative regulation of mitotic nuclear division [GO:0045839]; positive regulation of protein autophosphorylation [GO:0031954]; protein transport [GO:0015031]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi stack [GO:0005795]; membrane [GO:0016020] | clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; ubiquitin binding [GO:0043130] | PF03127;PF00790; | 1.20.58.160;1.25.40.90; | TOM1 family | PTM: Phosphorylated on tyrosines by FYN and LYN. {ECO:0000269|PubMed:17977829}. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack {ECO:0000250}. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17977829}. Membrane {ECO:0000269|PubMed:17977829}; Peripheral membrane protein {ECO:0000269|PubMed:17977829}; Cytoplasmic side {ECO:0000269|PubMed:17977829}. Note=A small proportion is membrane-associated. | null | null | null | null | null | FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
F1LM93 | YES_RAT | MGCIKSKENKSPAIKYTPENPTEPVNTSAGHYGVEHATAATTSSTKGASANFNSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPTSLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGILLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL | 2.7.10.2 | null | cell differentiation [GO:0030154]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of glucose transmembrane transport [GO:0010827]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | actin filament [GO:0005884]; centrosome [GO:0005813]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; postsynaptic specialization, intracellular component [GO:0099091] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; epidermal growth factor receptor binding [GO:0005154]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | null | PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-424 maintains enzyme activity by blocking CSK-mediated inhibition (By similarity). {ECO:0000250}.; PTM: Palmitoylation at Cys-3 promotes membrane localization. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1709169}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:1709169}. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis (By similarity). Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P07947, ECO:0000269|PubMed:21256972}. | Rattus norvegicus (Rat) |
F1LMN3 | E2F8_RAT | MENQKENLFSEPHKRGLVKSPLQESSKANVVLAEIQPDLGPLTTPTKPKEVSQGEPWTPTANLKMLISAVSPEIRSRDQKRGLSDNRSGLPEARDCLHEPQAKTNEKSQPSRKEKSLGLLCHKFLARYPKYPNPAVNNDICLDEVAEELDVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLTKTLGTLKSVGEENKYAEQIMMIKRKEHEQEFDFIKSCGLEDHHVIKSTAGQNGHSDMCFVELPGVEFRAASANSRKDKSLRVMSQKFVMLFLVSTPQIVSLEIAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNNSGSSPVMPLTASLEAEQSAKENCAKNLFSTRGKPSFTRHPSLIKLVKSIENDRRKISSAPSSPVKSSKAESSQNSPPVPNKMAQLAAICKMQLEEQSSEPRKRVKVNLTRSGHYKPLAPLDPAVNTELELLAPSLIQPLGMVPLIPSPLSSAVPVILPQAPSGPSYAIYLQPAQAQMLTPPHGLSPTVCPTQSSNATGSKDPTDAPTEKTATDATKPGSLQPAPERQGAKNRSKETTGDRGTKRTGALEDGGPGPIKKPKEDLKALENVPTPTTLFPSGYLIPLTQCPSLGPDPMLSNTENSGTLSPNHRIYGSPIAGVIPVASSELTAVNFPPFHVTPLKLMVSPTSMAAVPVGNSPALSSSHPAPTQNPSSAIVNFTLQHLGLISPGVQMSASPGPGAGTVPLSPRVEADNLSSRQGRATIHDSPVLGQSQLNGQPVAGTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSFMDFDGANKTSFGTLFVPQRKLEVSTEDVH | null | null | cell cycle comprising mitosis without cytokinesis [GO:0033301]; chorionic trophoblast cell differentiation [GO:0060718]; fibroblast proliferation [GO:0048144]; hepatocyte differentiation [GO:0070365]; negative regulation of cytokinesis [GO:0032466]; negative regulation of transcription by RNA polymerase II [GO:0000122]; placenta development [GO:0001890]; positive regulation of DNA endoreduplication [GO:0032877]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sprouting angiogenesis [GO:0002040]; trophoblast giant cell differentiation [GO:0060707] | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF02319; | 1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
F1LMV6 | DESP_RAT | MSCNGGSHPRINTLGRMTRAESGPDLRYEMTYSGGGGGGGGGGGGTSRMYYSRRCTVNDQNSDGYCQTGTMSRHQNQNTIQELLQNCADCLMRAELIAQPELKFGEGIQLAWNRELDEYFTQANDQMEIIDGLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISAPRVRRASSKGGYTCQSGSGWDEFTKRLTGECLGWMRQQRAEMDLMAWGVDSGSVEQHINSHRSIHNAIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFSIRMSQLEVKEKELNKLKQESDQLVLNQHPASDKIEAYMDTLQTQWSWILQITKCIDVHLKENAAYFQFFEEAQSTEAYLKGLQDSIRKKYPCDKNMPLQHLLEQIKELEKEREKILEYKRQVQNLVNKSKKIVQLKPRNPDYRSNKPIILRALCDYKQDQKIVHKGDECILKDNNERSKWYVTGPGGVDMLVPSVGLIIPPPNPLAVDLSCKIEQYYEAILALWNQLYINMKSLVSWHYCMIDIEKIRAMTIAKLKTMRQEDYMKTIEDLELHYQDFIKNSQGSEMFGDDDKRRMQSQFTDAQKHYQTLVIQLPGHPQHQTVTKTEITHVGTCQDVNHNKVIETNRENDKQETWLLMELQKIRRQMEHCEARMTLKNLLLTDQGSTHNITVKINELKSVQNDSQALAEVLNQLKDMLANFRGSEKYCYLQNEIFGLFQKLENINGVTDGYLNSLCSVRALLQAILQTEDMLKVYEARLTEEETVCLDLDKVEAYRCGLKKIKNDLNLKKSLLATMKTELQKAQQIHSQSSQQYPLYDLDLGKFTEKVTQLTDRWQKIDKQIDFRLWDLEKQIKQLRNYRDNYQSFCKWLYDAKRRQDSLESMKFGDSNTVMRFLNEQKNLHNEISGKRDKSEEVHKIAELCANSIKDYELQLASYTSGLETLLNIPIKRTMVQSPSGVILQEAADIHARYIELLTRSGDYYRFLSEMLKSLEDLKLKNTKIEVLEEELRLARDANSENCNKNKFLDQNLQKYQAECSQFKAKLVSLEELKRQAELDGKSAKQNLDKCYGQIKELNEKITRLTYEIEDEKRRRKTVEDRFDQQKNDYDQLQKARQCEKESLGWQKLESEKAIKEKEYEIERLRVLLQEEGARKREYENELAKVRNHYNEEMSNLRNKYETEINITKTTIKEISMQKEDDSKNLRNQLDRLSRENRDLKDEIVRLNDSILQATEQRRRAEENALQQKACGSEIMQKKQHLEVELKQVIQQRSEDNARHKQSLEEAAKTIQDKNKEIERLKAEYQEEAKRRWEYENELSKVRNSYDEEIISLRNKFETEINITKTTIHQLTMQKEEDTSGYRAQIDNLTRENRSLSEEVKRLKNTLAQTTENLRRVEENVQQQKASGSEMSQRKQQLEIELRQVSQMRTEESMRYKQSLDDAAKTIQDKNKEIERLKQLVDKETNERKCLEDENSKLQRVQYDLQKANNSATEAMSKLKVQEQELTRLRIDYERVSQERTVKDQDITRIQSSLKDLQLQKQKAEEELSRLKRTASDESSKRKMLEEELEAMRRSLKEQAVKITNLTQQLEQASIVKKRSEDDLRQQRDVLDGHVREKQRTQEELRRLSLDVEALRRQLVQEQENVKQAHLRNEHFQKAIEDKSRSLNESKIEIERLQSLTENLTKEHLMLEEELRNLRLEYDDLRRGRSEADNDKNSTISELRSQLQISNNRTLELQGLINDLQRERENLRQEIEKFQKQALEASNRIQESKSQCTQVVQERESLLVKIKVLEQDKARLQRLEDELNRAKATLEAETRVKQRLECEKQQIQNDLNQWKTQYSRKEETIRKIESEREKSEREKNSLRSEIERLQAEIKRIEERCRRKLEDSTRETQSQLETERCRLQKEIDKLRQRPYGSHRETQTEYEWTVDSSKLVFDGLRKKVTAMQLYECQLIDKTTLDKLLKGKKSVEEVASEIQPFLRGAGAIAGASASPKEKYSLVEAKRKKFITPESTVMLLEAQAATGGIIDPHRNEKLTVDNAIARDLIDFDDRQQIYTAEKAITGFDDPFSGKTVSVSEAIKKNLIDRETGMRLLEAQLASGGVVDPVNSVFLPKDVALARGLIDRDLYRSLNDPRDSQKNFVDPITKKKVSYMQLRERCRIEPHTGLLLLSVQKRSMSFQGIRQPVTVTELVDSGILRPSTVNELESGQISYDEVGERIKDFLQGSSCIAGIYNETTKQKLGIYEAMKIGLVRPGTALELLEAQAATGFIVDPVSNLRLPVEEAYKRGLVGIEFKEKLLSAERAVTGYNDPETGNIISLFQAMNKELIEKGHGIRLLEAQIATGGIIDPKESHRLPVDMAYKRGYFNEELSEILSDPSDDTKGFFDPNTEENLTYLQLKERCIKDEETGLCLLPLKEKKKQVQTSQKNTLRKRRVVIVDPETNKEMSVQEAYKKGLIDYETFKELCEQECEWEEITITGSDGSTRVVLVDRKTGSQYDIQDAIDKGLVDRKFFDQYRSGSLSLTQFADMISLKNGVGTSSGLSGSVNDDVFSSSRHESVSKISTISSVRNLTIRSSSLSDPLEESSPIAAIFDTENLEKISITEGIERGIVDSITGQRLLEAQACTGGIIHPTTGQKLSLQDAVSQGLIDQDMATRLKPAQKAFIGFEGVKGKKKMSAAEAVKEKWLPYEAGQRFLEFQFLTGGLVDPEVHGRISTEEAIRKGFIDGRAAQRLQDISSYAKILTCPKTKLKISYKDAMNRSMVEDITGLRLLEAASVSSKGLPSPYNMSAPGSRSGSRSGSRSGSRSGSRSGSRRGSFDATGNSSYSYSYSFSSSSIGY | null | null | adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; epithelial cell-cell adhesion [GO:0090136]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109]; keratinocyte differentiation [GO:0030216]; protein localization to cell-cell junction [GO:0150105]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; skin development [GO:0043588]; ventricular compact myocardium morphogenesis [GO:0003223]; wound healing [GO:0042060] | adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | protein kinase C binding [GO:0005080]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198] | PF00681;PF17902;PF18373;PF21019; | 1.20.58.1060;1.20.58.60;3.30.160.780;3.90.1290.10;2.30.30.40; | Plakin or cytolinker family | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:P15924}. Cell membrane {ECO:0000250|UniProtKB:E9Q557}. Note=Localizes at the intercalated disk in cardiomyocytes. {ECO:0000250|UniProtKB:E9Q557}. | null | null | null | null | null | FUNCTION: Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (PubMed:26858265). {ECO:0000269|PubMed:26858265}. | Rattus norvegicus (Rat) |
