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
|
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B1AS29 | GRIK3_MOUSE | MTAPWRRLRSLVWEYWAGFLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQSLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWAMERLQAAPRAESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRTLTADYALLMESTTIEYITQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFIYKLRKTAEREQRSFCSTVADEIRFSLTCQRRLKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMSCSTSLAPVFP | null | null | modulation of chemical synaptic transmission [GO:0050804]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; regulation of membrane potential [GO:0042391]; synaptic transmission, glutamatergic [GO:0035249] | axon [GO:0030424]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; glutamatergic synapse [GO:0098978]; kainate selective glutamate receptor complex [GO:0032983]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; terminal bouton [GO:0043195] | adenylate cyclase inhibiting G protein-coupled glutamate receptor activity [GO:0001640]; glutamate receptor activity [GO:0008066]; glutamate-gated receptor activity [GO:0004970]; kainate selective glutamate receptor activity [GO:0015277]; ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099507]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF01094;PF00060;PF10613; | 1.10.287.70;3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, GRIK3 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Receptor for glutamate that functions as a ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1ATG9 | TIKI2_MOUSE | MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRHPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTHVYFELDLTDPYTISALASCQLLPHGENLQDVLPRELYWRLKRHLDYVKLMIPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTETDVRSRGVPVLDLYLAQQAEKMKKSTGAVERVEEQCHPLNGLNFSQVLFALNQTLLQHESVRAGSLQAPYTTEDLIKHYNCGDLNAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLQENQDKICFFAFGAGHFLGNNTVIDVLRQAGLEVDHTPAGQAIHGPAAVGSPAPPPEITSPASPAPATPAAAVPEATSATPTTPPEEEDPVLSPHLLLPDSLSQLEEFGRQKWRKRLNKHQRPRQFNDLWVRIEDSTTISPPPLPLQPTPSSETTKPFVKSSHQLQQQDAVGPTSSSAPTLGLLHAITASIVAPFLLHSLGPS | 3.4.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000250}; | negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of protein oxidation [GO:1904808]; positive regulation of protein-containing complex assembly [GO:0031334]; proteolysis [GO:0006508]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; Wnt-protein binding [GO:0017147] | PF01963; | null | TIKI family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23152936}; Single-pass type I membrane protein {ECO:0000269|PubMed:23152936}. | null | null | null | null | null | FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1AUH1 | PTPRU_MOUSE | MARAQALVLALTFQFCAPETETPAAGCTFEEASDPVVPCEFSQAQYDDFQWEQVRIHPGTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDHKGYIGLDDILLFSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPTRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCYRYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLILTNPEGRKEGKEVTFQTDEDVPGGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVVVEEERPRRLRREPGAQDCFSVPLTFETALARGLVHYFGAELAASSLLEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLILGICAGGLAVLILLLGAIIVIIRKGRDRYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDAPGYSPRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALELR | 3.1.3.48 | null | animal organ regeneration [GO:0031100]; cell differentiation [GO:0030154]; dephosphorylation [GO:0016311]; homotypic cell-cell adhesion [GO:0034109]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; protein localization to cell surface [GO:0034394]; response to glucocorticoid [GO:0051384] | cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | beta-catenin binding [GO:0008013]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF00629;PF00102; | 2.60.120.200;2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2B subfamily | PTM: The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cell 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: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1AVY7 | KI16B_MOUSE | MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAANPLVKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINEDANVKLIRELRAEIARLKTLLAQGNQIALLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDGVQRPHHGILEGQAVLSSLPPSGGNSHLAPLMDARISAYIEEEVQRRLHDLHRAIGDANHTPADVMKSNEELHNGTTQRKLKYERMYSRSLGTNRDDLKDPIKISIPRYVLCGQGKDEHFEFEVKISVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVVAERRTHLEKYLREFFSVMLQSETSPLHINKVGLTLSKHTICEFSPFFKKGVFDYSSHGTG | null | null | cellular response to type II interferon [GO:0071346]; early endosome to late endosome transport [GO:0045022]; endoderm development [GO:0007492]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; formation of primary germ layer [GO:0001704]; Golgi to endosome transport [GO:0006895]; microtubule-based movement [GO:0007018]; receptor catabolic process [GO:0032801]; regulation of receptor recycling [GO:0001919] | cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; phagocytic vesicle [GO:0045335]; spindle [GO:0005819] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; plus-end-directed microtubule motor activity [GO:0008574]; small GTPase binding [GO:0031267] | PF00498;PF00225;PF00787; | 2.60.200.20;3.40.850.10;3.30.1520.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96L93}. Early endosome membrane {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm {ECO:0000250|UniProtKB:Q96L93}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96L93}. Note=It is unclear whether association with endosomes is mediated via phosphatidylinositol 3-phosphate (PtdIns(3)P)-binding or via its interaction with RAB14. {ECO:0000250|UniProtKB:Q96L93}. | null | null | null | null | null | FUNCTION: Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. {ECO:0000269|PubMed:21238925}. | Mus musculus (Mouse) |
B1AWL2 | ZN462_MOUSE | MEVLQCDGCDFRAPSYEDLKAHIQDVHTAFLQPTDVAEDNDDEPLSGSMNASNQTEVEFSSIKDEFVIAEDLPGQSATALGSGGYYGHSPGYYGQHITPNPKPTNKFFQCKFCVRYFRSKNLLIEHTRKVHGAQAEESPTGPPVPGSLNYNIMMHEGFGKVFSCQFCTYKSPRRARIIKHQKMYHKNSLKESTAPPPAPAPLPDPLVPPVSLQDPCKELPAEVVERSILESMVKPLTKSRGNFCCEWCSYQTPRRERWCDHMMKKHRSMVKILSSIRQQEGPNVSEAQNDNEPSPTSNSTYLSMNAASREMPNANVSNFRGSMGNSIMRPNSSSTSKFSSSMSYPQMKPKSPHNSGLVNLTERSRYGMSDMTNSSADLDTNSMLNDSSSDEDLNEVDSENGLSVLDHQASGLSAEQLMGSDGNKLLETKGIPFRRFMNRFQCPFCPFLTMHRRSISRHIENIHLSGKTAVYKCDECPFTCKSSLKLGAHKQCHTGTSDWDTVNSQSESLSSSLNEGMVSYESSSINGRKSGVMLDPLQQQQPPQPPPPLPPPPPPPSQPLPQPPPPPLQSPHQVPPPTQQPQPPTQAPPLHPYKCTMCSYSTMTLKGLRVHQQHKHSFCDNLPKFEGQPSSLPLENETDSHPSSSNTVKKSQTSILGLSSKNNFVAKANRKLASDFPLDLSPVKKRTRIDEIASNLQSKINQTKLQEDAIINVEDDEEEEDDNEVEIEVELDREEEATDPIMEVPTAFSAQQIWARDASEAQKEPNYRSITHDYTATNGAEIELTLSEDEEDYYGSSASMKDQVSNAALLNTQPAIYGTEPSNENTDFGDSGRLYYCKHCDFNNKSARSVSTHYQRMHPYIKFSFRYILDPNDHSAVYRCLECYIDYTNFEDLQQHYGEHHPEAMNVLNFDHSDLIYRCRFCSYTSPNVRSLMPHYQRMHPTVKINNAMIFSSYVVEQQEGLNAESQTLREILNSAPKSMATSTPVARGGGLPATFNKNTPPKTFTPECESQKDPSVNTVVVYDCDVCSFASPNMHSVLVHYQKKHPEEKASYFRIQKTMRMVSVDRGSALSQLSFEVGAPMSPKMSNMGSPPPPQPPPPDLSIELYYCKHCSYSNRSVVGVLVHYQKRHPEIKVTAKYIRQAPPTAAMMRGAEGLQDSPRPPAPLQLNSSERDCPPVETEMFFCQHCDYGNRTVKGVLIHYQKKHRDFKANADVIRQHTATIRSLCDRNQKPASCVLLPASGMERDKTKLRALKCRQCSYTSPYFYALRKHIKKDHPALKATVTSIMRWAFLDGLIEAGYHCEWCIYSHMEPSGLLLHYQRRHPEHYVDYTYMATKLWAGPDPSSPTLTMSAEAKTYRCRDCVFEAVSIWDITNHYQAFHPWAMNGDESVLLDIIKEKDGVDKALLAPEELIGPVNCENSIPNPLPEQEAECPEDARLSPEKSIHLASANPAISSTPYQCTVCQSEYNNLHGLLTHYGKKHPGMKVKAADFAQDIDINPGAVYKCRHCPYINTRIHGVLTHYQKRHPAIKVTAEDFVHDVEQSADISQNDVEETSRIFKQGYGAYRCKLCPYTHGTLEKLKIHYEKYHNQPEFDVFSPPPPKLPVSLEPEITTEVSPSQVSVTEEEVGEDPMSTAHFSTSHLVSHTVFRCQLCKYFCSTRKGIARHYRIKHNNVRAQPEGKNNLFKCALCAYTNPIRKGLAAHYQKRHDIDAYYTHCLAASRTISDKPNKVIIPSPPKDDSPQLSEELRRAVEKKKCSLCSFQSFSKKGIVSHYMKRHPGVFPKKQHASKLGGYFTAVYADEHEKPPLMEEEERSSFERAEVEGEAQDIEWLPFRCIKCFKLSFSTAELLCMHYTDHHSRDLKRDFVILGSGPRFQNSTFQCKHCDSKLQSIAELTSHLNIHNEEFQKRAKRQERRKQLLSKQKYADGAFADFKQERPFGHLEEVPKIKERKVVGYKCKFCVEVHPTLRAICNHLRKHVQYGSVPAVSAAVKGLRSHERSHLALAMFTREDKYSCQYCSFVSAFRHNLDRHMQTHHGHHKPFRCKLCSFKSSYNSRLKTHILKAHAGEHAYKCSWCSFSTMTISQLKEHSLKVHGKALTLPRPRIVSLLSSHAHPSSQKATPAEEVEDSNDSSYSEPPDVQQQLNHYQSAALARNKSRVSPVPPSGTAAGTEQKAEAVLHCEFCEFSSGYIQSIRRHYRDKHGGKKLFKCKDCSFYTGFKSAFTMHVEAGHSAVPEEGPKDLRCPLCLYHTKYKRNMIDHIVLHREERVVPIEVCRSKLSKYLQGVVFRCDKCTFTCSSDESLQQHIEKHNELKPYKCQLCYYETKHTEELDTHLRDEHKVSRNFELVGRVNLDQLEQMKEKIESSSSEDEDKDDEMSSKAEDRELMRFADRGPGVNTEKRFPCEFCGRAFSQGSEWERHVLRHGMSLHDTNQVSRNEIHTKEMVEESMQLPSIEAKEDDEPIGIDFPLKSETVTICVVAADKSLLEDAEAKNE | null | null | chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | null | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965}. | null | null | null | null | null | FUNCTION: Zinc finger nuclear factor involved in transcription by regulating chromatin structure and organization (PubMed:20219459, PubMed:21570965). Involved in the pluripotency and differentiation of embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG (PubMed:21570965). By binding PBX1, prevents the heterodimerization of PBX1 and HOXA9 and their binding to DNA (PubMed:17353115). Regulates neuronal development and neural cell differentiation (PubMed:21570965, PubMed:27621227). {ECO:0000269|PubMed:17353115, ECO:0000269|PubMed:20219459, ECO:0000269|PubMed:21570965, ECO:0000269|PubMed:27621227}. | Mus musculus (Mouse) |
B1AWN4 | AT10B_MOUSE | MTCSLDFSWLRWKWRTQDGFSQSPSETTPLLSPETDRQSHNTAEQRVVYPNNSMCHQDWKKVCRRYPGNSICTTKYTLLTFLPQNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITIFPLATVLLIIMVKDGIEDFKRYCFDREMNSASIQIYERKEQRYMLKRWQDVRVGDFVQMQCNEIVPADILLLFSSDPSGVCHLETANLDGETNLKQRRVVKGFSQPEVQFQPEHFHSTIVCEKPNNHLSKFKGYMEHPDQTRTGFGSESLLLRGCTIRNTEVAAGIVIYAGHETKAMLNNSGPRYKRSKIERRINTDIFFCIGLLFLMCLIGAVGHSLWNGTFKEHPPFDVPDADGNFLSLALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFLLHNDLDLYDEETDLSIQCRALNITEDLGQIQYIFSDKTGTLTENKMVFRRCTIVGSEYCHQENAKRLEMPKELDSDGEEWTQYQCLSFPPRWAQGSTTMRSQGGAQPLRRCHSARVPIQSHCRQRSVGRWETSQPPVAFSSSIEKDVTPDKNLLSKVRDAALWLETSDTRPAKPSHSTTASIADFFLALTICNSVMVSTTTEPRKRVTTPPANKALGTSLEKIQQLFQRLKLLSLSQSFSSTAPSDTDLGESLGPNLPTIDSDEKDDTSVCSGDCSTDGGYRSSTWEQGDILGSESGTSLEEGLEAPTLSQDEPELCYEAESPDEAALVHAARAYSFTLVSRTPEQVTVRLPQGICLTFDLLFTLGFDSVRKRMSVVVRHPLTDEIIVYTKGADSVIMDLLEDPACESNIDVEKKLKRIRARTQKHLDLYARDGLRTLCIAKKVVDEEDFQRWASFRREAEASLDNREELLMETAQHLENHLTLLGATGIEDRLQEGVPDTIAALREAGIQLWVLTGDKQETAVNIAYSCKLLDQTDTVYSINTENQETCESILNCTLEDIKRFHEPQQPARKLCGHRIPPKMPSVNSGAMAPEIGLVIDGKTLNAIFQGKLENKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLSVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAIARFSHLKKLLLVHGHWCYSRLARMVVYYFYKNVCYVNLLFWYQFFCGFSGSTMIDYWQMIFFNLFFTSLPPIIFGVLDKDVSAETLLALPELYKSGQNSECYNLPTFWVSMADAFYQSLICFFIPYLTYRGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTVLHGLVLLGSFLMYFVVSLIYNATCVTCNSPTNPYWVMERQLSDPTFYLICLLTPVVALLPRYFLLSLQGTYGKSLISKAQKIDKLPIDKRNLEIQNWRSKQRPAPASASASASAPATGTVHTRPPCHPVPPEAQQNFGASTSKSSGPPRQKHVEDRVLQDPRCSREHSRDDTCTVDTLAKLSSGECLLDPNRTVAPTAYSRGQKDVSRHSSKGSHRRSQSSLTI | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | lysosomal membrane organization [GO:0097212]; phospholipid translocation [GO:0045332] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345] | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000250|UniProtKB:O94823}. | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O94823}; Multi-pass membrane protein {ECO:0000255}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. {ECO:0000250|UniProtKB:O94823}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O94823}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O94823}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000250|UniProtKB:O94823}; | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes (By similarity). Plays an important role in the maintenance of lysosome membrane integrity and function in cortical neurons (PubMed:32172343). {ECO:0000250|UniProtKB:O94823, ECO:0000269|PubMed:32172343}. | Mus musculus (Mouse) |