F1LMY4 | RYR1_RAT | MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIYSTAGLYNQFIKGLDSFSGKPRGSGPPAGSALPIEGVILSLQDLIGYFEPPSEELQHEEKQTKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFLTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLGPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLQPIKEYRREGPRGPHLVGPSRCLSHLDFVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMNNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVDSQSRGDRARIFRAEKSYAVQSGRWYFEFEAVTTGRELGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPLEHPHYEVARMDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLASPGLQPPAEDEARAAEPDTDYENLRRSAGGWGEAEAGKDGTAKEGTPGGAAQPGVEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPSTPALPRLPRDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFDLRPGANIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLHVDTRRAGERLGWAVQCQEPLMMMALHIPEENSEPYIHLKRAQLDPRDLRDYRDTKFDSESSDSDQTPQPGCYHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTEETRAITLFPPGRSAEDGPRRHGLPGVGVTTSLRPPHHFSPPCFVVALPAAGAAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGVFSDEDVKQILKMIEPEVFTEEEEVEEEEEEEEEDEEEKEEDEEEEAHEKEDEEKEEAEEAAEEEKEELEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAERYVDKLQSNQRGRYGLLMKAFTMSAAETARRTREFRSPPQEQINMLLQFKNGADEEDCPLPEEIREDLVNFHQDLLAHCGIQLEGEEEEPEEESTLGSRLMSLLEKVRLVKKKEEKPEEEPAAEEHKPQSLQELVSHTVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISLSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSRRWALALTRYLCAVLPLITKCAPLLRGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRIAMPCLCAIAGALPPDYVDASYSSKTEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYAHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTVEKAREGEEEKTEKKKTRKISQTAQTYDPREGYNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGSHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRHGKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTRNPYVEKLRPALGECLARLAAAMPVAFLEPELNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMAEIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLRSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRSAWPRLPPSPSSSFSLPSPSELGRWLMKDHGHQLYEESFTVPLILDNAAFPLARNQSRAIGCAGVVRSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIVLAKARYALKDTDEEVREFLQNNLNLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYHLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKASWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENVEEGGEEEEVEVSFEEKEMEKQRLLYQQSRLHNRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCRWPHKTLSQREGQEERVMKVQTSGTLVIINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILDYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGESEKMELFVSFCEDTIFEMQIAAQISEPEGEPEEDDDEGAEEAEEGAAGPDGSGSAAAAGVWTWLATAAGRTLRGLSYRSLRRRVRRLRRLTAREAATAVAVLLWAMVARAGGAGAGAAAGVLRLLWGSLFGGGLVDSAKKVTVTELLAGMPDPTGDEVHGQQPSGAGSDAEGEGQGEGEGDAAEGVGDEEVAADQAGTGGADRTVAVADGSPFRPEGAGGLGDMGDTTPVEPPTPEGSPILKRKLGVDGEEEEPQPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKAPPPPPPKKEEAGGAGLEEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMSGAGSGDGSGWGSRASEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWIMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLG | null | null | calcium ion transport [GO:0006816]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; muscle contraction [GO:0006936]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; ossification involved in bone maturation [GO:0043931]; outflow tract morphogenesis [GO:0003151]; protein homotetramerization [GO:0051289]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of response to osmotic stress [GO:0047484]; release of sequestered calcium ion into cytosol [GO:0051209]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to caffeine [GO:0031000]; response to caloric restriction [GO:0061771]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to muscle activity [GO:0014850]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; skeletal muscle contraction [GO:0003009]; skeletal muscle fiber development [GO:0048741]; skin development [GO:0043588]; striated muscle contraction [GO:0006941] | calcium channel complex [GO:0034704]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; I band [GO:0031674]; junctional membrane complex [GO:0030314]; membrane [GO:0016020]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; ryanodine receptor complex [GO:1990425]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; vesicle [GO:0031982]; Z disc [GO:0030018] | ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; protease binding [GO:0002020]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; voltage-gated calcium channel activity [GO:0005245] | 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;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2840 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2840. {ECO:0000250|UniProtKB:P21817}.; PTM: Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise increases S-nitrosylation (By similarity). {ECO:0000250|UniProtKB:P11716, ECO:0000250|UniProtKB:P21817}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11316255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11716}. Note=The number of predicted transmembrane domains varies between orthologs. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11316255}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11316255). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (By similarity). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity). {ECO:0000250|UniProtKB:E9PZQ0, ECO:0000250|UniProtKB:P11716, ECO:0000305|PubMed:11316255}. | Rattus norvegicus (Rat) |
F1LN46 | CPT1C_RAT | MAEAHQASSLLSSLSSDGAEVELSSSVWQEIYLSALRSWKRNLWRVWNDFLAGVVPATPLSWLFLFSTIQLACLLQLDPSLGLMEKIKELLPDWGGQHHQLQGLLAAAVFASCLWGTLIFTLHVALRLLLSHHGWLLEPHGTMSSPTKTWLALVRIFSGRHPRLFSFQRALPRQPVPGAQETVRKYLESMRPVLRDDAFDSVVALANDFLRLQAPRLQLYLQLKSWCASNYVSDWWEEFVYLRSRGSLVNSTYYMMDFLYVTPTPLQAARAGNAVHTLLLYRHLLNRQEIPPTLLMGMRPLCSAQYERMFNTTRIPGVEKDYLCHLQDSQHVAVFHQGRFFRVGTHSSNGLLSPRALEQQFQYILDDPSPACPLEEHLAALTAAPRSMWAQVRESVKTHAATALETVEGAAFFVSLDSEPAGLTRENPAASLDTYAHTLLTGQGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPVAGHLWEFTLATECFQLGYATDGHCKGHPDPALPKPQRLQWDLPKQIQPSISLALRGAKTLSGNIDCHVFPFFHFGKSFIKGCHVSSDSFIQLVLQLAHFRDRGQFCLTYESAMTRLFLEGRTETVRSCTREACQFVRAMENKERTDQQCLALFREAVDKHQALLKAAMSGQGIDRHLFALYIMSRLLHMQSPFLTQVQSQQWLLSTSQIPVQQTHLFDVHNYPDYVSSGGGFGPAHDHGYGVSYIFMGENAISFHISSKQSSTETDSHRLGQHIEDALLDVASLFQAGQQFKRQFTGLGESSGWKYSNLSCKTVDPNIPKSSTNL | 3.1.2.22 | null | carnitine metabolic process [GO:0009437]; fatty acid metabolic process [GO:0006631]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072] | AMPA glutamate receptor complex [GO:0032281]; axon [GO:0030424]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794] | carnitine O-palmitoyltransferase activity [GO:0004095]; palmitoyl-(protein) hydrolase activity [GO:0008474] | PF00755;PF16484; | 6.10.250.1760;3.30.559.10;3.30.559.70; | Carnitine/choline acetyltransferase family | null | SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGD5}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18192268}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000250|UniProtKB:Q8BGD5}. | CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniProtKB:Q8TCG5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000250|UniProtKB:Q8TCG5}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.35 mM for palmitoyl-CoA {ECO:0000269|PubMed:18192268}; KM=58.53 mM for carnitine {ECO:0000269|PubMed:18192268}; Vmax=0.09 nmol/min/mg enzyme (towards carnitine) {ECO:0000269|PubMed:18192268}; Vmax=0.095 nmol/min/mg enzyme (towards palmitoyl-CoA) {ECO:0000269|PubMed:18192268}; | null | null | null | FUNCTION: Palmitoyl thioesterase specifically expressed in the endoplasmic reticulum of neurons. Modulates the trafficking of the glutamate receptor, AMPAR, to plasma membrane through depalmitoylation of GRIA1 (By similarity). Also regulates AMPR trafficking through the regulation of SACM1L phosphatidylinositol-3-phosphatase activity by interaction in a malonyl-CoA dependent manner (By similarity). Binds malonyl-CoA and couples malonyl-CoA to ceramide levels, necessary for proper spine maturation and contributing to systemic energy homeostasis and appetite control (By similarity). Binds to palmitoyl-CoA, but does not have carnitine palmitoyltransferase 1 catalytic activity or at very low levels (PubMed:18192268, PubMed:24222496). {ECO:0000250|UniProtKB:Q8BGD5, ECO:0000250|UniProtKB:Q8TCG5, ECO:0000269|PubMed:18192268, ECO:0000269|PubMed:24222496}. | Rattus norvegicus (Rat) |
F1LNJ2 | U520_RAT | MADVTARSLQYEYKANSNLVLQADRSLIDRTRRDEPTGEVLSLVGKLEGTRMGDKAQRTKPQMQEERRAKRRKRDEDRHDINKMKGYTLLSEGIDEMVGIIYKPKTKETRETYEVLLSFIQAALGDQPRDILCGAADEVLAVLKNEKLRDKERRREIDLLLGQTDDTRYHVLVNLGKKITDYGGDKEIQNMDDNIDETYGVNVQFESDEEEGDEDVYGEVREEASDDDMEGDEAVVRCTLSANLVASGELMSSKKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDDRECENQLVLLLGFNTFDFIKVLRQHRMMILYCTLLASAQSEAEKERIMGKMEADPELSKFLYQLHETEKEDLIREERSRRERVRQSRMDTDLETMDLDQGGEALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPALKPKPFGSEEQLLPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIVLDEIHLLHDDRGPVLEALVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYVGITEKKAIKRFQIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILITSHGELQYYLSLLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRMLRSPTLYGISHDDLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKARLVHGSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLILPEKYPPPTELLDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQNSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHTQTRLLSMAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFLHCTEKDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSKKDFFKKFLYEPLPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNYYNLQGISHRHLSDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKTNLLLQAHLSRMQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGDAKSNSLISIKRLTLQQKAKVKLDFVAPATGGHNYTLYFMSDAYMGCDQEYKFSVDVKEAETDSDSD | 3.6.4.13 | null | mRNA splicing, via spliceosome [GO:0000398]; spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) [GO:0000388] | catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type catalytic step 1 spliceosome [GO:0071006]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; RNA helicase activity [GO:0003724] | PF21188;PF00270;PF00271;PF18149;PF02889; | 1.10.150.20;2.60.40.150;3.40.50.300;1.10.3380.10;1.10.10.10; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}. | 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:O75643}; | null | null | null | null | FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. {ECO:0000250|UniProtKB:O75643}. | Rattus norvegicus (Rat) |