B1AWN6 | SCN2A_MOUSE | MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTMNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFKGRVKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGPSALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSMASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYLLKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK | null | null | cellular response to hypoxia [GO:0071456]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; intrinsic apoptotic signaling pathway in response to osmotic stress [GO:0008627]; membrane depolarization during action potential [GO:0086010]; memory [GO:0007613]; nerve development [GO:0021675]; nervous system development [GO:0007399]; neuron apoptotic process [GO:0051402]; neuronal action potential [GO:0019228]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814] | axon [GO:0030424]; axon initial segment [GO:0043194]; glutamatergic synapse [GO:0098978]; intercalated disc [GO:0014704]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; T-tubule [GO:0030315]; voltage-gated sodium channel complex [GO:0001518] | calmodulin binding [GO:0005516]; leucine zipper domain binding [GO:0043522]; sodium channel activity [GO:0005272]; sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.2/SCN2A subfamily | PTM: Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases voltage-gated sodium current and mediates the early response to acute hypoxia in neurons. Sumoylated SCN2A is located at the cell membrane. {ECO:0000250|UniProtKB:P04775}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827969}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10827969, ECO:0000269|PubMed:11166117, ECO:0000269|PubMed:28137877}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:10827969, PubMed:11166117, PubMed:28137877). Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory (PubMed:29867081). {ECO:0000269|PubMed:10827969, ECO:0000269|PubMed:11166117, ECO:0000269|PubMed:28137877, ECO:0000269|PubMed:29867081}. | Mus musculus (Mouse) |
B1AXD8 | AKIR2_MOUSE | MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPASAAASPAAATAAAAASAAAASPQKYLRMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLEASFQQADPGCTSDSQPHAFLISGPASPGTSSATSSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYDAFVKFTHDQIMRRYGEQPASYVS | null | null | adaptive immune response [GO:0002250]; cerebral cortex development [GO:0021987]; defense response to bacterium [GO:0042742]; embryo development ending in birth or egg hatching [GO:0009792]; innate immune response [GO:0045087]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nuclear protein quality control by the ubiquitin-proteasome system [GO:0071630]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of B cell activation [GO:0050871]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of innate immune response [GO:0045089]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome localization [GO:0031144]; protein import into nucleus [GO:0006606]; regulation of muscle cell differentiation [GO:0051147]; response to lipopolysaccharide [GO:0032496] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; transcription coregulator activity [GO:0003712] | null | null | Akirin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25107474, ECO:0000269|PubMed:30116001, ECO:0000269|PubMed:30801883}. Cytoplasm {ECO:0000269|PubMed:30801883}. Membrane {ECO:0000269|PubMed:30801883}. Note=Present mainly in the nuclear fraction, and at much lower level in the cytoplasmic and membrane fractions. {ECO:0000269|PubMed:30801883}. | null | null | null | null | null | FUNCTION: Molecular adapter that acts as a bridge between a variety of multiprotein complexes, and which is involved in embryonic development, immunity, myogenesis and brain development (PubMed:25107474, PubMed:26041538, PubMed:27871306, PubMed:30116001, PubMed:30801883). Plays a key role in nuclear protein degradation by promoting import of proteasomes into the nucleus: directly binds to fully assembled 20S proteasomes at one end and to nuclear import receptor IPO9 at the other end, bridging them together and mediating the import of pre-assembled proteasome complexes through the nuclear pore (By similarity). Involved in innate immunity by regulating the production of interleukin-6 (IL6) downstream of Toll-like receptor (TLR): acts by bridging the NF-kappa-B inhibitor NFKBIZ and the SWI/SNF complex, leading to promote induction of IL6 (PubMed:18066067, PubMed:25107474). Also involved in adaptive immunity by promoting B-cell activation (PubMed:26041538). Involved in brain development: required for the survival and proliferation of cerebral cortical progenitor cells (PubMed:27871306). Involved in myogenesis: required for skeletal muscle formation and skeletal development, possibly by regulating expression of muscle differentiation factors (PubMed:30801883). Also plays a role in facilitating interdigital tissue regression during limb development (PubMed:30116001). {ECO:0000250|UniProtKB:Q53H80, ECO:0000269|PubMed:18066067, ECO:0000269|PubMed:25107474, ECO:0000269|PubMed:26041538, ECO:0000269|PubMed:27871306, ECO:0000269|PubMed:30116001, ECO:0000269|PubMed:30801883}. | Mus musculus (Mouse) |
B1AY10 | NFX1_MOUSE | MAEAPPVSGTFKFNTDAAEFIPQERKTSGLNCGTQRRLDSSRIGRRNYSSSPPCHLPRHIPYEDISAVHQHSYASGSKPKSPQGFFQSSNKSLKNHGLQNQPWQKARNEKHQNRNKKAQGLSEQTSDTSSLESVARSESGTNPREHSPSESEKEVVIADPRGAKPKKAAQLTYNYGRGPKAKGRLRSEWGNRMSPKSEDENTRPVAISHTDSSDASCRKPVVDPCVCRRNEQRRYPQKRPPWEVEGARPRPGRNPPKQESQRHINAGPKTNMSPIPKDNLRERPTKSACDTGNLAVVSKSSRRVNQEKTAVRRQDPQVLSPFPRGKQNHMLKNVETHTGSLIEQLTTEKYECMVCCELVQVTAPVWSCQSCFHVFHLNCIKKWARSPASHADGQSGWRCPACQNVSAHVPNTYTCFCGKVKNPEWSRNEIPHSCGEVCRKKQPGQDCPHSCNLLCHPGPCPPCPAFTTKTCECGRTRHTVRCGQPVSVHCSNACENILNCGQHHCAELCHGGQCQPCRIILNQVCYCGSTSRDVLCGTDVGKSDGFGDFSCLKICGKDLKCGSHTCSQVCHPQPCQPCPRLPHLVRYCPCGQTPLSQLLEHGSNARKTCMDPVPSCGKVCGKPLACGSSDFIHTCEKLCHEGDCGPCSRTSVISCRCSFRTKELPCTSLKSEDATFMCDKRCNKKRLCGRHKCNEICCVDKEHKCPLICGRKLRCGLHRCEEPCHRGNCQTCWQASFDELTCHCGASVIYPPVPCGTRPPECTQTCARIHECDHPVYHSCHSEEKCPPCTFLTQKWCMGKHELRSNIPCHLVDISCGLPCSAMLPCGMHKCQRLCHKGECLVDEACKQPCTTPRGDCGHPCMAPCHPSLPCPVTACKAKVELQCECGRRKEMVICSEASGTYQRIVAISMASKITDMQLGDSVEISKLITKKEVQQARLQCDEECAALERRKRLAEAFDITDDSDPFNVRSSASKFSDSLKDDARKDLKFVSDVEKEMETLVEAVNKGKNNKKSHCFPPMNRDHRRIIHDLAQVYGLESISYDSEPKRNVVVTAVRGKSVCPPTTLTSVIERETQTRPPPPIPHHRHQADKAPGSSTLQKIVKEAVIDYFDVQD | 2.3.2.- | null | negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein autoubiquitination [GO:0051865] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01424;PF01422; | 3.30.1370.50; | NFX1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Together with PABPC1 or PABPC4, acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269|PubMed:12047746}. | Mus musculus (Mouse) |
B1AY15 | UBP51_MOUSE | MRGTQGAQEMKPELWPEPKPTSENLTSRGSGSYEKVLPSIPAACHTSSSSVCPRRKPRPRPQPRSRSRGGRGLKAPPPPPAKPPPPPPAPPPPPLPKQRSVAWRNSRRRSRPGPRPQTRKSYSSDHGSSRDSDGSENSLLEVGSNKGPTGCCHVESFKVAKNWQRNLRMIYQRFIWSGTPETRKRKAKSCICQICSTHKNRLHSCLSCVFFGCFTDKHIHIHAETTQHNLAVDLCHGVIYCFMCRDYVYDKDIEKIAKETKEKILGLLSSPTGDASYQQLMASEVEENQLTCESKDQETSLVKPKKKRRKKTMYYTVGFRGLINLGNTCFMNCIVQVLTHIPLLKEFFLSNKHKCMMTSPSLCLVCEMSLLFQAMYSGNQSPHIPYKLLHLIWIHAEHLAGYRQQDAQEFLIAILDVLHRHSRDDGIDQEGNSNCCNCIIDHIFTGSLQSDLTCQVCHGVSTTIDPCWDISLDLPGPYTPGRASSSTSSRDGQKPRVISLTDCLKWFTRPEDLGSSAKIKCSQCQSYQESTKQLTMKKLPIVACFHLKRFEHLGKQRRKINSFISFPLELDMTPFLASTKESIMKGQPLTECVPSENKYSLFAVINHHGTLESGHYTSFVRQEKDQWFSCDDAVVTKATMEELLNSEGYLLFYHRQDIEKE | 3.4.19.12 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; proteolysis [GO:0006508]; regulation of cell cycle process [GO:0010564]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of double-strand break repair via nonhomologous end joining [GO:2001032] | chromosome [GO:0005694] | chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843]; histone binding [GO:0042393]; histone H2A deubiquitinase activity [GO:0140950]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q70EK9}. Note=Dissociates from chromatin immediately after DNA damage and reassociates with chromatin following DNA repair. {ECO:0000250|UniProtKB:Q70EK9}. | 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:27083998}; | null | null | null | null | FUNCTION: Specifically deubiquitinates 'Lys-14' (H2AK13Ub) and 'Lys-16'(H2AK15Ub) of histone H2A regulating the DNA damage response at double-strand breaks (DSBs). USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1 (PubMed:27083998). Functions in DNA double-strand break repair also by mediating the deubiquitination and subsequent stabilization of DGCR8, leading to the recruitment of DGCR8 binding partners to double strand breaks such as RNF168 or MDC1. In addition, promotes the deubiquitination and stabilization of the transcriptional repressor ZEB1. {ECO:0000250|UniProtKB:Q70EK9, ECO:0000269|PubMed:27083998}. | Mus musculus (Mouse) |
B1AYL1 | SCN7A_MOUSE | MLTSPEPKGLVPFTTESLELIENHIAKKCNEDPEEEEGLKPSRNLEAGKRLPIPYGTLPRGTVSEPLEDVDPYYYVKRNTFMVLNRSRVIFRFNAVSIFCTLSPLNSLRRAAIKALVHPLFRLLILISVLTDSILMCMSNLPEWILAIENTLLGIYAFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRFSPLSSFLMLKTIRTFRILKIIPLNHGLQSIVMTLAQCLKKLFGAIALALFFLAVFSLLGMGLFMGNLKHKCLRWPEENENETLHNRTGSLNYSPERINFYYMEGAKYALLCGNRTDAGQCPEGYVCVKEGTNPDNGFTSFDNFGWSLLAMFRLMTQDYPELLYHQILYASGKVYMIFFVMISFWFAFYLTSLFLGILTMTYEKEKQRACEESGGLDPKCQQTVKELDEENDAAEMETTQIEMKKRSPTSINTTLDILEDTTLGHREEPETSRKKCPICWHKFIKTCFIWKCSPCWVKLNEFADRVITHPLADLFLVICIVLNICFLALEHFPMSEELRSLLHVGNLVFIGIYTIEMILKIIAMHPYGYFQISWNIFDSILVVLELTEILLADVEGLAVLITVPLIFIKLGKYGPPFKSLMRILGSSLMALKDLVLLLCIFVYFSAVFGMKLFGRSYKDCVCHIKEDCQPQRWHMSDFLHAYMTVFRILCGEWIETLWECMEVAGQAWCIPFYMMVILIGNLLILYLFVTLVSSFSYYDATSEVNKEAKNLQLAMARIKSGINSMLLKLMCTERSVPTEATDQICDPSVKENISGHTLSELSNTQTFLRYKDQSSSTEKTPVTESESQSLIASPSASETVPIASGESDIENLDNKETRSKSGNGGSKEKMKQSSSSECSTVDIAISEEEEMVYEHEKSKLHKNGYERKSSTGQISRESRNGKIWKNIRKTCCKIVENSWFECFIGLVTLLCTGTLALEDIYIDQRKTTKILLEYADMIFAYIFILEMLLKWVAYGFKAFFSNNWYKLDFMVVIVFCLSLIGKTREDLNPLTSIKFLRALRVLSQFERMKVVLRALIKTTLPTVSVFLVCLMIWLLFSVIGVQLFAGKFYECIDPTKGERFPVFEVMNKSQCEKLLFNESMPWENAKLNFDNVGNGFLSLLQVATFNGWISIMNSAIDSVGVNMQPSFEYNLYMYSYFIIFVIFGLFLPLCMLIGVIIRNFNKQKIKQGGSNIFITVKQKKQYRALKKLLYADVQKPTPRPRNKFQGFLFDLVTHRVFNVIIILLICFQATTIMIQKDEQSPQMETAIFWMNSIFVMLFTLECILKLTAFRCHYFTSAWNVHDFMVVIFSITGLLLPLTIGQYFVPPSLVQLILLSRVIHILRPGKGPKVFHDLMLPLILALPALLNISLLIFLVMFIYAIFGMYNFAYVKKEAGINDVSNFETFGSSMLCLFQVTTFSGWDGMLDAIFNSQWSDCDPDKINPGTQVKGDCGSPSVGISYFVSYILISWLIIVNMYIVLIMEFLSIPSQKKSRTLSEDDFRRFFRVWNRFDPDRTQYIDSSKLSDFAAALDPPLFMAKPNKGQLVAMDLPMAAGDRIHCLDILLAFTKRVMGKDERVEKILSEIESGFMLANPFKITYEPITTTLKRKQEAVSATIIQRAYKSYRLRQNDKNVSDTPAIDDRRDDLTSKGAHSGKIEEKASIQTQI | 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] | 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:0000269|PubMed:17408578}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:11992118, ECO:0000269|PubMed:17408578}; | 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:11027237, PubMed:11992118, PubMed:17408578, PubMed:27252474). 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 (PubMed:11027237, PubMed:17408578, PubMed:27252474). By mediating sodium influx into keratinocytes, also plays a role in skin barrier homeostasis (By similarity). {ECO:0000250|UniProtKB:Q01118, ECO:0000269|PubMed:11027237, ECO:0000269|PubMed:11992118, ECO:0000269|PubMed:17408578, ECO:0000269|PubMed:27252474}. | Mus musculus (Mouse) |