F1LP64 | TRIPC_RAT | MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPRAFQHIESLSETNKPPSKSKKRHLDQEQQLKSAQLPSTSKAHTRKSVAAGSSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPAGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPEGNQETVNSSAARTDEAPQGAAASSSVAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNPLANTNTSGYSDLKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSLGSTTPASSGTATAATNASADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSAQSNSNNIEPARTAGVSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPVGRVEPVGHAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGSGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSVQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESSKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVANPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQQSFHLS | 2.3.2.26 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; heterochromatin boundary formation [GO:0033696]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of embryonic development [GO:0045995]; ubiquitin-dependent protein catabolic process [GO:0006511] | nuclear speck [GO:0016607]; nucleoplasm [GO:0005654] | nuclear thyroid hormone receptor binding [GO:0046966]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00632;PF02825; | 3.30.720.50;3.30.2410.10;3.90.1750.10;1.25.10.10; | UPL family, K-HECT subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14669}. | 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:Q14669}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q14669}. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex. {ECO:0000250|UniProtKB:Q14669}. | Rattus norvegicus (Rat) |
F1LP90 | MINK1_RAT | MGDPAPARQSDFIFLVALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFTDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDRSRKKRGEKEETEYEYSGSEEEDDSHGEEGEPSSIMNVPGESTLRREFLRLQQENKSNSEALKQQQQLQQQQQRDPEAHIKHLLHQRQRRIEEQKEERRRVEEQQRREREQRKLQEKEQQRRLEDMQALRREEERRQAEREQEYKRKQLEEQRQSERLQRQLQQEHAYLNSQKQQQQQQQQQQQQQQQQILPGDRKPLYHYGRGINPADKPAWAREVEERARMNKQQNSPLAKTKPSSAGPEPPIPQASPSPPGPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKPYAAPVPRSQSLQDQPTRNLAAFPASHDPDPAAVPTPTATPSARGAVIRQNSDPTSEGPGPSPNPPSWVRPDNEAPPKVPQRTSSIATALNTSGAGGSRPAQAVRARPRSNSAWQIYLQRRAERGTPKPPGPPAQPPGPPNTSSNPDLRRSDPGWERSDSVLPASHGHLPQAGSLERNRNRVGASTKLDSSPVLSPGNKAKPEDHRSRPGRPADFVLLKERTLDEAPKPPKKAMDYSSSSEEVESSEDEEEEGDGEPSEGSRDTPGGRSDGDTDSVSTMVVHDVEEVSGTQPSYGGGTMVVQRTPEEERSLLLADSNGYTNLPDVVQPSHSPTENSQGQSPPTKDGGGDYQSRGLVKAPGKSSFTMFVDLGIYQPGGSGDTIPITALVGGEGGRLDQLQFDVRKGSVVNVNPTNTRAHSETPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDMEGCGHYRVVKYERIKFLVIALKNSVEVYAWAPKPYHKFMAFKSFADLPHRPLLVDLTVEEGQRLKVIYGSSAGFHAVDVDSGNSYDIYIPVHIQSQITPHAIVFLPNTDGMEMLLCYEDEGVYVNTYGRIIKDVVLQWGEMPTSVAYICSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLNRNCIMNW | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; chemical synaptic transmission [GO:0007268]; dendrite morphogenesis [GO:0048813]; MAPK cascade [GO:0000165]; negative thymic T cell selection [GO:0045060]; neuron cellular homeostasis [GO:0070050]; neuron projection morphogenesis [GO:0048812]; positive regulation of JNK cascade [GO:0046330]; positive regulation of p38MAPK cascade [GO:1900745]; protein autophosphorylation [GO:0046777]; regulation of AMPA receptor activity [GO:2000311]; regulation of cell migration [GO:0030334]; regulation of cell-cell adhesion [GO:0022407]; regulation of cell-matrix adhesion [GO:0001952]; regulation of MAPK cascade [GO:0043408] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; postsynaptic density [GO:0014069] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00780;PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:21048137}. Cell projection, axon {ECO:0000269|PubMed:21048137}. Cell projection, dendrite {ECO:0000269|PubMed:21048137}. | 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; 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; | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking (PubMed:21048137). Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons (PubMed:21048137). Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates TANC1 upon stimulation by RAP2A, MBP and SMAD1 (By similarity). Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1 (By similarity). Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (By similarity). {ECO:0000250|UniProtKB:Q8N4C8, ECO:0000250|UniProtKB:Q9JM52, ECO:0000269|PubMed:21048137}. | Rattus norvegicus (Rat) |
F1LQ48 | HNRPL_RAT | MSRRLLPRAEKRRRRLEQRQQPDEQLRRAGAMVKMAAAGGGGGGGRYYGGGNEGGRAPKRLKTENAGDQHGGGGGGGSGAAGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGEGRGFPSVDSRGSCAPARRPPRKFSPVLPLFPSHPPGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPDYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKMNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPTSVKVFSGKSERSSSGLLEWDSKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS | null | null | cellular response to amino acid starvation [GO:0034198]; circadian rhythm [GO:0007623]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of translation [GO:0045727]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; response to peptide [GO:1901652] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; pronucleus [GO:0045120]; ribonucleoprotein complex [GO:1990904]; ribonucleoprotein granule [GO:0035770]; synapse [GO:0045202] | mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; mRNA CDS binding [GO:1990715]; pre-mRNA intronic binding [GO:0097157]; RNA binding [GO:0003723]; transcription cis-regulatory region binding [GO:0000976] | PF00076;PF13893;PF11835; | 3.30.70.330; | null | PTM: Several isoelectric forms of the L protein are probably the results of post-translational modifications. {ECO:0000250|UniProtKB:P14866}.; PTM: Phosphorylation at Ser-578 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. {ECO:0000250|UniProtKB:P14866}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P14866}. Cytoplasm {ECO:0000269|PubMed:18161049}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. {ECO:0000250|UniProtKB:P14866}. | null | null | null | null | null | FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (By similarity). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8. {ECO:0000250|UniProtKB:P14866}. | Rattus norvegicus (Rat) |
F1LQ70 | LOX12_RAT | MGRYRVRVVTGAWLFSGSVNLVRLWLVGAHREARLELQLRPARGKEEEFDFDVAEDLGPLQFVKLHKEHTVVDDAWFCNLITVQGPGMSAEAVFPCYRWVQGEGILRLPEGTARLAGDNALDVFQKHREKELKERQQTYRWATWKQGLPQTIAADCKDDLPPNMRFHEEKRLDFEWTLKAGVLEMGLKRVYTLLRSWNRLEDFDQIFWGQKSALAEKVHRCWQEDELFGYQFLNGANPMLLRRSTSLPSRLVLPPGTEELQAQLEKELKDGCLFEADFILLDGIPANVIRGEQQYLAAPLVMLRMDPSGKLLPMAIQIQPPNPSSPAPTLFLPSDPPLAWLLAKIWVRNSDFQLQELQFHLLNTHLVAEVIAVATMRCLPGLHPIFKLLVPHIRYTMEINTRSRTQLISDGGIFDQVVSTGGGGHVQLLTRAVAQLTYCSLCPPDDLATRGLLRVPSALYAQDALQLWEVTARYVNGMVHLFYQSDDIVRGDPELQAWCREITEVGLCHAQDRGFPVSFQSRAQLCHFLTMCVFTCTSQHAAINQGQLDWYGWVPNAPCTMRMPPPTSKDDVTMETIMGSLPDVQKSCLQMTITWHLGRLQPDMVPLGHHKEKYFSDPRTKAVLSQFQADLENLEKEITARNQQLDLPYEYLKPSRIENSITI | 1.13.11.-; 1.13.11.31; 1.13.11.33; 3.3.2.- | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; cellular response to lipid [GO:0071396]; establishment of skin barrier [GO:0061436]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; leukotriene A4 metabolic process [GO:1901751]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; lipid oxidation [GO:0034440]; lipoxin A4 biosynthetic process [GO:2001303]; lipoxin B4 biosynthetic process [GO:2001306]; lipoxygenase pathway [GO:0019372]; negative regulation of apoptotic process [GO:0043066]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of platelet aggregation [GO:0090331]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of endothelial tube morphogenesis [GO:1905956]; positive regulation of gene expression [GO:0010628]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of smooth muscle cell proliferation [GO:0048661]; unsaturated fatty acid metabolic process [GO:0033559] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; sarcolemma [GO:0042383] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane {ECO:0000250}. Note=Membrane association is stimulated by EGF. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:23382512}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=2 H2O + 2 leukotriene A4 + O2 = 2 lipoxin A4; Xref=Rhea:RHEA:48584, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57463, ChEBI:CHEBI:67026; Evidence={ECO:0000269|PubMed:23382512}; CATALYTIC ACTIVITY: Reaction=2 H2O + 2 leukotriene A4 + O2 = 2 lipoxin B4; Xref=Rhea:RHEA:48588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57463, ChEBI:CHEBI:67031; Evidence={ECO:0000269|PubMed:23382512}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:16869, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57446; EC=1.13.11.33; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16870; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate = (13S,14S)-epoxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + H2O; Xref=Rhea:RHEA:53532, ChEBI:CHEBI:15377, ChEBI:CHEBI:78048, ChEBI:CHEBI:131958; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53533; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanine; Xref=Rhea:RHEA:50184, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071, ChEBI:CHEBI:132077; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50185; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-alanine; Xref=Rhea:RHEA:50172, ChEBI:CHEBI:15379, ChEBI:CHEBI:132071, ChEBI:CHEBI:132074; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50173; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-gamma-aminobutanoate; Xref=Rhea:RHEA:50180, ChEBI:CHEBI:15379, ChEBI:CHEBI:132072, ChEBI:CHEBI:132078; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50181; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-gamma-aminobutanoate; Xref=Rhea:RHEA:50176, ChEBI:CHEBI:15379, ChEBI:CHEBI:132072, ChEBI:CHEBI:132075; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50177; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:50188, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002, ChEBI:CHEBI:132076; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50189; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:50168, ChEBI:CHEBI:15379, ChEBI:CHEBI:59002, ChEBI:CHEBI:132073; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50169; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-taurine; Xref=Rhea:RHEA:50160, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060, ChEBI:CHEBI:132061; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50161; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurine; Xref=Rhea:RHEA:50156, ChEBI:CHEBI:15379, ChEBI:CHEBI:132060, ChEBI:CHEBI:132062; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50157; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:41332, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:78048; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41333; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,14S)-dihydroperoxy-(4Z,8E,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64724, ChEBI:CHEBI:15379, ChEBI:CHEBI:156049, ChEBI:CHEBI:156082; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64725; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoate; Xref=Rhea:RHEA:64728, ChEBI:CHEBI:15379, ChEBI:CHEBI:140349, ChEBI:CHEBI:156049; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64729; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate; Xref=Rhea:RHEA:48704, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:90772; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48705; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(8Z,10E,14Z)-eicosatrienoate; Xref=Rhea:RHEA:41328, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:78047; Evidence={ECO:0000250|UniProtKB:P18054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41329; Evidence={ECO:0000250|UniProtKB:P18054}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781; Evidence={ECO:0000250|UniProtKB:P39655}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:41324, ChEBI:CHEBI:15379, ChEBI:CHEBI:78043, ChEBI:CHEBI:78046; Evidence={ECO:0000250|UniProtKB:P39655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41325; Evidence={ECO:0000250|UniProtKB:P39655}; CATALYTIC ACTIVITY: Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14R,15S)-epoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:50276, ChEBI:CHEBI:15379, ChEBI:CHEBI:131965, ChEBI:CHEBI:132063; Evidence={ECO:0000250|UniProtKB:P39655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50277; Evidence={ECO:0000250|UniProtKB:P39655}; CATALYTIC ACTIVITY: Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14S,15R)-epoxy-(5Z,8Z,10E)-eicosatrienoate; Xref=Rhea:RHEA:50284, ChEBI:CHEBI:15379, ChEBI:CHEBI:131964, ChEBI:CHEBI:132065; Evidence={ECO:0000250|UniProtKB:P39655}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50285; Evidence={ECO:0000250|UniProtKB:P39655}; | null | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:23382512}. | null | null | FUNCTION: Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:23382512). Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE. Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA. Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets (By similarity). An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites (PubMed:23382512). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE) (By similarity). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic. Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells (By similarity). {ECO:0000250|UniProtKB:P18054, ECO:0000250|UniProtKB:P39655, ECO:0000269|PubMed:23382512}. | Rattus norvegicus (Rat) |
F1LQQ7 | SCN7A_RAT | MLTSPEPKGLVPFTAESLELIKNHIAKKCNEEHEEEDLKPSWGLEAGKKLPFAYGTLPQGTVSEPLEDVDPYYYVKRNTFMVLNRNRVIFRFNAVSILCTLSPLSSLRRAVIKVLVHPLFRLLILISVLTDSILMCMSNLPEWILAVENTLLGIYTFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRSSPLSSLPMFKTIRTLRILKIIPLNHGLQSIVVTLVQCLKKLLGAIALALFFLTVSSLFGMGLFMGNLKHKCVRWPQEDGNDVMYNGTGSQYHILERENFYYMEGARYALLCGNKTDAGLCPEGYMCVKEGSNPDNGFTSFDNFGWALLAMFRLMTQDYPELLYHQILYASGKIYMIFFVLISFWFAFYMASLFLGILTMAYEQEKQRASEESRDMDSKCHQTVKEFEEEHEGAEMETTQIEMKKRSPTSINTTLDILEDTALGHKEEPETSRKECPLCWYKFTKTCFIWKCSPCWIKLNEFADRIITHPLFDLFLVICIILNICFLALEHFPMSEELMSLLAIGNLVFIGIYTIEMILKIIAMHPYGYFQISWHIFDSILVVLGLTEMLLADIEEITVFILVPLIFIKLGKYAPPFKNLMRILGRALVALKDLVLLVSIFIYFSAVFGMKLFGRSYKDCVCHVDQDCQRQRWHMSDFLHAYVTVFRILCGEWIETLWECMEVAGEAWCIPFYMMVILIGNLLILYLFVALVSSFASYDATTEVSKEAKNLQLAVAWIKMVINCVLLKILCKEKTVSTEATDQTCDPSVKENISGHTLSELSNTQTFLRYKDQSSGTEKTPVTESESQSLIASPSVSETVPIASGESDIENLDNKETRSKSANGSSKEKMKQSSSSECSTVDIAISEEEEMVYEHEKSKLHKNGYERKSSAGQVSRESRNGKIWRNIRKTCCKIVENSWFECFIGLVTLLCTGTLALEDIYIDQRKTIKIFLEYGDMIFAYIFILEMLLKWVAYGFKAYFSNNWYKLDFMVVIVLCLSLIGKTREDLNPLASIKFLRALRVLSQFERMKVVLRALIKTTLPAVSVFLVCLMIWLLFSVMGVFLFAGKFYECIDPTRGERFSVFEVMNKSQCENLVFNESMPWENAKLNFDNVGNGFLSLFQVATFNGWISIMNSAIDSVGVYMQPSFEHSLHMYTYFIIFVVFGLFLPLCMLIGVIIRNFNKQKIKQGGSNIFITVKQKKQYRALKKLLYADSQKPAARPRNKFQGFICDVVTHRVFNVIIILLICFQATTIMIQNDEQSPQIETAVFWMNSLFTMLFTLECILKLTAFRCHYFTSAWNVHDFMVVVFSITGLLLPLSIGQYFVPPSLVQLLLLSRIIHVLRPGKGPKVFHDLMLPLMLSLPALLNIALLIFLVMFIYAIFGMYNFAYVKKEAGINDVSNFETFGSSMLCLFQVTTFSGWDGMLDAIFNSQWSDCDPDKINPGTQVRGDCGSPSVGIFYFVSYILISWLIIVNMYVVLIMEFLSIPSKRKNRTLSEDDFRRFFKVWNRFDPDRTQYIDSTKLSDFAAALDPPLFMAKPNKGQLVAMDLPMAAGDRIHCLDILLAFTKRVMGKDERVEKILSEIESGFMLANPFKITYEPITTTLKRKQEAVSATIIQRAYKSYRLRQSDKKIQDIPEIDDGREDPNSKGVHSGQIEEKASIQTQI | null | null | cellular homeostasis [GO:0019725]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; osmosensory signaling pathway [GO:0007231]; response to bacterium [GO:0009617]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814] | axon [GO:0030424]; glial cell projection [GO:0097386]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518] | osmolarity-sensing monoatomic cation channel activity [GO:1990760]; sodium channel activity [GO:0005272]; transmembrane transporter binding [GO:0044325]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, SCN7A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01118}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:21084682}; | null | null | null | null | FUNCTION: Sodium leak channel functioning as an osmosensor regulating sodium ion levels in various tissues and organs. While most sodium channels are voltage-gated, SCN7A is not and lets sodium flow through membrane along its concentration gradient (PubMed:21084682, PubMed:9001394). In glial cells of the central nervous system, senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake through activation of nearby neurons to maintain appropriate sodium levels in the body (By similarity). By mediating sodium influx into keratinocytes, also plays a role in skin barrier homeostasis (By similarity). {ECO:0000250|UniProtKB:B1AYL1, ECO:0000250|UniProtKB:Q01118, ECO:0000269|PubMed:21084682, ECO:0000269|PubMed:9001394}. | Rattus norvegicus (Rat) |