B1AZ99 | OTUD3_MOUSE | MSRKQAAKSRPGSGGRRAEAERKRDERAARRALAKERRNRPDPGGSGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLSKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAPAHLLTDFQMLHQDGANKKEKMKTKGVDVKDGLRDDVEDAVHKVGSATGCTDFNLIVQNLEAENYNIKSAITALLQVNQGTGNDAEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGRMETSEARASPAEESKAHKSQLPKVTNKQRREQQRLEKKKRQEERHRLKALENRNGSRDTGRSEADMNTQVTLVKTFAALNI | 3.4.19.12 | null | cellular response to nutrient levels [GO:0031669]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; protein K11-linked deubiquitination [GO:0035871]; protein K6-linked deubiquitination [GO:0044313]; protein stabilization [GO:0050821]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843] | PF02338; | 3.90.70.80; | null | PTM: Glucose and fatty acids stimulate CREBBP-dependent acetylation, promoting its nuclear translocation. {ECO:0000269|PubMed:35675826}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35675826}. Nucleus {ECO:0000269|PubMed:35675826}. Note=Glucose or fatty acid promote nuclear translocation upon acetylation. {ECO:0000269|PubMed:35675826}. | 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:0000305|PubMed:35675826}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin (PubMed:35675826). Also hydrolyzes heterotypic (mixed and branched) and homotypic chains (PubMed:35675826). Important regulator of energy metabolism (PubMed:35675826). Glucose and fatty acids trigger its nuclear translocation by CBP-dependent acetylation (PubMed:35675826). In the nucleus, deubiquitinates and stabilizes the nuclear receptor PPARD regulating the expression of various genes involved in glucose and lipid metabolism and oxidative phosphorylation (PubMed:35675826). Also acts as a negative regulator of the ribosome quality control (RQC) by mediating deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby antagonizing ZNF598-mediated 40S ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q5T2D3, ECO:0000269|PubMed:35675826}. | Mus musculus (Mouse) |
B1AZI6 | THOC2_MOUSE | MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGNLKHEQASSVLNDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSDTVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELGQDLSGNITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCEPQTLCHILGFKFKFYQEPSGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEYKREIVEAKQIVRKLTMVVLSSEKLDERDKEKDKDDEKVEKPPDNQKLGLLEALLKVGDWQHAQNIMDQMPPYYAASHKLIALAICKLIHITVEPLYRRVGVPKGAKGSPVSALQNKRAPKQVESFEDLRRDVFNMFCYLGPHLSHDPILFAKVVRIGKSFMKEFQSDGSKQEDKEKTEVILSCLLSITDQVLLPSLSLMDCNACMSEELWGMFKTFPYQHRYRLYGQWKNETYNGHPLLVKVKAQTIDRAKYIMKRLTKENVKPSGRQIGKLSHSNPTILFDYILSQIQKYDNLITPVVDSLKYLTSLNYDVLAYCIIEALANPEKERMKHDDTTISSWLQSLASFCGAVFRKYPIDLAGLLQYVANQLKAGKSFDLLILKEVVQKMAGIEITEEMTMEQLEAMTGGEQLKAEGGYFGQIRNTKKSSQRLKDALLDHDLALPLCLLMAQQRNGVIFQEGGEKHLKLVGKLYDQCHDTLVQFGGFLASNLSTEDYIKRVPSIDVLCNEFHTPHDAAFFLSRPMYAHHISSKYDELKKSEKGSKQQHKVHKYITSCEMVMAPVHEAVVSLHVSKVWDDISPQFYATFWSLTMYDLAVPHTSYEREVNKLKVQMKAIDDNQEMPPNKKKKEKERCTALQDKLLEEEKKQMEHVQRVLQRLKLEKDNWLLAKSTKNETITKFLQLCIFPRCIFSAIDAVYCARFVELVHQQKTPNFSTLLCYDRVFSDIIYTVASCTENEASRYGRFLCCMLETVTRWHSDRATYEKECGNYPGFLTILRATGFDGGNKADQLDYENFRHVVHKWHYKLTKASVHCLETGEYTHIRNILIVLTKILPWYPKVLNLGQALERRVNKICQEEKEKRPDLYALAMGYSGQLKSRKSHMIPENEFHHKDPPPRNAVASVQNGPGGGTSSSSIGNASKSDESGAEETDKSRERSQCGTKAVNKASSTTPKGNSSNGNSGSNSNKAVKENDKEKVKEKEKEKKEKTPATTPEARALGKDSKEKPKEERPNKEDKARETKERTPKSDKEKEKFKKEEKAKDEKFKTTVPIVESKSTQEREREKEPSRERDVAKEMKSKENVKGGEKTPVSGSLKSPVPRSDISEPDREQKRRKIDSHPSPSHSSTVKDSLIDLKDSSAKLYINHNPPPLSKSKEREMDKKDLDKSRERSREREKKDEKDRKERKRDHSNNDREVPPDITKRRKEENGTMGVSKHKSESPCESQYPNEKDKEKNKSKSSGKEKSSSDSFKSEKMDKISSGGKKESRHDKEKIEKKEKRDSSGGKEEKKHHKSSDKHR | null | null | blastocyst development [GO:0001824]; cell morphogenesis [GO:0000902]; generation of neurons [GO:0048699]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; negative regulation of neuron projection development [GO:0010977]; neuron development [GO:0048666]; poly(A)+ mRNA export from nucleus [GO:0016973]; regulation of gene expression [GO:0010468]; regulation of mRNA export from nucleus [GO:0010793]; RNA splicing [GO:0008380]; stem cell division [GO:0017145] | chromosome, telomeric region [GO:0000781]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; THO complex part of transcription export complex [GO:0000445] | mRNA binding [GO:0003729] | PF11262;PF11732;PF16134; | null | THOC2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as a component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development. {ECO:0000250|UniProtKB:Q8NI27}. | Mus musculus (Mouse) |
B1AZP2 | DLGP4_MOUSE | MKGLGDSRPRHLSDSLDPPHEPLFAGPDRNPYLLSPTEAFAREARFPGQNTLPGDGLFPLNNQLPPPSSTFPRIHYNSHFEVPEESPFPSHAQATKINRLPANLLDQFEKQLPIHRDGFSTLQFPRGEAKARGESPGRIRHLVHSVQRLFFTKAPSMEGTAGKVGGNGSKKGGLEDGKGRRAKSKERAKAGEPKRRSRSNISGWWSSDDNLDGEGGAFRSGPASGLMTLGRQQERTQPRYFMHAYNTISGHMLKTTKNTTTELTAPPPPPAPPATCPSLGVGTDTNYVKRGSWSTLTLSHAHEVCQKTSATLDKSLLKSKSCHQGLAYHYLQVPGGGGEWSTTLLSPRDMDSTAEGPIPCRRMRSGSYIKAMGDEDSDESGGGSPKPSPKTAARRQSYLRATQQSLGEQSNPRRSLDRLDSVDMLLPSKCPSWEDDYNPISDSLNDSSCISQVFGQASLIPQLFGHDQQVREADLSDQYEAACESACSEAESTTAEALDLPLPSYFRSRSHSYLRAIQAGCSQEEDSVSLQSLSPPPSTGSLSNSRTLPSSSCLVAYKKTPPPVPPRTTSKPFISVTVQSSTESAQDTYLDSQDHKSEVTSQSGLSNSSDSLDSSTRPPSVTRGGITPGPEAPEPPPKHAALKSEQGTLTSSESHSEAIPKRKLSSIGIQVDCIQPVPKEEPSPATKFQSIGIQVEDDWRSSAPSHSMSSRRDTDSDTQDANDSSCKSSERSLPDCTSHPNSISIDAGPRQAPKIAQIKRNLSYGDNSDPALEASSLPPPDPWLETSSSSPAEPAQPGACRRDGYWFLKLLQAETERLEGWCCQMDKETKENNLSEEVLGKVLSAVGSAQLLMSQKFQQFRGLCEQNLNPDANPRPTAQDLAGFWDLLQLSIEDISMKFDELYHLKANSWQLVETPEKRKEEKKPPPPVPKKPAKSKAAVSRDKASDAGDKQRQEARKRLLAAKRAASVRQNSATESADSIEIYVPEAQTRL | null | null | signaling [GO:0023052] | cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; postsynaptic specialization [GO:0099572]; synapse [GO:0045202] | molecular adaptor activity [GO:0060090]; protein domain specific binding [GO:0019904] | PF03359; | null | SAPAP family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
B1B0V2 | EZHIP_MOUSE | MASSSSPERGLEALRDTDESEGEAPGPSGPRGRGGPSGAGSALRLRSLEAEMAAACVTSTAGEDLGTFSEPGSQHGDPEGGGGPDLELGHARPMMRSQRELGLTPKGGGKADQGGKGRKGGSGSPPHTKSSRKREQPNPNRSLMAQGAAGPPLPGARGSPAMPQPESSLSPRPDQSHHFDFPVGNLEAPGPTLRSSTSQGSGSTPVPEALRCAESSRAESDQSSPAGRELRQQASPRAPDDDDDGDGGPDPRGSGTPEGWVLRSGVVPFGRRSSASEVSPEEVRPEAQCTGWNLRPRPRSSASAVSPEARPKAQSAGRNLRPRPRSSASVVSPEARPKAQSAGRNLRPRPRSSASVVSPEARPEAQSAGRNLRPRATPRVPVAPSSTTRSSSDRGSSRAPRSRSRSRSCSTPRLGSDHQRSRKIKMRLDLQVDREPESEAEQEEQELESEPGPSSRPQASRSSSRFAVPGRSSLAAEDSPPRRPVRMRASSPSPPGRLYPLPKHYFEGVHSPSSSSSESSSVSSSHSPLNKAPDPGSSPPLSSLSGPNPFWLALIADLDNLDSSSPRVPGEEIEAAPHTREEEDKKCRG | null | null | chromatin organization [GO:0006325]; oocyte development [GO:0048599] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | protein-containing complex binding [GO:0044877] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86X51}. Cytoplasm {ECO:0000250|UniProtKB:Q86X51}. | null | null | null | null | null | FUNCTION: Inhibits PRC2/EED-EZH1 and PRC2/EED-EZH2 complex function by inhibiting EZH1/EZH2 methyltransferase activity, thereby causing down-regulation of histone H3 trimethylation at 'Lys-27' (H3K27me3) (PubMed:31086175). Probably inhibits methyltransferase activity by limiting the stimulatory effect of cofactors such as AEBP2 and JARID2 (By similarity). Inhibits H3K27me3 deposition during spermatogenesis and oogenesis (PubMed:31451685). {ECO:0000250|UniProtKB:Q86X51, ECO:0000269|PubMed:31086175, ECO:0000269|PubMed:31451685}. | Mus musculus (Mouse) |
B1B534 | EHD2_ORYSJ | MLLSDLSSDQEATGSNSHGGGGGDRMVVGSHGAAHVVLSNLFLPPAAAAAATMLLPAAPVMVRPAAMAAAQEPRAKKKRSLPGNPDPEAEVIALSPRALVATNRFVCEVCNKGFQRDQNLQLHRRGHNLPWKLRHRAAAVSAVTTAAPAPRKRVYVCPEPTCVHHDPARALGDLTGIKKHFSRKHGEKRWRCERCGKRYAVHSDWKAHVKNCGTREYRCDCGILFSRKDSLLTHRAFCDALAEESARLLAAANNSSSITTTTCNNSNISSNNNNNNINSISNSNNLLITSSSSSPPLFLPFSTTPAENPNPNQLLFLQQHQAAHHQLLLPQFQQPPSSPPAYFDHLAFGGGGGVITGSSCNDDNSSIAGDVMVAAGGDSVSFGLTSEGSVTMHAGDVGRRRLTRDFLGVDHDAGEVDELELDELPADLSTTAAACQGCNFAAATTAACCATDFTTGSRQYLGRLPPVNETWSHNF | null | null | long-day photoperiodism, flowering [GO:0048574]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; short-day photoperiodism, flowering [GO:0048575] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF12874; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969, ECO:0000269|PubMed:24280027}. | null | null | null | null | null | FUNCTION: Transcription activator that acts as a flowering master switch in both long and short days, independently of the circadian clock (PubMed:18725639, PubMed:18774969, PubMed:18790997, PubMed:19304997, PubMed:24280027). Promotes flowering upstream of HD1 by up-regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT1 (PubMed:18725639, PubMed:18774969, PubMed:18790997). Seems to repress FTL11 expression (PubMed:18725639). May recognize the consensus motif 5'-TTTGTCGTAAT-3' in target gene promoters (PubMed:18725639). {ECO:0000269|PubMed:18725639, ECO:0000269|PubMed:18774969, ECO:0000269|PubMed:18790997, ECO:0000269|PubMed:24280027, ECO:0000303|PubMed:19304997}. | Oryza sativa subsp. japonica (Rice) |
B1H134 | FLRT3_XENTR | MSTETWNLFVAWAQLLLLFRISPQYVNAKPCPSVCRCDGGFIYCNDRDLTSIPSGIPDDATTLYLQNNQINNAGIPSDLRGLDKVERIYLYRNSLDEFPINLPKNVKELHLQENNIRTITYDALSQIPSIEELHLDDNSVSAVSIEDGAFRDNIFLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTIAEISLQDLTNLKRLVLDGNLLNNNGLGERVFMNLINLTELSLVRNSLTSPPANLPGTNLRKLYLQENHMNYVPPNAFADLTQLYRLDMSNNNITALPQGIFDDLDNLTQLFLRNNPWYCGCKMKWVRDWLQSLPSKVNVRGLMCQAPERVRGMTIKDLNKELFDCKDRIGSNTIHVTTTVLNSLLPAQGQWPVPVTKQPEIRPPDINKIFRTTPIPVKKIITIQVKSITTETIYISWKVALPMTALRLSWQLGHSPVFGSITETIVTGDRTEYLLTALEPESPYRICMVPMETGNIYLSDETPVCIETETAPLKMYNPTTTLNREQEKEPYKNSSLPLAAIIGGAVALVAITLLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFPMIPINSDPISKEEFIIHTIFPPNGVSLYKNSHSESSSNRSYRDSGIPDSDHSHS | null | null | cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; embryonic morphogenesis [GO:0048598]; fibroblast growth factor receptor signaling pathway [GO:0008543]; head development [GO:0060322]; heart development [GO:0007507]; neuron projection development [GO:0031175]; neuron projection extension [GO:1990138]; proepicardium cell migration involved in pericardium morphogenesis [GO:0003345]; response to axon injury [GO:0048678]; synapse assembly [GO:0007416] | axon terminus [GO:0043679]; axonal growth cone [GO:0044295]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060] | null | PF13855; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BGT1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, growth cone membrane {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses. Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234, ECO:0000250|UniProtKB:Q8BGT1}. | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners (By similarity). Modulates cadherin-dependent cell-cell adhesion and cell sorting (By similarity). Plays a role in the spatial organization of brain neurons. Plays a role in vascular development. Plays a role in cell-cell adhesion via its interaction with latrophilins that are expressed at the surface of adjacent cells. Mediates axon attraction towards cells expressing ntn1. mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with unc-5 family members. Plays a role in the regulation of the density of glutamaergic synapses (By similarity). Plays a role in signaling cascades downstream of fgfr1, and possibly also other fgfr family members (By similarity). Plays a role in embryonic morphogenesis, but not in embryonic patterning (PubMed:19492039). {ECO:0000250|UniProtKB:Q70AK3, ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:19492039}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1H1X1 | FXL17_XENLA | MGHVAPHASKKEHVAPHAAEKDHVAPHASKKEHVAPHAAEKGQVAPYAAGEGQVAPNAAGERPVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEAQVAPHAAGEGRVAPHAAGDGQVEHCTVEDREEGHIGTTEQGHMSHYTSKLEHMAPPSAQTEAVVSYVAGERHAPPDCTVSGPAMCCSAEARQTTPDWTTTGPEISQGTLPGLTVLHVGGTWQTFAAEDEPCVTTLLSPVKPLSSSRKYAPYNLQIPSYSESEPQAHKGLSSETFGPCEPLHINQLPSSLLLKIFSNLSLNERCILASLVCKYWRDLCLDSQFWKQLDLSNRQQIKDNILEEIASRSQNITEINISDCFSVSDQGVCVVALKCPGLVKYTAYRCKQLSDISLIALAAHCPSLQKVHVGNQDKLSDEALIQMGRRCKELKDIHFGQCYKISDEGLIVIAKGCQKLQKIYMQENKLVSDESVKAFAEHCPGLQYVGFMGCSVTSEGVINLTKLKHLSSLDLRHITELDNETVMEIVKQCQHLTSLNLCLNRSINDRCVEVIAKEGRSLKELYLVTCKITDYALIAIGRYSKSIETVDVGWCKEITDYGAKQIAQSSKSIRYLGLMRCDKVNEATVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNASPAT | null | null | nervous system development [GO:0007399]; neural crest cell differentiation [GO:0014033]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein ubiquitination [GO:0016567]; regulation of smoothened signaling pathway [GO:0008589]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | null | PF12937;PF13516; | 3.80.10.10; | FBXL17 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UF56}. Nucleus {ECO:0000250|UniProtKB:Q9UF56}. Note=Present in the cytoplasm and nucleus; more abundant in the cytoplasm. {ECO:0000250|UniProtKB:Q9UF56}. | null | null | null | null | null | FUNCTION: Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome (By similarity). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (PubMed:30190310). {ECO:0000250|UniProtKB:Q9UF56, ECO:0000269|PubMed:30190310}. | Xenopus laevis (African clawed frog) |
B1H234 | FLRT3_RAT | MISPAWSLFLIGTKIGLFFQVAPLSVMAKSCPSVCRCDAGFIYCNDRSLTSIPVGIPEDATTLYLQNNQINNVGIPSDLKNLLKVQRIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPGGLPRTIEELRLDDNRISTISSPSLHGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTSLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWLQSLPVKVNVRGLMCQAPEKVRGMAIKDLSAELFDCKDSGIVSTVQITTAIPNTAYPAQGQWPAPVTKQPDIKNPKLTKDQRTTGSPSRKTILITVKSVTPDTIHISWRLALPMTALRLSWLKLGHSPAFGSITETIVTGERSEYLVTALEPESPYRVCMVPMETSNLYLFDETPVCIETQTAPLRMYNPTTTLNREQEKEPYKNPNLPLAAIIGGAVALVSIALLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFQMLPISNEPISKEEFVIHTIFPPNGMNLYKNNLSESSSNRSYRDSGIPDLDHSHS | null | null | axon guidance [GO:0007411]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; embryonic morphogenesis [GO:0048598]; fibroblast growth factor receptor signaling pathway [GO:0008543]; head development [GO:0060322]; heart development [GO:0007507]; neuron projection development [GO:0031175]; neuron projection extension [GO:1990138]; positive regulation of synapse assembly [GO:0051965]; proepicardium cell migration involved in pericardium morphogenesis [GO:0003345]; response to axon injury [GO:0048678]; synapse assembly [GO:0007416]; synapse organization [GO:0050808]; synaptic membrane adhesion [GO:0099560] | axon terminus [GO:0043679]; axonal growth cone [GO:0044295]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic membrane [GO:0097060] | chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104]; protein homodimerization activity [GO:0042803] | PF13855; | 3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}. Synapse, synaptosome {ECO:0000269|PubMed:22405201}. Postsynaptic density {ECO:0000269|PubMed:22405201}. Cell projection, dendrite {ECO:0000269|PubMed:22405201}. Synapse {ECO:0000269|PubMed:22405201}. Presynaptic cell membrane {ECO:0000269|PubMed:15485775}. Cell projection, axon {ECO:0000269|PubMed:15485775}. Cell projection, growth cone membrane {ECO:0000269|PubMed:15485775}. Cytoplasmic vesicle {ECO:0000269|PubMed:15485775}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergic synapses (PubMed:22405201). Proteolytic cleavage in the juxtamembrane region gives rise to a shedded ectodomain (By similarity). {ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}. | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (By similarity). Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity). Promotes neurite outgrowth (in vitro) (By similarity). Mediates cell-cell contacts that promote an increase both in neurite number and in neurite length (PubMed:15485775). Plays a role in the regulation of the density of glutamaergic synapses (PubMed:22405201). Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal morphogenesis during embryonic development, but not for normal embryonic patterning. Required for normal ventral closure, headfold fusion and definitive endoderm migration during embryonic development. Required for the formation of a normal basement membrane and the maintenance of a normal anterior visceral endoderm during embryonic development (By similarity). {ECO:0000250|UniProtKB:Q8BGT1, ECO:0000250|UniProtKB:Q9NZU0, ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}. | Rattus norvegicus (Rat) |
B1H267 | SNX5_RAT | MAAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN | null | null | epidermal growth factor catabolic process [GO:0007174]; intracellular protein transport [GO:0006886]; negative regulation of blood pressure [GO:0045776]; pinocytosis [GO:0006907]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of insulin receptor signaling pathway [GO:0046628]; retrograde transport, endosome to Golgi [GO:0042147] | brush border [GO:0005903]; cytoplasmic side of early endosome membrane [GO:0098559]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endosome [GO:0005768]; macropinocytic cup [GO:0070685]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; retromer complex [GO:0030904]; ruffle [GO:0001726]; tubular endosome [GO:0097422] | D1 dopamine receptor binding [GO:0031748]; dynactin binding [GO:0034452]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314] | PF00787;PF09325; | 1.20.1270.60;3.30.1520.10; | Sorting nexin family | null | SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y5X3}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane ruffles in response to EGFR stimulation (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3}. | null | null | null | null | null | FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation. Plays a role in macropinocytosis (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3}. | Rattus norvegicus (Rat) |
B1H278 | TRI11_RAT | MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECREVSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPTCERSEHWAHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALVSELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDSPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETVNRKEKGELSAGNGFWILVFLGSFYNSNERAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETPFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ | 2.3.2.27 | null | innate immune response [GO:0045087]; negative regulation of AIM2 inflammasome complex assembly [GO:0140972]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neurogenesis [GO:0050768]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral transcription [GO:0032897]; positive regulation of viral entry into host cell [GO:0046598]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation of gene expression [GO:0010468]; suppression of viral release by host [GO:0044790] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | protein domain specific binding [GO:0019904]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | TRIM/RBCC family | PTM: Autoubiquitinated upon DNA stimulation; autoubiquitination promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes. {ECO:0000250|UniProtKB:Q96F44}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F44}. Nucleus {ECO:0000250|UniProtKB:Q96F44}. | 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:Q96F44}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q96F44}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity). Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2. Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (By similarity). {ECO:0000250|UniProtKB:Q96F44, ECO:0000250|UniProtKB:Q99PQ2}. | Rattus norvegicus (Rat) |
B1H3E1 | NLK2_XENTR | MAFQGPGRSLPGQLCAGVFGGLIQPPLGQKFYCPNGGSGGGGVPAVPSPLPQALSAPQCNGDGRGEPEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPQIDCFEEIYVITELMQTDLHKVIVSPQPLSSDHIKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESQHMTQEVVTQYYRAPEILMGSRHYRSAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPPLTAMRSACEGARAHILRGPHKPPSLSVLYMLSGEATHEAVHLLCRMLLFDPLKRISAKDALAHPYLEEGRLRYHTCMCHCCYSVSSGRVYTADFEPTATNRFDDSYEKSLTSVWQVKELVHRFITDQQQGKRPPLCINPHSAAFKTFIRSTAWHSSKVSKKEER | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | anterior/posterior pattern specification [GO:0009952]; mesoderm formation [GO:0001707]; nervous system development [GO:0007399]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of protein ubiquitination [GO:0031398]; serine phosphorylation of STAT protein [GO:0042501]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. | 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=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q8QGV6}; 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=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q8QGV6}; | null | null | null | null | FUNCTION: Negatively regulates Wnt/beta-catenin-signaling during development. Plays a role together with sox11 in neural induction during early embryogenesis. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 to phosphorylate stat3. Augments the rnf138/narf-directed ubiquitination and degradation of tcf/lef by enhancing the association of rnf138/narf and tcf/lef. Phosphorylates mef2a to play a role in anterior neural development, including eye formation (By similarity). {ECO:0000250}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1INP5 | BXB_CLOBK | MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P10844}; Note=Binds 1 zinc ion per subunit (By similarity). {ECO:0000250|UniProtKB:P10844}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | lipid binding [GO:0008289]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | SUBCELLULAR LOCATION: [Botulinum neurotoxin type B]: Secreted {ECO:0000250|UniProtKB:P10844}. Host synapse, host presynaptic cell membrane {ECO:0000250|UniProtKB:P10844}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin B light chain]: Secreted {ECO:0000250|UniProtKB:P10844}. Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:P10844}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin B heavy chain]: Secreted {ECO:0000250|UniProtKB:P10844}. Host synapse, host presynaptic cell membrane {ECO:0000250|UniProtKB:P10844}. Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane {ECO:0000250|UniProtKB:P0DPI0}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000250|UniProtKB:P10844}; | null | null | null | null | FUNCTION: [Botulinum neurotoxin type B]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin B which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). {ECO:0000250|UniProtKB:P10844}.; FUNCTION: [Botulinum neurotoxin B light chain]: Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '76-Gln-|-Phe-77' bond in synaptobrevin-2/VAMP2, blocking neurotransmitter release (By similarity). {ECO:0000250|UniProtKB:P10844}.; FUNCTION: [Botulinum neurotoxin B heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind simultaneously to adjacent but separate sites at the tip of the HC. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). {ECO:0000250|UniProtKB:P10844}. | Clostridium botulinum (strain Okra / Type B1) |
B1IZU5 | HCHA_ECOLC | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) |
B1LQP2 | HCHA_ECOSM | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli (strain SMS-3-5 / SECEC) |
B1MK49 | PHY_MYCA9 | MHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEVFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLPDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPWCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDPLDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQEFGPR | 3.7.1.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30784195}; | null | null | metal ion binding [GO:0046872]; phloretin hydrolase activity [GO:0050180] | PF18089; | null | DAPG/phloretin hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate; Xref=Rhea:RHEA:23396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16204, ChEBI:CHEBI:16331, ChEBI:CHEBI:17276; EC=3.7.1.4; Evidence={ECO:0000269|PubMed:30784195}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=81.2 uM for phloretin {ECO:0000269|PubMed:30784195}; KM=2590 uM for MAPG {ECO:0000269|PubMed:30784195}; Note=kcat is 0.85 sec(-1) with phloretin as substrate. kcat is 49.6 sec(-1) with MAPG as substrate. {ECO:0000269|PubMed:30784195}; | null | null | null | FUNCTION: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG). {ECO:0000269|PubMed:30784195}. | Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium abscessus) |