F1LQX4 | RHG44_RAT | MKKQFNRMRQLANQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLGKMLKLCGETEDELAQELIHFELRVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNIQEQDKRLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQSEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEIEFNITGSYGSPVHVNHNANYSSMPSPDMDPADRRQPEQARRPLSVATDNMMLEFYKKDGLRKIQSMGVRVMDTSWVARRGSSAGRKAACAPPSMQPPAPPSELAAPLPSPLPEQVPDSPATPAPALSPSGASLQPTPERPSVSKSKELSPGSGQKGSPGSIQGTTCPGTQLGPQPAASPSQLPADQSPHTLRKVSKKLAPIPPKVPFVQPGTVSDQPTGQPSPVSLSPTPPSTPSPYGLSYPPGYSMASGQLSPASAPPLASPSVFTSTLAKSRPTPKPRQRPTLPPPQPPSVSLSASSPQSTEHPMLDGMSPGESMSTDLVHFDVPSIHIELGSTLRLSPLEHARRHSVTDKRDSEEESESTAL | null | null | exocytosis [GO:0006887]; modification of dendritic spine [GO:0098886]; modification of postsynaptic structure [GO:0099010]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of filopodium assembly [GO:0051490]; negative regulation of Rac protein signal transduction [GO:0035021]; neurotransmitter receptor transport, endosome to postsynaptic membrane [GO:0098887]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of GTPase activity [GO:0043087]; regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane [GO:0099152]; signal transduction [GO:0007165] | dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; leading edge membrane [GO:0031256]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; recycling endosome [GO:0055037] | GTPase activator activity [GO:0005096]; phospholipid binding [GO:0005543]; small GTPase binding [GO:0031267] | PF03114;PF00620; | 1.20.1270.60;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:25498153}. Recycling endosome {ECO:0000250|UniProtKB:Q5SSM3}. Presynapse {ECO:0000269|PubMed:23739967}. Cell projection, dendrite {ECO:0000269|PubMed:25498153}. Note=In CA1 hippocampal synapses, detected at both presynaptic and postsynaptic sites (By similarity). Located in convoluted dendritic plasma membrane sections enriched in polymerized actin and myosin (patches) along dendrites where often emerge filopodia (PubMed:25498153). {ECO:0000250|UniProtKB:Q5SSM3, ECO:0000269|PubMed:25498153}. | null | null | null | null | null | FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. Acts as a GAP at least for CDC42 and RAC1 (PubMed:25498153). In neurons, is involved in dendritic spine formation and synaptic plasticity in a specific RAC1-GAP activity (PubMed:25498153). Limits the initiation of exploratory dendritic filopodia. Recruited to actin-patches that seed filopodia, binds specifically to plasma membrane sections that are deformed inward by acto-myosin mediated contractile forces. Acts through GAP activity on RAC1 to reduce actin polymerization necessary for filopodia formation (PubMed:25498153). In association with SHANK3, promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation (By similarity). {ECO:0000250|UniProtKB:Q5SSM3, ECO:0000269|PubMed:25498153}. | Rattus norvegicus (Rat) |
F1LQY6 | NECA2_RAT | MCERAARLCRAGAHRLLREPPPQGRALGGLLRWVGARMGEPRAPLVPDIPAADPDPGPAAPRGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEGLFHTIDSDNTNHVDTKELCDYFVEHMGDYEDVLASLETLNHSVLKAMGYTKKVYEGGNNVDQFVTRFLLKETANQIQSLLSSVESAVEAIEEQTSQIRQDHCKPSPGVNESRYGGPTPPYIPNHKLVVPEPVKSLPVAIGEPKEEGLEVQISRLAELIGRLESKTLSFDLQQRLSDEEGTNMYLQLVRQEMAVCPEQLGEFLDSLRQYLRSTAEERNCFHVAAVRMADGLTFVIYEFWETEEEWKRHLQSPVCKAFRHVKVDTLSQPEALSQISVPAAWCTSGRD | null | null | calcium-mediated signaling [GO:0019722]; negative regulation of G protein-coupled receptor internalization [GO:1904021]; positive regulation of adenosine receptor signaling pathway [GO:0060168]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glutamate receptor signaling pathway [GO:1900451]; positive regulation of protein localization to membrane [GO:1905477]; regulation of amyloid precursor protein biosynthetic process [GO:0042984] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; plasma membrane [GO:0005886] | A2A adenosine receptor binding [GO:0031687]; calcium ion binding [GO:0005509]; type 5 metabotropic glutamate receptor binding [GO:0031802] | PF03992;PF13499; | 3.30.70.100;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17689978}. Cell projection, dendrite {ECO:0000269|PubMed:17689978}. Cell projection, axon {ECO:0000269|PubMed:17689978}. Cell membrane {ECO:0000250|UniProtKB:Q7Z6G3}. Note=Colocalizes with ADORA2A and/or mGluR5/GRM5 at the plasma membrane (By similarity). Found in neuronal somata (PubMed:26843217). Detected in the cytoplasm of striatal neurons, at postsynaptic sites, filling dendritic shafts and spines, and at presynaptic sites, filling axon terminals (PubMed:17689978). {ECO:0000250|UniProtKB:Q7Z6G3, ECO:0000269|PubMed:17689978, ECO:0000269|PubMed:26843217}. | null | null | null | null | null | FUNCTION: May act as a signaling scaffold protein that senses intracellular calcium. Can modulate ligand-induced internalization of ADORA2A and coupling efficiency of mGluR5/GRM5; for both receptors may regulate signaling activity such as promoting MAPK1/3 (ERK1/2) activation. {ECO:0000250|UniProtKB:Q7Z6G3}. | Rattus norvegicus (Rat) |
F1LR10 | LIMA1_RAT | MESTPFNRRQWTSLSLRVTAKELSLVNKNKSSTIVEIFSKYQKAAEEANMERKKNNTESLPQHFRRGTLSVLKKKWENPVAGAESHTDSLPNSSSDGGHTADHPPAEVTAKAAPGARADREEHTQPRSRFGSRPEAVTQCRYPRSEDSHDFKAQATESQNMENCLGDSRHEAEKPEMSENTETSGKIEKYNVPLNRLKMMFEKGEHSQNKSPWTQGRNAGGRRLSENSCSLDDLEIGAGHLSSSAFNSEKNESKRNLELPRLSETSIKDRMAKYQAAVSKQSSPASYASELKPSESKTHKWEQKENVPPGPEACSIHQEGSKVSATENSLVAHPVPAEDDTCNSQGRSEAQQPIYTKPLSPDARTSSLPESSPSKTAKKFQAPARESCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHKQHKDLWASKGENEETLGRPAQPPSAGETPHSPGVEDAPIAKVGVLAASMEAKASSQREREENKPAETKKLRIAWPPPAEQGSSGSAPEEGFKVSKPKWPPEDEVCKTEAPEDVDLDLKKLRRSSSLKERSRPFTVAASFRTSSVKSPKPLSPSLRKGWSEPEPEQSEEFGGGTVTQTESPRPSREKESVGKSRWQSEEAEAEAEEAPRGRDGRSFELESESFIGNGASIAEDDVAPAQRSPLEPESPGWPGFGDTTTAKEFNQKSQDVGFWEGEVVRELSVEEQIKRNRYYDEDEDEE | null | null | actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; intestinal cholesterol absorption [GO:0030299]; negative regulation of actin filament depolymerization [GO:0030835]; ruffle organization [GO:0031529] | actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; metal ion binding [GO:0046872] | PF00412; | 2.10.110.10; | null | PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhanced cell motility. {ECO:0000250|UniProtKB:Q9ERG0}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Note=This cytoskeletal protein colocalizes with actin stress fibers and focal adhesion plaques. Expressed mainly in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (By similarity). Colocalizes with PXN at focal adhesions in mesangial cells (By similarity). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000250|UniProtKB:Q9UHB6}. | null | null | null | null | null | FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250|UniProtKB:Q9ERG0, ECO:0000250|UniProtKB:Q9UHB6}. | Rattus norvegicus (Rat) |
F1LRS8 | CD2AP_RAT | MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERPGNVASLVQRISTYGLPAGGIQPHPQTKAMKKKTKKRQCKVLFEYSPQNEDELELTVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTDDGEMHDAQEESEVSLTGPTSPMPSPGNGSEPAPGSVTQPKKIRGVGFGDIFKEGSVKLRTRTSSSETEEKKSEKPLILQSLGSRTQNVEVTKPDIDGKIKAKEYCKTVFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVFPDNFAVQISELDKDFPKPKKPPPPAKGPAPKPDPLAGEKKTFPLKAEDRDEKSLLEQKPSKPAAPQVPPKKPTPPTKANNLLRSPGTMYPKRPEKPVPPPPPTAKINGEVSTISSKIDTEPLSKPKLDPEQLPVRPKSVDLDALVARNSKETDNVNFDDIASSENLLHLTANRPKMPGRRLPGRFNGGHSPTQSPEKTLKLPKDDDSGNIKPSEFKKDAGYSSKPSLSAPSSASKVNTAAFLSPLELKAKVEADDGKKSSLDELRAQIIELLCIVDALKKDHGKELEKLRRELEEEKAMRSNLEVEIAKLKKAVLLS | null | null | actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; adipose tissue development [GO:0060612]; apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cell migration [GO:0016477]; cell population proliferation [GO:0008283]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction organization [GO:0045216]; collateral sprouting [GO:0048668]; endothelium development [GO:0003158]; ERK1 and ERK2 cascade [GO:0070371]; filopodium assembly [GO:0046847]; gene expression [GO:0010467]; glomerulus development [GO:0032835]; glucose import [GO:0046323]; immunological synapse formation [GO:0001771]; inflammatory response [GO:0006954]; kidney development [GO:0001822]; lipid metabolic process [GO:0006629]; liver development [GO:0001889]; localization of cell [GO:0051674]; lymph node development [GO:0048535]; maintenance of blood-brain barrier [GO:0035633]; male gonad development [GO:0008584]; membrane organization [GO:0061024]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of small GTPase mediated signal transduction [GO:0051058]; negative regulation of transforming growth factor beta1 production [GO:0032911]; nerve growth factor signaling pathway [GO:0038180]; neuron projection development [GO:0031175]; neurotrophin signaling pathway [GO:0038179]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; podocyte differentiation [GO:0072112]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein secretion [GO:0050714]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein catabolic process [GO:0030163]; protein heterooligomerization [GO:0051291]; protein secretion [GO:0009306]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of receptor-mediated endocytosis [GO:0048259]; regulation of synaptic plasticity [GO:0048167]; renal albumin absorption [GO:0097018]; response to glial cell derived neurotrophic factor [GO:1990790]; response to insulin [GO:0032868]; response to oxidative stress [GO:0006979]; response to transforming growth factor beta [GO:0071559]; response to virus [GO:0009615]; response to wounding [GO:0009611]; stress-activated MAPK cascade [GO:0051403]; synapse organization [GO:0050808]; T cell receptor signaling pathway [GO:0050852]; transforming growth factor beta1 production [GO:0032905]; vesicle organization [GO:0016050] | actin filament [GO:0005884]; axon [GO:0030424]; cell leading edge [GO:0031252]; cell periphery [GO:0071944]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; filamentous actin [GO:0031941]; growth cone [GO:0030426]; late endosome [GO:0005770]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; podosome [GO:0002102]; protein-containing complex [GO:0032991]; ruffle [GO:0001726]; slit diaphragm [GO:0036057]; trans-Golgi network membrane [GO:0032588]; vesicle [GO:0031982] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; protein-containing complex binding [GO:0044877]; SH3 domain binding [GO:0017124]; vascular endothelial growth factor receptor binding [GO:0005172] | PF00018;PF14604; | 2.30.30.40; | null | PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction {ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte slit diaphragm between podocyte foot processes (By similarity). During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase (By similarity). {ECO:0000250|UniProtKB:Q9JLQ0, ECO:0000250|UniProtKB:Q9Y5K6}. | null | null | null | null | null | FUNCTION: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (PubMed:18753381). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis. Plays a role in epithelial cell junctions formation (By similarity). {ECO:0000250|UniProtKB:Q9JLQ0, ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:18753381}. | Rattus norvegicus (Rat) |
F1LTE0 | TANC2_RAT | MFRNSLKMLLTGGKSSRKNRSSDGGSEEPPDRRQSSVDSRQSRSGPGGISTESDCAFEPDYAVPALPVSEGDVEQELGPPPSVDEAANTLMTRLGFLLGEKVTEVQPGDQYSMEVQDENQTSAITQRISPCSTLTSSTASPPASSPCSTLPPVSTNATAKDCSYGAVTSPTSTLESRDSGIIATLTNYSENMERTKYVGEAGKELGSGGNLKPWQSQKSSMDSCLYRVDENMAASTYSLNKIPERNLETVLSQSVQSIPLYLMPRPNSVAATSSAHLEDLAYLDEQRHTPLRTSLRMPRQSMSGARTQQDLRVRFAPYRPPDISLKPLLFEVPSITTESVFVGRDWVFHEIDAQLQSSNASVNQGVVIVGNIGFGKTAIISRLVALSCHGTRMRQIASDSPHASPKHVDANRELPLTQAPSAHSSIASGSCPGTPEMRRRQEEAMRRLASQVVAYHYCQADNAYTCLVPEFVHNVAALLCRSPQLTAYREQLLREPHLQSMLSLRSCVQDPMASFRRGVLEPLENLHKERKIPDEDFIILIDGLNEAEFHKPDYGDTIVSFLSKMIGNFPSWLKLIVTVRTSLQEITKLLPFHRIFLDRLEENEAIDQDLQAYILHRIHSSSEIQNNISLNGKMDNTTFGKLSSHLKTLSQGSYLYLKLTFDLIEKGYLVLKSSSYKVVPVSLSEVYLLQCNMKFPTQSSFDRVMPLLNVAVASLHPLTDEHIFQAINAGSIEGTLEWEDFQQRMENLSMFLIKRRDMTRMFVHPSFREWLIWREEGEKTKFLCDPRSGHTLLAFWFSRQEGKLNRQQTIELGHHILKAHIFKGLSKKVGVSSSILQGLWISYSTEGLSMALASLRNLYTPNIKVSRLLILGGANINYRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDASSESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIQCDWTMAGQQQGVFKKSQAIQQALIAAASMGYTEIVSYLLDLPEKDEEEVERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGAVPLFSTVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVDFLLAQGASIALMDKEGLTALSWACLKGHLSVVRSLVDNGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKIGPATWAMATSKPDIMIILLSKLMEEGDMFYKKGKVKEAAQRYQYALKKFPREGFGEDLKTFRELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLKEAIKLCPNNREIQRLLMRVEEECRQMQQQQQPPPPPQQPPEELPEEETEPEPQPEDIYSVQDIFEEEYLEQDVENVSIGLQTEARPSQGLPVIQSPPSSPAHRDSAYISSSPLGSHQVFDFRSNSSVGSPTRQGYQSTSPALSPTHQNSHYRPSPPHTSPAHQGASYRFSPPPVGGQGKEYPSPPPSPLRRGPQYRASPPAESMSIYRSQSGSPVRYQQEANVSQLPGRPKSPLSKMAQRPYQMPQLPVAVPQQGLRLQPAKAQIVRSNQPSSAVHSSTVIPTGAYGQVAHPMASKYQSSQGDMGVSQSRLVYQGSIGGIVGDGRPVQHVQASLSAGAICQHGGLTKEDLPQRPSSAYRGGMRYSQTPQIGRSQSASYYPVCHSKLDLERSSSQLGSPDVSHLIRRPISVNPNEIKPHPPTPRPLLHSQSVGLRFSPSSNSISSTANLTPTFRPSSSIQQMEIPLKPAYDRSCDELSPVSPTQGGYPSEPTRSRTTPFMGIIDKTARTQQYPHLHQQNRTWAVSSVDTVLSPTSPGNLSQPESFSPPSSISNIAFYNKTNNAQNGHLLEDDYYSPHGMLANGSRGDLLERVSQASSYPDVKVARTLPVAQAYQDNLYRQLSRDSRQGQTSPIKPKRPFVESNV | null | null | dense core granule cytoskeletal transport [GO:0099519]; in utero embryonic development [GO:0001701]; regulation of dendritic spine development [GO:0060998]; regulation of dendritic spine morphogenesis [GO:0061001] | axon [GO:0030424]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density, intracellular component [GO:0099092] | null | PF12796;PF13181; | 1.25.40.20;1.25.40.10; | TANC family | null | SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000269|PubMed:30021165}. | null | null | null | null | null | FUNCTION: Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines. {ECO:0000269|PubMed:30021165}. | Rattus norvegicus (Rat) |
F1LVW7 | DIAP3_RAT | MEKHRARALGRDSKASRRKGLPSAPPAGPYELGEKRPKLHLNIRTLTDDMLDKFASIRIPKGSKKERPPLPQLKTVSGSSDYSSVSSETMENNPKSLSENEVLKLFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTGSLRSSRQISPQEFIHELKMGYTGERLFTYLESLRVSLTSNPVSWVQNFGHEGLGLLLDILEKLINGQIQEKVVKKTQHKVIQCLRALMNTQYGLERIMSDERSLSLLAKAMDPKQPSMMADVVKLLSAVCIVGEESILEEVLEALTSAGEERKIDRFFSIVEGLRHNSVQLQVACMQLINALVTSPDDLDFRLHLRNEFMRCGLKEILPNLKGIKNDGLDIQLKVFDEHKEEDLSEFSHRFEDIRAEFDEASDVYSVVWDTVKETRAEGHFVSILQHLLLIRNDRFIRQQYFKLIDECVSQIVLHRDGIDPDFTYRKRLDLDLSQFVDVCIDQAKLEEWEEKASEHCKKFEKECTDHQETQAQLQKKEAKINELQAELQAFKSQFGALPPGTKIPLQTSAKGEPGPSAFPPAPPALGAGVPPPPPPPPPPPPPLPGMAMPFGGPVPPPPPLGFLGGQNFIPLNLPFGLKPKKEFKPEISMRRLNWLKIGPNEMSENCFWIKVNENKYENKDLLCKLENTFCCLEKEKRDTNDFDEKKVIKKRMKELKFLDPKIAQNLSIFLSSFRVPYEKIRTMILEVDEAQLSESMIQNLMKHLPDEEQLKSLSQFRSDYNSLCEPEQFAVVMSNVKRLRPRLTAILFKLQFEEQVNNINPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFDLSSLCKLKDTKSADQKTTLLHFLVDVCEEKHPDILPFVDDLAHLDKASRVSVEMLEKSLKQMGRQLLQLEKNLETFPPPEDLHDKFVIKMSSFIITAKEHYGKLSTLLDNMTQLYQSVMSYYAVDTKKVSVEEFFNDLNNFRTSFMQALKENIRKREAAEKEKRARIAKERAEKERLERQQEKKRLLEMKTEGDETGVMDSLLEALQSGAAFRDRRKRTPKLKDIRQSLSPMSQRPVLKVCNHENQKMQLSEGSRPHHSINCTSTRTPVAKELNCNLDTHTSTGRIKAVEKEACNAESNRKKEMELLGSVSKSESVPEVEALLARLRAL | null | null | actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; autophagosome-lysosome fusion [GO:0061909]; cell projection organization [GO:0030030]; chromosome segregation [GO:0007059]; cytoskeleton organization [GO:0007010]; endosomal transport [GO:0016197]; erythrocyte differentiation [GO:0030218]; erythrocyte enucleation [GO:0043131]; establishment of cell polarity [GO:0030010]; gene expression [GO:0010467]; head development [GO:0060322]; in utero embryonic development [GO:0001701]; inner ear receptor cell differentiation [GO:0060113]; integrin-mediated signaling pathway [GO:0007229]; macrophage differentiation [GO:0030225]; microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]; negative regulation of microtubule depolymerization [GO:0007026]; neuron differentiation [GO:0030182]; organelle organization [GO:0006996]; podosome assembly [GO:0071800]; protein-containing complex remodeling [GO:0034367]; sensory perception of sound [GO:0007605]; spermatogenesis [GO:0007283] | actin filament [GO:0005884]; actin filament bundle [GO:0032432]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; ESCRT I complex [GO:0000813]; filamentous actin [GO:0031941]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; ribbon synapse [GO:0097470]; spindle pole [GO:0000922]; stereocilia tip-link density [GO:1990427] | actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267] | PF06367;PF06371;PF02181; | 1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10; | Formin homology family, Diaphanous subfamily | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9Z207}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18651670}. Nucleus {ECO:0000269|PubMed:18651670}. Note=During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis (By similarity). Shuttles between the cytoplasm and the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9NSV4, ECO:0000250|UniProtKB:Q9Z207}. | null | null | null | null | null | FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Required for cytokinesis, stress fiber formation and transcriptional activation of the serum response factor. Binds to GTP-bound form of Rho and to profilin: acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity. {ECO:0000250|UniProtKB:Q9Z207}. | Rattus norvegicus (Rat) |