B1MTB0 | HMGB1_PLEMO | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (NLS 1 and NLS 2) leads to cytoplasmic localization and subsequent secretion. Acetylation on Lys-3 results in preferential binding to DNA ends and impairs DNA bending activity (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB1 (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so). {ECO:0000250|UniProtKB:P09429}.; PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation with LPS (By similarity). {ECO:0000250|UniProtKB:P63158}.; PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing peptide which may mediate immunogenic activity; the peptide antagonizes apoptosis-induced immune tolerance. Can be proteolytically cleaved by a thrombin:thrombomodulin complex; reduces binding to heparin and pro-inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103}.; PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. {ECO:0000250|UniProtKB:P09429}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}; Extracellular side {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus. Translocates from the nucleus to the cytoplasm upon autophagy stimulation. Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced HGMB1 which subsequently gets oxidized. Also released from apoptotic cells. Active secretion from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells, natural killer cells and plasma cells in response to various stimuli such as LPS and cytokines involves a nonconventional secretory process via secretory lysosomes. Found on the surface of activated platelets. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.; FUNCTION: Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. May be involved in nucleotide excision repair (NER), mismatch repair (MMR) and base excision repair (BER) pathways, and double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. May be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.; FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.; FUNCTION: In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T-cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes. {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}. | Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch) |
B1NF18 | C719B_PAPSO | MAPINIEGNDFWMIACTVIIVFALVKFMFSKISFYQSANTTEWPAGPKTLPIIGNLHQLGGGVPLQVALANLAKVYGGAFTIWIGSWVPMIVISDIDNAREVLVNKSADYSARDVPDILKIITANGKNIADCDSGPFWHNLKKGLQSCINPSNVMSLSRLQEKDMQNLIKSMQERASQHNGIIKPLDHAKEASMRLLSRVIFGHDFSNEDLVIGVKDALDEMVRISGLASLADAFKIAKYLPSQRKNIRDMYATRDRVYNLIQPHIVPNLPANSFLYFLTSQDYSDEIIYSMVLEIFGLGVDSTAATAVWALSFLVGEQEIQEKLYREINNRTGGQRPVKVVDLKELPYLQAVMKETLRMKPIAPLAVPHVAAKDTTFKGRRIVKGTKVMVNLYAIHHDPNVFPAPYKFMPERFLKDVNSDGRFGDINTMESSLIPFGAGMRICGGVELAKQMVAFALASMVNEFKWDCVSEGKLPDLSEAISFILYMKNPLEAKITPRTKPFRQ | 1.14.19.67 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q94IP1}; | hormone biosynthetic process [GO:0042446]; morphine biosynthetic process [GO:0097295]; progesterone metabolic process [GO:0042448] | endoplasmic reticulum membrane [GO:0005789] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; salutaridine synthase activity [GO:0047055]; steroid 17-alpha-monooxygenase activity [GO:0004508] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(R)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + salutaridine; Xref=Rhea:RHEA:17713, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58061, ChEBI:CHEBI:58144, ChEBI:CHEBI:58210; EC=1.14.19.67; Evidence={ECO:0000269|PubMed:19567876, ECO:0000269|PubMed:22098111}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.2 uM for (R)-reticuline {ECO:0000269|PubMed:19567876}; Note=kcat is 1.64 min(-1) for (R)-reticuline.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:19567876}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19567876}; | FUNCTION: Cytochrome P450 monooxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:19567876, PubMed:22098111). Catalyzes the formation of the morphinan alkaloid salutaridine by intramolecular phenol oxidation of (R)-reticuline without the incorporation of oxygen into the product (PubMed:19567876, PubMed:22098111). Can also use (R)-norreticuline as substrate (PubMed:19567876). {ECO:0000269|PubMed:19567876, ECO:0000269|PubMed:22098111}. | Papaver somniferum (Opium poppy) |
B1NF19 | C719D_ARGME | MEEKIMTNNSPWILTSSTTTTTTILLSLLFTIFIILRRNKSSSSKMVWPTGPKTLPIIGNMNILGGTALHVVLHNLAKTYGNVMTIWIGSWRPVIVVSDIDRAWEVLVNKSSDYSARDMPEITKLATADWKTISSSDSGPFWTNLRKGLQNVALSPQNLSSQSKFQERDIIKTIQNLKEEAKMNNGIVKPLDHLKKAMVRLISRLIYGQDFDNDEYVEEMHHTIEELIRVSGYARLAEAFYYAKYLPSHKKAVREVLQANQRVQNLVRPLLSLNSPTNTYLHFLRSQNYEDEVIIFAIFEAYLLGVDSTSSTTAWALAYLIREPNVQEKLYEELKNFTNDNDRKMVKFEDLNKLQYLQAVVKETMRMKPIAPLAIPHKACRETSLMGRKVNQGTRVMVNIYALHHNQNVWKEPYKFNPERFLQKNQDGVDGKAMEQSLLPFSAGMRICAGMELGKLQFSFALANLVNAFKWSCVSDGVFPDMSDQLGFVLLMKTPLEAGIVPRM | 1.14.19.64; 1.14.19.68; 1.14.19.73 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | isoquinoline alkaloid biosynthetic process [GO:0033075] | endoplasmic reticulum membrane [GO:0005789] | (S)-canadine synthase activity [GO:0047056]; (S)-nandinine synthase activity [GO:0102632]; (S)-stylopine synthase activity [GO:0047052]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-cheilanthifoline + O2 + reduced [NADPH--hemoprotein reductase] = (S)-stylopine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:13773, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16233, ChEBI:CHEBI:18285, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.19.64; Evidence={ECO:0000269|PubMed:21094631}; CATALYTIC ACTIVITY: Reaction=(S)-tetrahydrocolumbamine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-canadine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21456, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16592, ChEBI:CHEBI:17772, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.19.68; Evidence={ECO:0000269|PubMed:21094631}; CATALYTIC ACTIVITY: Reaction=(S)-scoulerine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-nandinine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50364, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17129, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132749; EC=1.14.19.73; Evidence={ECO:0000269|PubMed:21094631}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 13.8 min(-1) for (S)-cheilanthifoline. {ECO:0000269|PubMed:21094631}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:21094631}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-35 degrees Celsius. {ECO:0000269|PubMed:21094631}; | FUNCTION: Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (S)-cheilanthifoline to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-tetrahydrocolumbamine to (S)-canadine. Can be involved in both sanguinarine and berberine biosynthesis. Catalyzes an oxidative reaction that does not incorporate oxygen into the product. {ECO:0000269|PubMed:21094631}. | Argemone mexicana (Mexican prickly poppy) |
B1NWR6 | NA228_NEMVE | MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00706; | 2.20.20.10; | Sea anemone sodium channel inhibitory toxin family, Type II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18538344}. | null | null | null | null | null | FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity for arthropod over mammalian channels (PubMed:18538344). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Also causes paralysis of cherry shrimps immediately after injection at very low doses (PubMed:29424690). Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes (PubMed:22048953). It has also been observed to cause death of zebrafish larvae within 1 hour (PubMed:31134275). {ECO:0000269|PubMed:18538344, ECO:0000269|PubMed:22048953, ECO:0000269|PubMed:29424690, ECO:0000269|PubMed:31134275}. | Nematostella vectensis (Starlet sea anemone) |
B1NWS4 | NA225_NEMVE | MASFKIVIVCLALLVAVACARRRDMMSDDELDFHLSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF00706; | 2.20.20.10; | Sea anemone sodium channel inhibitory toxin family, Type II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18538344}. | null | null | null | null | null | FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity for arthropod over mammalian channels (PubMed:18538344). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Also causes paralysis of cherry shrimps immediately after injection at very low doses (PubMed:29424690). Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes (PubMed:22048953). It has also been observed to cause death of zebrafish larvae within 1 hour (PubMed:31134275). {ECO:0000269|PubMed:18538344, ECO:0000269|PubMed:22048953, ECO:0000269|PubMed:29424690, ECO:0000269|PubMed:31134275}. | Nematostella vectensis (Starlet sea anemone) |
B1NY81 | CAS31_MEDTR | MSQYQQGYGDQTRRVDEYGNPLTSQGQVDQYGNPISGGGMTGATGHGHGHHQQHHGVGVDQTTGFGSNTGTGTGYGTHTGSGGTHTGGVGGYGTTTEYGSTNTGSGYGNTDIGGTGYGTGTGTGTTGYGATGGGTGVGYGGTGHDNRGVMDKIKEKIPGTDQNASTYGTGTGYGTTGIGHQQHGGDNRGVMDKIKEKIPGTDQNQYTHGTGTGTGTGYGTTGYGASGVGHQQHGEKGVMDKIKEKIPGTEQNTYGTGTGTGHGTTGYGSTGTGHGTTGYGDEQHHGEKKGIMEKIKEKLPGTGSCTGHGQGH | null | null | cold acclimation [GO:0009631]; nodulation [GO:0009877]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | metal ion binding [GO:0046872] | PF00257; | null | Plant dehydrin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29868087}. | null | null | null | null | null | FUNCTION: Intrinsically disordered protein acting as a chaperone (By similarity). Ensures leghemoglobins (e.g. LB120-1) protection from denaturation under thermal and drought stresses to delay root nodule nitrogenase inactivation and subsequent nodule senescence, thus supporting symbiotic nitrogen fixation (SNF) (PubMed:29868087). {ECO:0000250|UniProtKB:P42763, ECO:0000269|PubMed:29868087}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
B1P1D9 | JZ11F_CHIGU | MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E0 | JZ11C_CHIGU | MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFRSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E1 | JZ11B_CHIGU | MKVSVVITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E2 | JZ11D_CHIGU | MKASVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1E3 | JZ11E_CHIGU | MKVSVLITLAVLGVMFVWTSAAELEERGSDQRDSPAWLKSMERIFQSEERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1P1F5 | JZT32_CHIGU | KASVLITLAVLGVMFVWTSAAELEERGSDQRDSPALIKSMAKVFQSEERECTKLLGGCTKDSECCPHLGCRKKWPYHCGWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 47 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17476710}. | null | null | null | null | null | FUNCTION: Inhibits TTX-sensitive and TTX-insensitive sodium currents (IC(50) is 0.6 uM and 0.95 uM respectively) on rat dorsal root ganglion (DRG) neurons (PubMed:18581053, PubMed:19409400). Inhibits muscular subtypes sodium channels Nav1.4/SCN4A and Nav1.5/SCN5A transiently transfected in to HEK293 cells (IC(50) is 5.42 uM and 0.45 uM respectively). Also blocks Kv2.1/KCNB1 potassium channels expressed in X.laevis oocytes with an IC(50) of 604 nM. Injection of the toxin in mice was immediately followed by general ataxia, lack of response to stimuli and semiparalysis (PubMed:19409400). {ECO:0000269|PubMed:18581053, ECO:0000269|PubMed:19409400}. | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
B1PRL5 | CAVN4_RAT | MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVATVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDVPCPASLSVVKDRSLPENEEEAEEVFDPPIDLSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSKENMQKTRQNFDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISNATPSKEAFKIRSLRKPKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDGFSETEKEVTKVGYIPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS | null | null | cell differentiation [GO:0030154]; muscle organ development [GO:0007517]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | null | PF15237; | null | CAVIN family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:A2AMM0}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:A2AMM0}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Cell membrane {ECO:0000250|UniProtKB:A2AMM0}. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm. Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000250|UniProtKB:A2AMM0}. | null | null | null | null | null | FUNCTION: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes (By similarity). Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway (PubMed:18332105). {ECO:0000250|UniProtKB:A2AMM0, ECO:0000269|PubMed:18332105}. | Rattus norvegicus (Rat) |
B1PVZ9 | KARG_METEN | MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKKTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSMQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEGGIYDISNKRRMGLTEFQAVKEMQDGILELIKIEKEMI | 2.7.3.3 | null | female gonad development [GO:0008585]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | null | arginine kinase activity [GO:0004054]; ATP binding [GO:0005524]; creatine kinase activity [GO:0004111] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine; Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3; Evidence={ECO:0000269|PubMed:12496430, ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330, ECO:0000269|PubMed:21645540}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941; Evidence={ECO:0000305|PubMed:12496430, ECO:0000305|PubMed:19341812, ECO:0000305|PubMed:21507330, ECO:0000305|PubMed:21645540}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22942; Evidence={ECO:0000305|PubMed:12496430, ECO:0000305|PubMed:19341812, ECO:0000305|PubMed:21507330, ECO:0000305|PubMed:21645540}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.33 mM for ATP (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:19341812}; KM=1.59 mM for L-arginine (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:19341812}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:19341812}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19341812}; | FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine. {ECO:0000269|PubMed:12496430, ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330, ECO:0000269|PubMed:21645540}. | Metapenaeus ensis (Greasyback shrimp) (Penaeus ensis) |
B1Q005 | MBOA4_RAT | MDWLQFFFLHPVSLYQGAAFPFALLFNYLCITESFPTRARYLFLLAGGGVLALAAMGPYALLIFIPALCAVAMISSLSPQEVHGLTFFFQMGWQTLCHLGLHYKEYYLCEPPPVRFYITLSSLMLLTQRVTSLSLDISEGKVEAAWRGTRSRSSLCEHLWDALPYISYLLFFPALLGGSLCSFQRFQACVQRPRSLYPSISFWALTWRGLQILGLECLKVALRRVVSAGAGLDDCQRLECIYIMWSTAGLFKLTYYSHWILDDSLLHAAGFGSEAGQRPGEERYVPDVDIWTLETTHRISLFARQWNRSTAQWLKRLVFQRSRRWPVLQTFAFSAWWHGLHPGQVFGFLCWSVMVKADYLIHTFANGCIRSWPLRLLYRSLTWAHTQIIIAYVMLAVEGRSFSSLCRLCCSYNSIFPVTYCLLLFLLARRKHKCN | 2.3.1.- | null | lipid modification [GO:0030258]; peptidyl-serine octanoylation [GO:0018191] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; serine O-acyltransferase activity [GO:0016412] | PF03062; | null | Membrane-bound acyltransferase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59965; Evidence={ECO:0000269|PubMed:18443287}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + L-seryl-[protein] = CoA + O-decanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59972, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15486, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:143549; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59973; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141128; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + L-seryl-[protein] = CoA + O-butanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68276, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17461, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:177287; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68277; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + pentanoyl-CoA = CoA + O-pentanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68280, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17462, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:177288; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68281; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=hexanoyl-CoA + L-seryl-[protein] = CoA + O-hexanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68284, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17463, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:177289; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68285; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=heptanoyl-CoA + L-seryl-[protein] = CoA + O-heptanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68288, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17464, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811, ChEBI:CHEBI:177290; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68289; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + nonanoyl-CoA = CoA + O-nonanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68292, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17465, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:76291, ChEBI:CHEBI:177291; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68293; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + L-seryl-[protein] = CoA + O-dodecanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68296, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17466, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:177292; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68297; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + tetradecanoyl-CoA = CoA + O-tetradecanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68300, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17467, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:177293; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68301; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + L-seryl-[protein] = CoA + O-fatty acyl-L-seryl-[protein]; Xref=Rhea:RHEA:68272, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17460, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636, ChEBI:CHEBI:177286; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68273; Evidence={ECO:0000250|UniProtKB:Q96T53}; | null | null | null | null | FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity) (PubMed:18443287). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity). {ECO:0000250|UniProtKB:Q96T53, ECO:0000269|PubMed:18443287}. | Rattus norvegicus (Rat) |
B1Q006 | MBOA4_DANRE | MIDLLWISSDGHPQLFYQFINIPFAFLFHCLSSQGHLSIINRYVYLAMGGFMLAIATMGPYSSLLFLSAIKLLLLIHYIHPMHLHRWILGLQMCWQTCWHLYVQYQIYWLQEAPDSRLLLAISALMLMTQRISSLSLDFQEGTISNQSILIPFLTYSLYFPALLGGPLCSFNAFVQSVERQHTSMTSYLGNLTSKISQVIVLVWIKQLFSELLKSATFNIDSVCLDVLWIWIFSLTLRLNYYAHWKMSECVNNAAGLGVYFHKHSGQTSWDELSDGSVLVTEASSRPSVFARKWNQTTVDWLRKIVFNRTSRSPLFMTFGFSALWHGLHPGQILGFLIWAVTVQADYKLHRFSHPKLNSLWRKRLYVCVNWAFTQLTVACVVVCVELQSLASVKLLWSSCIAVFPLLSALILIIL | 2.3.1.- | null | lipid modification [GO:0030258]; peptidyl-serine octanoylation [GO:0018191]; response to food [GO:0032094] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | serine O-acyltransferase activity [GO:0016412] | PF03062; | null | Membrane-bound acyltransferase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59965; Evidence={ECO:0000269|PubMed:18443287}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + L-seryl-[protein] = CoA + O-decanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59972, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15486, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:143549; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59973; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141128; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + L-seryl-[protein] = CoA + O-butanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68276, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17461, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:177287; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68277; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + pentanoyl-CoA = CoA + O-pentanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68280, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17462, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:177288; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68281; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=hexanoyl-CoA + L-seryl-[protein] = CoA + O-hexanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68284, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17463, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:177289; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68285; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=heptanoyl-CoA + L-seryl-[protein] = CoA + O-heptanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68288, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17464, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811, ChEBI:CHEBI:177290; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68289; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + nonanoyl-CoA = CoA + O-nonanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68292, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17465, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:76291, ChEBI:CHEBI:177291; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68293; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + L-seryl-[protein] = CoA + O-dodecanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68296, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17466, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:177292; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68297; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + tetradecanoyl-CoA = CoA + O-tetradecanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:68300, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17467, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:177293; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68301; Evidence={ECO:0000250|UniProtKB:Q96T53}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + L-seryl-[protein] = CoA + O-fatty acyl-L-seryl-[protein]; Xref=Rhea:RHEA:68272, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:17460, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636, ChEBI:CHEBI:177286; Evidence={ECO:0000250|UniProtKB:Q96T53}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68273; Evidence={ECO:0000250|UniProtKB:Q96T53}; | null | null | null | null | FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity) (PubMed:18443287). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity). {ECO:0000250|UniProtKB:Q96T53, ECO:0000269|PubMed:18443287}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B1Q236 | SYG1_CAEEL | MVRWQTWPLLLLFQLVTCQQLQQRIVEAPKDTLAAVGETAILTCRVEHQQGPVQWMKDDFGLGTDRDKPLPGNKRYRMVGSAANGEYNLEISNVTLFDDDDFACQISESDHAKAVVSSKAKLTVLVRPTPPKIVKSHHSLKAIAGDPITQSCLSRKGKPPPTIGWAIASDEHGKHIVSWLGESRSKFGGIHAKPEISQETVIAHVNETTQVEEGGNNSREDSSIYSIMSNLSFIPRPEDDHKYLICISQHMTFPNKIEVDSVKLSLRYAPQINLTVASKLPLRENGSALLACNVNAKPLDNVKISWYKGNQKLRETGDTLTFETLKMEDHNRDIFCEATNEIGTTRGSIKLNVAFGARIMSTSQDKEVNEGDNAFFHCATLANPAPAIFWTRGDSDEIIGHGENLTLENVRTWQQGNYNCTATVEGFRKQILSHYLHIRGPPTVSMKDEVSASLDEATEIICEISGRPKTNNVRWTVNGKEINFNNGRITVHQYPKPYGKESILKIKDLKEEDFGVYNCSANNGLGFDNRGTLLKKRNILDWIVITAKFDRMVALAIISAGVLLVSLLCCLCMCRSNCRSRKSKFIDDQSDVTVKCEALDGQYFPEMYSSSPVDNVHLSTKDYISIPQNNPDLDFLGATGSFGPPGGLYPKCFNNSANEYIYNRYEHSYGSFGSGLSTPGGVSDMYGVAMSDKLPVMETLQEVETPKTSNYNFLSSPEVVRPISRTSTHV | null | null | actin filament bundle assembly [GO:0051017]; branching morphogenesis of a nerve [GO:0048755]; cell-cell adhesion [GO:0098609]; cell-cell signaling [GO:0007267]; collateral sprouting [GO:0048668]; synapse assembly [GO:0007416]; synapse organization [GO:0050808]; synaptic target recognition [GO:0008039] | axon [GO:0030424]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636]; synapse [GO:0045202]; synaptic membrane [GO:0097060] | cell adhesion molecule binding [GO:0050839]; protein-containing complex binding [GO:0044877] | PF08205;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:15035988, ECO:0000269|PubMed:17626846}. Synapse {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:24485456}. | null | null | null | null | null | FUNCTION: Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). Also required for F-actin assembly at the synaptic region and for axon branch formation (PubMed:24439377). {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:15035988, ECO:0000269|PubMed:17626846, ECO:0000269|PubMed:21858180, ECO:0000269|PubMed:24439377, ECO:0000269|PubMed:24485456}. | Caenorhabditis elegans |