F1LX07 | S2512_RAT | MAVKVHTTKRGDPHELRNIFLQYASTEVDGEHYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYVEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDVMVTIRSHMLTPFVEENLVSAAGGSTSHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDIEVTKEEFASAITYGVVTPINVGILYFINNVHISTGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIWLQIAESAYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGTGSVVGELMYKNSFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIKLTVNDFVRDKFTRRDGSIPLPAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLQDLGLFGLYKGAKACFLRDIPFSAIYFPVYAHCKLLLADENGHVGGINLLTAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGVTLVTYELLQRWFYIDFGGLKPSGSEPTPKSRIADLPPANPDHIGGYRLATATFAGIENKFGLYLPKFKSPGVAAAQPKVAAAAQ | null | null | aspartate transmembrane transport [GO:0015810]; glutamate biosynthetic process [GO:0006537]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; negative regulation of glucose catabolic process to lactate via pyruvate [GO:1904024]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of myelination [GO:0031643]; response to calcium ion [GO:0051592] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | 3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313] | 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:4436323, ECO:0000305|PubMed:486467}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:4436323}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamate(in) = 3-sulfino-L-alanine(in) + H(+)(out) + L-glutamate(out); Xref=Rhea:RHEA:70967, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:486467}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + L-aspartate(in) = 3-sulfino-L-alanine(in) + L-aspartate(out); Xref=Rhea:RHEA:70975, ChEBI:CHEBI:29991, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:486467}; | null | null | null | null | FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:4436323). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation (PubMed:486467). {ECO:0000269|PubMed:4436323, ECO:0000269|PubMed:486467}. | Rattus norvegicus (Rat) |
F1LXF1 | BCR_RAT | MVDSVGFAEAWRAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQPPDGAAEPRASAPRLPPAPADGADPAPVEESEARPDGEGSPSKGRPATARRPAAAAPADRDDRGPPTSVAALRSNFEKIRKGPAQPGSADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQQSAGQGLGEAPRPHYRGRSSESSCGLDGDYEDAELNPRFLKDNLINANGGNRPPWPPLEYQPYQSIYVGGMMVEGEGKSPLLRSQSTSEQEKRLTWPRRSYSPRSFEDSGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCQKRHRQCQVVVSEATIVGVRKTGQIWPSDGDSTFQGEADSSFGTPPGYGCAADQAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSPASGALEPTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMETAEKCCQANAQFAEISENLRARSNKDVKDSTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPSSHPDHSLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHIFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEALPNIPLVPDEELDALKIKISQIKSDIQREKRANKGSKVMERLRKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRESIREQQKKCFKSFSLTSVELQMLTNSCVKLQTVHHIPLTINKEDDESPGLYGFLHAIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTTEPNWNEEFEIELEGSQTLRILCYEKCYNKMKMAKEDGESADKLMGKGQVQLDPQTLQDRDWQRTVIDMNGIEVKLSVKFTSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKETVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV | 2.7.11.1 | null | actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; cell migration [GO:0016477]; cellular response to lipopolysaccharide [GO:0071222]; definitive hemopoiesis [GO:0060216]; establishment of localization in cell [GO:0051649]; focal adhesion assembly [GO:0048041]; homeostasis of number of cells [GO:0048872]; inner ear morphogenesis [GO:0042472]; intracellular protein transmembrane transport [GO:0065002]; keratinocyte differentiation [GO:0030216]; macrophage migration [GO:1905517]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of cellular extravasation [GO:0002692]; negative regulation of inflammatory response [GO:0050728]; negative regulation of macrophage migration [GO:1905522]; negative regulation of neutrophil degranulation [GO:0043314]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of respiratory burst [GO:0060268]; neuromuscular process controlling balance [GO:0050885]; neutrophil degranulation [GO:0043312]; phagocytosis [GO:0006909]; phosphorylation [GO:0016310]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of phagocytosis [GO:0050766]; regulation of cell cycle [GO:0051726]; regulation of nitrogen compound metabolic process [GO:0051171]; regulation of Rho protein signal transduction [GO:0035023]; regulation of vascular permeability [GO:0043114]; renal system process [GO:0003014]; response to lipopolysaccharide [GO:0032496]; small GTPase-mediated signal transduction [GO:0007264] | axon [GO:0030424]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF09036;PF00168;PF19057;PF00620;PF00621; | 4.10.280.30;2.60.40.150;1.20.900.10;2.30.29.30;1.10.555.10; | null | PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation by HCK is important for interaction with GRB2. {ECO:0000250|UniProtKB:P11274}. | SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000269|PubMed:20962234}. | 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:P11274}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; 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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P11274}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. The amino terminus contains an intrinsic kinase activity (By similarity). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity. Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (By similarity). {ECO:0000250|UniProtKB:P11274, ECO:0000250|UniProtKB:Q6PAJ1}. | Rattus norvegicus (Rat) |
F1LYL9 | SOX9_RAT | MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQAGKVDLKREGRPLAEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVSYTGSYGISSTAPTPATAGHVWMSKQQAPPPPPQQPPQAPQAPQAPPQQQAPPQPQQAPQQQQAHTLTTLSSEPGQSQRTHIKTEQLSPSHYSEQQQHSPQQISYSPFNLPHYNPSYPTITRSQYDYTDHQNSGSYYSHAAGQGSGLYSTFTYMNPAQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP | null | null | anterior head development [GO:0097065]; aortic valve morphogenesis [GO:0003180]; apoptotic process [GO:0006915]; astrocyte fate commitment [GO:0060018]; bone mineralization [GO:0030282]; branching involved in ureteric bud morphogenesis [GO:0001658]; bronchus cartilage development [GO:0060532]; cAMP-mediated signaling [GO:0019933]; canonical Wnt signaling pathway [GO:0060070]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate commitment [GO:0045165]; cell fate specification [GO:0001708]; cell population proliferation [GO:0008283]; cell proliferation involved in heart morphogenesis [GO:0061323]; cell-cell adhesion [GO:0098609]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to heparin [GO:0071504]; cellular response to interleukin-1 [GO:0071347]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system development [GO:0007417]; chondrocyte development [GO:0002063]; chondrocyte differentiation [GO:0002062]; chondrocyte differentiation involved in endochondral bone morphogenesis [GO:0003413]; chondrocyte hypertrophy [GO:0003415]; chromatin remodeling [GO:0006338]; cochlea morphogenesis [GO:0090103]; cytoskeleton organization [GO:0007010]; endocardial cushion morphogenesis [GO:0003203]; endochondral bone morphogenesis [GO:0060350]; endocrine pancreas development [GO:0031018]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation [GO:0050673]; epithelial cell proliferation involved in prostatic bud elongation [GO:0060517]; epithelial to mesenchymal transition [GO:0001837]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; ERK1 and ERK2 cascade [GO:0070371]; extracellular matrix assembly [GO:0085029]; extracellular matrix organization [GO:0030198]; gene expression [GO:0010467]; glandular epithelial cell differentiation [GO:0002067]; glial cell fate specification [GO:0021780]; growth plate cartilage chondrocyte growth [GO:0003430]; hair follicle development [GO:0001942]; Harderian gland development [GO:0070384]; heart development [GO:0007507]; heart valve development [GO:0003170]; heart valve formation [GO:0003188]; heart valve morphogenesis [GO:0003179]; homeostasis of number of cells within a tissue [GO:0048873]; intestinal epithelial cell differentiation [GO:0060575]; intestinal epithelial structure maintenance [GO:0060729]; intrahepatic bile duct development [GO:0035622]; lacrimal gland development [GO:0032808]; limb bud formation [GO:0060174]; lung epithelial cell differentiation [GO:0060487]; lung smooth muscle development [GO:0061145]; male germ-line sex determination [GO:0019100]; male gonad development [GO:0008584]; male sex determination [GO:0030238]; mammary gland development [GO:0030879]; mesenchymal cell apoptotic process [GO:0097152]; mesenchymal cell proliferation [GO:0010463]; metanephric nephron tubule formation [GO:0072289]; metanephric tubule development [GO:0072170]; morphogenesis of a branching epithelium [GO:0061138]; morphogenesis of an epithelium [GO:0002009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of beta-catenin-TCF complex assembly [GO:1904864]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of bone mineralization [GO:0030502]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of gene expression [GO:0010629]; negative regulation of immune system process [GO:0002683]; negative regulation of mesenchymal cell apoptotic process [GO:2001054]; negative regulation of miRNA transcription [GO:1902894]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of photoreceptor cell differentiation [GO:0046533]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell development [GO:0014032]; neuron fate specification [GO:0048665]; Notch signaling pathway [GO:0007219]; notochord development [GO:0030903]; nucleosome assembly [GO:0006334]; oligodendrocyte differentiation [GO:0048709]; ossification [GO:0001503]; otic vesicle development [GO:0071599]; otic vesicle formation [GO:0030916]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell proliferation involved in heart morphogenesis [GO:2000138]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of gene expression [GO:0010628]; positive regulation of kidney development [GO:0090184]; positive regulation of male gonad development [GO:2000020]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of mesenchymal stem cell differentiation [GO:2000741]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prostate gland development [GO:0030850]; prostate gland morphogenesis [GO:0060512]; protein localization to nucleus [GO:0034504]; protein-containing complex assembly [GO:0065003]; regulation of apoptotic process [GO:0042981]; regulation of branching involved in lung morphogenesis [GO:0061046]; regulation of cell adhesion [GO:0030155]; regulation of cell cycle process [GO:0010564]; regulation of cell differentiation [GO:0045595]; regulation of cell population proliferation [GO:0042127]; regulation of cell proliferation involved in tissue homeostasis [GO:0060784]; regulation of epithelial cell proliferation involved in lung morphogenesis [GO:2000794]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; renal vesicle induction [GO:0072034]; response to fatty acid [GO:0070542]; response to organic cyclic compound [GO:0014070]; retina development in camera-type eye [GO:0060041]; retinal rod cell differentiation [GO:0060221]; Sertoli cell development [GO:0060009]; Sertoli cell differentiation [GO:0060008]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; somatic stem cell population maintenance [GO:0035019]; spermatogenesis [GO:0007283]; stem cell proliferation [GO:0072089]; tissue homeostasis [GO:0001894]; trachea cartilage development [GO:0060534]; transcription by RNA polymerase II [GO:0006366]; type I pneumocyte differentiation [GO:0060509]; ureter development [GO:0072189]; ureter morphogenesis [GO:0072197]; ureter smooth muscle cell differentiation [GO:0072193]; ureter urothelium development [GO:0072190] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667] | beta-catenin binding [GO:0008013]; bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; pre-mRNA intronic binding [GO:0097157]; protein kinase A catalytic subunit binding [GO:0034236]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976] | PF00505;PF12444; | 1.10.30.10; | null | PTM: Acetylated; acetylation impairs nuclear localization and ability to transactivate expression of target genes. Deacetylated by SIRT1. {ECO:0000250|UniProtKB:Q04887}.; PTM: Phosphorylation at Ser-64 and Ser-211 by PKA increases transcriptional activity and may help delay chondrocyte maturation downstream of PTHLH/PTHrP signaling. Phosphorylation at either Ser-64 or Ser-211 is required for sumoylation, but phosphorylation is not dependent on sumoylation. Phosphorylated on tyrosine residues; tyrosine dephosphorylation by PTPN11/SHP2 blocks SOX9 phosphorylation by PKA and subsequent SUMOylation. {ECO:0000250|UniProtKB:Q04887}.; PTM: Sumoylated; phosphorylation at either Ser-64 or Ser-211 is required for sumoylation. Sumoylation is induced by BMP signaling pathway. {ECO:0000250|UniProtKB:Q04887}.; PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation and is negatively regulated by DDRGK1. {ECO:0000250|UniProtKB:Q04887}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04887, ECO:0000255|PROSITE-ProRule:PRU00267}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (By similarity). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6 (PubMed:26150426). Also binds to some promoter regions (By similarity). Plays a central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes (By similarity). Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix (By similarity). Controls epithelial branching during kidney development (By similarity). {ECO:0000250|UniProtKB:Q04887, ECO:0000269|PubMed:26150426}. | Rattus norvegicus (Rat) |
F1LYQ8 | FARP1_RAT | MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVLVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDKIVEFHHSHIGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSTRSLVSQPTAPNSEVPKQSPQSASLTFGEGTESPSAQSCQQAKETKVCTLEPGPRQSPALSKSPSGSKAADGTAAAAPPEEEDEEEGGKDGIRPSNPQPPQPSTGSLTGSPHLSELSINSQGGAAPANVTLSPNLSPDNKQASPLISPLLNDQACPRTDDEEEGRRKRFPTDKAYYIAKEVSTTERTYLKDLEVIASWFQSTVSKEDSMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAHIRGDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALETSIKGSRRLEHFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPNHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVIPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEEEWGVPHCLTLRGQRQSIIVAASSRSEMEKWLEDIQMAIDLAEKSNGPTPELLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRSTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDSHPLASLPLLGYSLTIPSESENIHKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRAHSLSHKESHLY | null | null | dendrite morphogenesis [GO:0048813]; enzyme-linked receptor protein signaling pathway [GO:0007167]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; postsynaptic actin cytoskeleton organization [GO:0098974]; Rac protein signal transduction [GO:0016601]; regulation of presynapse assembly [GO:1905606]; retrograde trans-synaptic signaling by trans-synaptic protein complex [GO:0098942]; synapse assembly [GO:0007416] | cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extrinsic component of postsynaptic membrane [GO:0098890]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978] | cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF08736;PF09380;PF00373;PF09379;PF00169;PF00621; | 1.20.80.10;1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000269|PubMed:23209303}. Cytoplasm, cytosol {ECO:0000269|PubMed:23209303}. Cell projection, filopodium {ECO:0000269|PubMed:23209303}. Cell projection, dendrite {ECO:0000269|PubMed:23209303}. Cell projection, dendritic spine {ECO:0000269|PubMed:23209303}. Note=Recruited to the cell membrane via interaction with CADM1. | null | null | null | null | null | FUNCTION: May play a role in semaphorin signaling (By similarity). Functions as a guanine nucleotide exchange factor for RAC1. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses. {ECO:0000250, ECO:0000269|PubMed:23209303}. | Rattus norvegicus (Rat) |
F1LZW6 | S2513_RAT | MAAAKVALTKRADPAELKAIFLKYASIEKNGEFFMSPHDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVRQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNAKTGKVTAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTRSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGSRKDVEVTKEEFALAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGMLPFNLAEAQRQQKASGDAARPFLLQLAESAYRFGLGSIAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLTVNDFVRDKFMHKDGSVPLLAEIFAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVTDCFRKILREEGPKALWKGAGARVFRSSPQFGVTLLTYELLQRWFYVDFGGVKPVGSELVPKSRITLPAPNPDHVGGYKLAVATFAGIENKFGLYLPLFKPSASTSKVTAVGS | null | null | aspartate transmembrane transport [GO:0015810]; ATP biosynthetic process [GO:0006754]; cellular respiration [GO:0045333]; gluconeogenesis [GO:0006094]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | 3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313] | 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:4436323, ECO:0000305|PubMed:486467}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:4436323}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamate(in) = 3-sulfino-L-alanine(in) + H(+)(out) + L-glutamate(out); Xref=Rhea:RHEA:70967, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:486467}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + L-aspartate(in) = 3-sulfino-L-alanine(in) + L-aspartate(out); Xref=Rhea:RHEA:70975, ChEBI:CHEBI:29991, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:486467}; | null | null | null | null | FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:4436323). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation (PubMed:486467). {ECO:0000269|PubMed:4436323, ECO:0000269|PubMed:486467}. | Rattus norvegicus (Rat) |
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