B1Q257 | GCY10_CAEEL | MLKSLLIIVIVFLHRELCDGIQLILFDNWPSAQNVCASAVADATANGQCTTKSIQKHLELLTVIILLKLFGVFHRINQQHGCSGDNSVKSASYAINAVASRTSGELDFVFVGPTCTTDIRTIGDFAEIWKSPVIGYEPVFEARGVQELTSVINVAQFSVGGVAETLVFLMKELEQVEITLVGSVKVLPNGLSLSNDLRSYNEIMNSFKIREYVEVDENDVDWTKVDQKIKRGARMIVVCADFYDIYSAFYNIGIRSLSGFRFIIVVILNKPPDEILNQPNVKNLLYGSNAFIISPLQEQYSDAFSIMQDVIPNLADDQFTTFLRIYHACYAYCVGSVNGAETQTDNYHTAMSGKAVTTKYGTFTFDNSGSVLTNYAVFTINPAEMTFESILTLKSVAKSCDTYNCFQLSPNKTSDLLWTLKDMDPPDDCVAKSSCVNYIPHIIAAVVIVTIIVIAIVIIVKQRRHKLNIYKLTWKVPKESLKIIVNKNADAKMQRELENRASNTDNAAALTSRRRVFGSYALVGTQRAEYVQFKQIRKINFPETTLDYLYSLKQLQHDNLAKFYGIQVNDDIMTMTILHTLVERGTLEEFCLDRDFGMDDTFKSAFMRDILKGLQYLHKSSIGYHGHLQASTCLIDINWVLKLTLYGVSNFMSDQLDAENIKVPEQAAHMITYPQYVCFPPEHIREYDDSGKQPPRVVRGSPKGDIYCVGMIFYMMVEREDPYHLIHSVERPNATLIKQILNENHMPRITDDYRQENMLLEMCKECWDRNPDKRPTIKKLIESISTVYPLSKGNLVDQMIRMSEKYADELEQMVAIRTADLADAQMQTMRLLNEMLPASIAKDLKNGLIMPPRSYESATVMFVQICDFNALMKRSSPEQVIAFLNDIYDQFDTVIKRHDAYKVETTGETYMVASGVPHENEGRHIFEVAEISLEIREISYIYVLQHDKNYKLRIRIGFHAGPIAAGVIGIRSPRYCLFGDTVNFASRMQSNCPPNQIQTSEITARLLFDSHEYKFVKRGIVHVKGKGEVNCYWLNEHLHEETEPPLPPMTPVPNPLRRGSIVPLQKA | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; chemosensory behavior [GO:0007635]; intracellular signal transduction [GO:0035556]; negative chemotaxis [GO:0050919]; negative regulation of multicellular organism growth [GO:0040015]; olfactory behavior [GO:0042048]; olfactory learning [GO:0008355]; phototransduction [GO:0007602]; positive chemotaxis [GO:0050918]; positive regulation of gene expression [GO:0010628]; protein localization to non-motile cilium [GO:0097499]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of multicellular organism growth [GO:0040014]; regulation of neurogenesis [GO:0050767]; response to odorant [GO:1990834]; sensory perception of bitter taste [GO:0050913]; sensory perception of smell [GO:0007608] | non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF00069; | 3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:10774726}. Note=Localizes in cilium of sensory neurons. {ECO:0000269|PubMed:10774726}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187}; | null | null | null | null | FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward volatile odorants in AWC sensory neurons and their avoidance in AWB sensory neurons (PubMed:10774726, PubMed:8348618). May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP (PubMed:23874221). Involved in phototransduction in ASJ neurons downstream of G protein coupled-photoreceptor lite-1 (PubMed:20436480). Required to maintain the expression of putative olfactory receptor str-2 in AWC neurons in adults (PubMed:10571181). In AWB and AWC sensory neurons, mediates the recognition of food oders which subsequently allows for the detection of preferred food sources (PubMed:25009271). Involved in AWB sensory neuron development and extension during postembryonic development, potentially via mediating localization of tub-1 and PI(4,5)P2 to membrane cilia (PubMed:31259686). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:10571181, ECO:0000269|PubMed:10774726, ECO:0000269|PubMed:20436480, ECO:0000269|PubMed:23874221, ECO:0000269|PubMed:25009271, ECO:0000269|PubMed:31259686, ECO:0000269|PubMed:8348618}. | Caenorhabditis elegans |
B1Q2B6 | OLIS_CANSA | MNHLRAEGPASVLAIGTANPENILLQDEFPDYYFRVTKSEHMTQLKEKFRKICDKSMIRKRNCFLNEEHLKQNPRLVEHEMQTLDARQDMLVVEVPKLGKDACAKAIKEWGQPKSKITHLIFTSASTTDMPGADYHCAKLLGLSPSVKRVMMYQLGCYGGGTVLRIAKDIAENNKGARVLAVCCDIMACLFRGPSESDLELLVGQAIFGDGAAAVIVGAEPDESVGERPIFELVSTGQTILPNSEGTIGGHIREAGLIFDLHKDVPMLISNNIEKCLIEAFTPIGISDWNSIFWITHPGGKAILDKVEEKLHLKSDKFVDSRHVLSEHGNMSSSTVLFVMDELRKRSLEEGKSTTGDGFEWGVLFGFGPGLTVERVVVRSVPIKY | 2.3.1.206; 4.4.1.- | null | cannabinoid biosynthetic process [GO:1901696]; polyketide biosynthetic process [GO:0030639]; terpenoid biosynthetic process [GO:0016114] | null | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; lyase activity [GO:0016829] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=3 H(+) + hexanoyl-CoA + 3 malonyl-CoA = 3,5,7-trioxododecanoyl-CoA + 3 CO2 + 3 CoA; Xref=Rhea:RHEA:34119, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:62620, ChEBI:CHEBI:66957; EC=2.3.1.206; Evidence={ECO:0000269|PubMed:19454282, ECO:0000269|PubMed:19581347, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34120; Evidence={ECO:0000269|PubMed:19454282, ECO:0000269|PubMed:19581347, ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=3,5,7-trioxododecanoyl-CoA = CO2 + CoA + olivetol; Xref=Rhea:RHEA:20261, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:66957, ChEBI:CHEBI:66960; Evidence={ECO:0000269|PubMed:19454282, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20262; Evidence={ECO:0000269|PubMed:19454282, ECO:0000269|Ref.3}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60.8 uM for hexanoyl-CoA {ECO:0000269|PubMed:19454282}; KM=88.9 uM for butyryl-CoA {ECO:0000269|PubMed:19454282}; KM=99.1 uM for isovaleryl-CoA {ECO:0000269|PubMed:19454282}; KM=81.7 uM for octanoyl-CoA {ECO:0000269|PubMed:19454282}; Note=kcat is 2.96 min(-1) with hexanoyl-CoA as substrate (PubMed:19454282). kcat is 0.719 min(-1) with butyryl-CoA as substrate (PubMed:19454282). kcat is 0.585 min(-1) with isovaleryl-CoA as substrate (PubMed:19454282). kcat is 0.525 min(-1) with octanoyl-CoA as substrate (PubMed:19454282). {ECO:0000269|PubMed:19454282}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:18323613, PubMed:19454282, PubMed:19581347, PubMed:22802619). Polyketide synthase responsible for olivetol biosynthesis, from a C(12)-polyketide, probably 3,5,7-trioxododecanoyl-CoA (PubMed:19454282, Ref.3). Catalyzes the first step in the cannabinoids biosynthetic pathway. The preferred substrate is hexanoyl-CoA, but accepts also CoA esters with C4 to C8 aliphatic side chains (PubMed:19454282). When using malonyl-CoA and hexanoyl-CoA as substrates, produces undetermined compounds distinct form olivetol or olivetolic acid (PubMed:19581347) that could be hexanoyl triacetic acid lactone (HTAL) (PubMed:18323613) and pentyl diacetic acid lactone (PDAL) (PubMed:22802619). Produces olivetolic acid when acting in concert with olivetolic acid cyclase (OAC). {ECO:0000269|PubMed:18323613, ECO:0000269|PubMed:19454282, ECO:0000269|PubMed:19581347, ECO:0000269|PubMed:22802619, ECO:0000269|Ref.3}. | Cannabis sativa (Hemp) (Marijuana) |
B1Q3J6 | DNM1B_ORYSJ | MVKSPCSPVTTGKKRCRAKPQKKDEDTTDKGKLDEGPLDATKEMNGVGKGDSRAACKRPRRAAACSDFKEKSVRLSDKSSVVATNGNKMEEEEMDAVKLTKLGPEVQRPCRKLIDFILHDADGKLQPFEMSEIDDFFITALIMPMDDDLEKDRQKGVRCEGFGRIEDWAISGYDEGTAVVWVSTEVADYECVKPAGNYKSYYDHFYEKAQVCVEVYRKLARSVGGNPNLGLEELLASVVRSINAIKGYSGTLSKDFVISNGEFVYNQLIGLDETANTDDEKFATLPVLLALRDGCKSRVEVSKLQPNISNGSLKINDAECKEVSEDDDEKLARLLQQEEEWKMMKQRGKRGTTSQKNVYIKISEAEIANDYPLPAYYKPSSQEMDEYIFDSEDSFYSDVPVRILNNWALYNADSRLIPLELIPMKAGAENDIVVFGSGFMREDDGSCCSTAESAKLSSSSSSNHQDAGVSIYLSPIKEWVIEFGGSMICITIRTDVAWYKLRQPTKQYAPWCEPVLKTARLSVSIITLLKEQSRASKLSFADVIKKVAEFDKGSPAFVSSNVALVERYIVVHGQIILQQFSDFPDETIRRSAFATGLLMKMEQRRHTKLVMKKKVQVMRGENLNPSATMGPASRRKVMRATTTRLINRIWSDYYTHHFPEDSKDADVNEAKEIDDELEENEDEDAEEEAQIEEENVSKTPPSTRSRKLVSQTCKEIRWEGEAIGKTPSGEALYKCAYVRELRINLGRTVALEDDSGELVMCFVEYMFQKLNGAKMVHGRLLQKGSETVLGNAANERDLFLTNECLEFELEDIKELMSVNLQSLPWGHKYRKENAEADRIERAKAEDRKKKGLPMEYLCKSLYWPEKGAFFSLPHDKLGLGNGFCSSCQQKEPDCDELQILSKNSFIYRNITYNVNDYLYIRPDFFSQEEDRATFKGGRNVGLKPYVVCHLLDVHEPAGSRKIHPASTKISVRRFYRPDDISSAKAYVSDIREVYYSENIVKVPVDMIEGKCEVKKKIDISNSDVPVMVEHEFFCEHFYDPATGALKQLPPNVKLMSVQQKATGALKKNKGKQICESDQVDSDKCTKVSKENRLATLDIFAGCGGLSEGLQQAGVSFTKWAIEYEEPAGEAFTKNHPEAAVFVDNCNVILKAIMDKCGDADDCISTSEAAEQAAKFSQDNIMNLPVPGEVEFINGGPPCQGFSGMNRFNQSPWSKVQCEMILAFLSFAEYFRPRFFLLENVRNFVSFNKGQTFRLTVASLLEMGYQVRFGILEAGTFGVAQSRKRAFIWAAAPGETLPDWPEPMHVFASPELKINLPDGKYYAAAKSTAGGAPFRAITVRDTIGDLPKVENGASKLLLEYGGEPISWFQKKIRGNTIALNDHISKEMNELNLIRCQRIPKRPGCDWHDLPDEKVKLSSGQLVDLIPWCLPNTAKRHNQWKGLYGRLDWEGNFPTSVTDPQPMGKVGMCFHPDQDRIITVRECARSQGFPDNYQFAGNIQSKHRQIGNAVPPPLAFALGRKLKEAVDAKRQ | 2.1.1.37 | null | embryo development ending in seed dormancy [GO:0009793]; genomic imprinting [GO:0071514]; methylation [GO:0032259]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677] | PF01426;PF00145;PF12047; | 2.30.30.490;3.90.120.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10018}; | null | null | null | null | FUNCTION: Major CG methylase that methylates chromatin CpG residues and maintains DNA methylation (PubMed:24535433, PubMed:25002488). Plays a major role in genomic imprinting, regulation of embryogenesis and seed viability (PubMed:24535433, PubMed:25002488). Maintains DNA methylation at the FIE1 gene locus in the embryo (PubMed:24535433). {ECO:0000269|PubMed:24535433, ECO:0000269|PubMed:25002488}. | Oryza sativa subsp. japonica (Rice) |
B1V8A0 | SH3GH_CAEEL | MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQQKPQCRALFDFDAQSEGELDFKEGTLIELVSQIDENWYEGRVNGKTGLFPVTYVQVLVPLK | null | null | clathrin-dependent endocytosis [GO:0072583]; necroptotic process [GO:0070266]; synaptic vesicle uncoating [GO:0016191] | glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; presynapse [GO:0098793]; synaptic vesicle [GO:0008021] | null | PF03114;PF07653; | 1.20.1270.60;2.30.30.40; | Endophilin family | null | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Membrane {ECO:0000305|PubMed:21029864}; Peripheral membrane protein {ECO:0000305|PubMed:21029864}. Note=Localizes to neuromuscular junctions. Co-localizes with snb-1/synaptobrevin and rab-3 but not dyn-1 and apt-4 (PubMed:14622579, PubMed:21029864). Exocytosis promotes dissociation from synaptic vesicles (PubMed:21029864). {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. | null | null | null | null | null | FUNCTION: Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis (PubMed:14622579, PubMed:21029864). By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion (PubMed:21029864). In a similar manner, involved in necrotic neuronal cell death induced by abnormal hyperactivation of ion channels (PubMed:22157748). Plays a minor role in responses to mechanical stimuli (PubMed:17928447). Plays a minor role in unc-26/synaptojanin localization to synapses (PubMed:14622579). {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:17928447, ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:22157748}. | Caenorhabditis elegans |
B1VB63 | PDUB_CITFR | MSSNELVDQIMAQVIARVATPEQQAIPENNPPTRETAMAEKSCSLTEFVGTAIGDTVGLVIANVDSALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTFGDVYANEAGHIEMQYTARASYALEKAFGAPIGRACGVIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVISAREIGKTVLGTLGSEPKNDRPSYI | null | null | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469] | structural molecule activity [GO:0005198] | PF00936; | 3.30.70.1710; | EutL/PduB family | PTM: In purified BMCs seen as a 30.0 kDa and 25.0 kDa form; the smaller form is called PduB'. {ECO:0000269|PubMed:18332146}. | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}. | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) shell dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of the gene gives large amorphous intracellular structures; when only PduB is overexpressed large circular bodies are observed which contain concentric rings, whereas with PduB' overexpression internal bodies with regular straight-lined structures were generated (PubMed:18332146). The N-terminus of the long form (PduB) is required for correct formation of BMCs. May play a major role in binding the enzyme contents to the shell (By similarity). {ECO:0000250|UniProtKB:P37449, ECO:0000269|PubMed:18332146}.; FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the appearance of BMCs in its cytoplasm. {ECO:0000269|PubMed:18332146}.; FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000305|PubMed:20417607}. | Citrobacter freundii |
B1VB77 | PDUS_CITFR | MKTAMTAESTLYDAQTIRERVRAAGVVGAGGAGFPAHVKLQAQVDTFLVNAAECEPMLKVDQQLMAVQAERLIRGVQYAMTATGARAGIIALKEKYQRAINALTPLLPAGIRLHILPDVYPAGDEVLTIWMATGRRVPPAALPVSVGVVVNNVQTVLNITRAVEQQYPVTRRTLTVNGAVARPITLTVPIGMSLREVLALAGGATVDDPGFINGGPMMGGLITSLDTPVSKTTGGLLVLPKSHALIQRRMQDERTVLSVAKTVCEQCRLCTDLCPRHLIGHELSPHLLVRAVNYQQAATPQLLLTALTCSECNVCESVACPVGISPMRINRMLKRELRALNHRYEGPLNPEDEMAKYRLIPVKRLITKLGLSDWYHDAPLTETDYPTDKTTLLLRQHIGASAIPCVLQGEHVVRGQCVADVPSGALGAPVHASIDGIVSEITEQSITVIRG | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|PROSITE-ProRule:PRU00711, ECO:0000269|PubMed:21103360}; Note=Binds 2 [4Fe-4S] clusters (By similarity) (PubMed:21103360). The two centers are coupled but must possess different redox potentials (PubMed:21103360). {ECO:0000255|PROSITE-ProRule:PRU00711, ECO:0000269|PubMed:21103360}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:21103360}; Note=Binds one FMN non-covalently per monomer. {ECO:0000250|UniProtKB:Q9XDM9}; | propanediol catabolic process [GO:0051144] | bacterial microcompartment [GO:0031469]; membrane [GO:0016020] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872] | PF01512;PF13534;PF13375;PF10531; | 3.10.20.600;1.10.1060.10;3.40.50.11540; | PduS cobalamin reductase family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000250|UniProtKB:Q9XDM9}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for aquacob(III)alamin {ECO:0000269|PubMed:21103360}; KM=24.7 uM for NADH {ECO:0000269|PubMed:21103360}; | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000269|PubMed:18332146}. | null | null | FUNCTION: A bifunctional cobalamin reductase that converts cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC (PubMed:21103360). Cobalamin reduction probably occurs spontaneously in the presence of free reduced flavin nucleotides, this protein may be involved in electron transfer for this reduction (By similarity). {ECO:0000250|UniProtKB:Q9XDM9, ECO:0000269|PubMed:21103360}.; FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the appearance of BMCs in its cytoplasm. {ECO:0000305}.; FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000305|PubMed:18332146}. | Citrobacter freundii |
B1VTI5 | GRIF_STRGG | MVHVRKNHLTMTAEEKRRFVHAVLEIKRRGIYDRFVKLHIQINSTDYLDKETGKRLGHVNPGFLPWHRQYLLKFEQALQKVDPRVTLPYWDWTTDHGENSPLWSDTFMGGNGRPGDRRVMTGPFARRNGWKLNISVIPEGPEDPALNGNYTHDDRDYLVRDFGTLTPDLPTPQELEQTLDLTVYDCPPWNHTSGGTPPYESFRNHLEGYTKFAWEPRLGKLHGAAHVWTGGHMMYIGSPNDPVFFLNHCMIDRCWALWQARHPDVPHYLPTVPTQDVPDLNTPLGPWHTKTPADLLDHTRFYTYDQ | 1.10.3.15; 1.10.3.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:16282322}; Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:16282322}; | antibiotic biosynthetic process [GO:0017000]; melanin biosynthetic process [GO:0042438]; pigmentation [GO:0043473] | null | copper ion binding [GO:0005507]; o-aminophenol oxidase activity [GO:0050149]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 3-amino-4-hydroxybenzoate + H(+) + N-acetyl-L-cysteine + 2 O2 = CO2 + grixazone B + 4 H2O; Xref=Rhea:RHEA:41420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:60005, ChEBI:CHEBI:73483, ChEBI:CHEBI:78236; EC=1.10.3.15; Evidence={ECO:0000269|PubMed:16282322}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41421; Evidence={ECO:0000305|PubMed:16282322}; CATALYTIC ACTIVITY: Reaction=2 3-amino-4-hydroxybenzaldehyde + N-acetyl-L-cysteine + 2 O2 = formate + grixazone A + H(+) + 3 H2O; Xref=Rhea:RHEA:41424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:73482, ChEBI:CHEBI:78236, ChEBI:CHEBI:78237; EC=1.10.3.15; Evidence={ECO:0000269|PubMed:16282322}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41425; Evidence={ECO:0000305|PubMed:16282322}; CATALYTIC ACTIVITY: Reaction=4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O; Xref=Rhea:RHEA:40963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17293, ChEBI:CHEBI:18112; EC=1.10.3.4; Evidence={ECO:0000269|PubMed:16282322}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40964; Evidence={ECO:0000305|PubMed:16282322}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for alpha-aminophenol {ECO:0000269|PubMed:16282322}; KM=0.58 mM for 3,4-AHBAL {ECO:0000269|PubMed:16282322}; KM=0.75 mM for 2-amino-4-methylphenol {ECO:0000269|PubMed:16282322}; KM=0.41 mM for 3,4-dihydroxybenzaldehyde {ECO:0000269|PubMed:16282322}; KM=19 mM for catechol {ECO:0000269|PubMed:16282322}; KM=5.5 mM for L-DOPA {ECO:0000269|PubMed:16282322}; Note=kcat is 20 sec(-1) with alpha-aminophenol as substrate. kcat is 14 sec(-1) with 3,4-AHBAL as substrate. kcat is 18 sec(-1) with 2-amino-4-methylphenol as substrate. kcat is 0.8 sec(-1) with 3,4-dihydroxybenzaldehyde as substrate. kcat is 12 sec(-1) with catechol as substrate. kcat is 0.066 sec(-1) with L-DOPA as substrate. {ECO:0000269|PubMed:16282322}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8.5 and 10.5. {ECO:0000269|PubMed:16282322}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:16282322}; | FUNCTION: Involved in the biosynthesis of the parasiticide antibiotic grixazone. Catalyzes the oxidation of 3-amino-4-hydroxybenzoate (3,4-AHBOA) to yield the corresponding quinone imine which is then non-enzymatically conjugated with the thiol group of N-acetylcysteine. The resultant compound is oxidized to its quinone imine enzymatically and is then dimerized non-enzymatically with another quinone imine oxidized by GriF to yield grixazone B. 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) can also be used as substrate to yield grixazone A. In the grixazone biosynthetic pathway, it can also function as an o-aminophenol oxidase that catalyzes the formation of the phenoxazinone chromophore from alpha-aminophenol. It can also use 2-amino-4-methylphenol, and to a lesser extent, 3,4-dihydroxybenzaldehyde, catechol and 3,4-dihydroxy-L-phenylalanine (L-DOPA) as substrates. In contrast to tyrosinases, it does not display monophenolase activity. {ECO:0000269|PubMed:16282322, ECO:0000303|PubMed:19268377}. | Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
B1W019 | GCOA_STRGG | MSQITLPAFHMPFQSAGCHPGLAETREAAWEWAAAEGLDLSVPARRKMIRTRPELWISLIFPQATQAHLDLFCQWLFWAFLVDDEFDDGPAGRDPLMCERAIARLVDVFDGAAPNGPMERALAGLRDRTCRGRSPQWNRQFRRDTAAWLWTYYAEAVERAAGQVPSRAEFAKHRRDSVAMQPFLCLHEITAGIDLPDSARSLPAYIALRNAVTDHSGLCNDICSFEKEAALGYEHNAVRLIQRDRGSTLQEAVDEAGIQLARIAERVQRAERELIEEIEAAGIDGPTRTALERCVRDYRGLVRGDFDYHARAERYTRPDLVELDERDSLSRHFAA | 4.2.1.138; 4.2.3.89 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21693706}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21693706}; Note=Binds 3 Mg(2+) ions per subunit. To a lesser extent, can also use Mn(2+) instead of Mg(2+). Cannot use Fe(2+), Co(2+), Zn(2+), Ni(2+), or Cu(2+). {ECO:0000269|PubMed:21693706}; | sesquiterpene biosynthetic process [GO:0051762]; sesquiterpenoid biosynthetic process [GO:0016106] | null | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances [GO:0016823]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; sesquiterpene synthase activity [GO:0010334] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:31815, ChEBI:CHEBI:33019, ChEBI:CHEBI:63190, ChEBI:CHEBI:175763; EC=4.2.3.89; Evidence={ECO:0000269|PubMed:21693706}; CATALYTIC ACTIVITY: Reaction=(+)-(E)-beta-caryophyllene + H2O = (+)-caryolan-1-ol; Xref=Rhea:RHEA:31795, ChEBI:CHEBI:15377, ChEBI:CHEBI:63190, ChEBI:CHEBI:63196; EC=4.2.1.138; Evidence={ECO:0000269|PubMed:21693706}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=95.6 nM for farnesyl diphosphate (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:21693706}; Note=kcat is 0.025 sec(-1) for (+)-caryolan-1-ol formation (at pH 7.5 and 30 degrees Celsius).; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for (+)-caryolan-1-ol synthesis. {ECO:0000269|PubMed:21693706}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for (+)-caryolan-1-ol synthesis. {ECO:0000269|PubMed:21693706}; | FUNCTION: Sesquiterpene cyclase that first catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (+)-beta-caryophyllene intermediate, and then its conversion to (+)-caryolan-1-ol via a second cyclization and the addition of a water molecule. {ECO:0000269|PubMed:21693706}. | Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) |
B1WAR9 | GWL_XENTR | MGVVVAETSQNGDISLLSEKKFTVPQPPSIEEFSIVKPISRGAFGKVYLARRKNNNKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLIMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLKRELSMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPVGGRTQGSIAQQTEGMRGNASTPLLMKKKENSVKGNKLMISCPEAGLSSPSMPVKCLTPNLLKCRTPFTTSSTSSQSRICLSSLESECGMSPRWENCSQDAEAPPYLNSSRVKDCSSEQARSKKPMGSSASQNLKHLEFAFSPIVDRRTGKKAGFQDETGELSDTPLATLGAKGVIRKCLYDNNAQEKHKDLGKDDQGELEKLTISPDSPPWLANGSVAPIQFNDDEIIEKMGIKRNYDLVEKSPEQEVLQDKKTNTDYKRGCTITGYPVSQSTGLTMEINSLFLSELRSSTNNYASDRKSEDDYISAPRTHENLGSGNTIAKNLLCELDDNCERDGEANSNSGCEEGENQKESLNQDSESSSADMSVTENQIERELCQVDKSIKELSFEESPSESNEETTPENKGMAFMAENDALKREPNRSVLPETLHNVLASPAPTSAMAHPRRKPMVAFRSYNSPINGSNLSEPSRISMNSADKIHFSLGCTGSFPMAVTPAQKKVQGLTETPYRTPKTVRRGGLQAENERILGTPDYLAPELLLGKSHGPAVDWWALGVCLFEFLTGIPPFNDETPSQVFQNILNRDIPWPEEEETLSVNAQSAIEILLAIDQTKRAGLKDLKAHHLFHAIEWDDLQNLPMPFIPQPDDETDTTYFEARNNAQHLKVSGFSL | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-752 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | 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 that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and ensa at 'Ser-67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). {ECO:0000250}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B1WBP0 | MPPD2_RAT | MAHGIPSQGKVTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDKEFMADLVKQDYYRFPSVSKLKPEDFDNVQSLLTNSIYLQDSEVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGTDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGTMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19004815, ECO:0000269|PubMed:21824479}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:19004815}; | null | null | AMP binding [GO:0016208]; GMP binding [GO:0019002]; manganese ion binding [GO:0030145]; phosphoric diester hydrolase activity [GO:0008081] | PF00149; | 3.60.21.10; | UPF0046 family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for p-nitrophenyl phenyphosphonate {ECO:0000269|PubMed:19004815}; KM=1.5 mM for manganese {ECO:0000269|PubMed:19004815}; Vmax=8 umol/min/mg enzyme with p-nitrophenyl phenyphosphonate as substrate {ECO:0000269|PubMed:19004815}; | null | null | null | FUNCTION: Displays low metallophosphoesterase activity (in vitro) (PubMed:19004815, PubMed:21824479). May play a role in the development of the nervous system (Probable). {ECO:0000269|PubMed:19004815, ECO:0000269|PubMed:21824479, ECO:0000305}. | Rattus norvegicus (Rat) |
B1WC10 | FRITZ_RAT | MSFCLTELHLWSLKSTLHIADRDIGVYQYYDKKDLPVSAAEHGNLEEKQRLAESRDYPWTLKNRRPEKLRDSLKELEELMQNSQCVLCQWKSKHICQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFAKKMDSLDVNKRLEKLSALDYKISYHDIPGPATRTVDRHLAINSTQDLAVCWWPLLSDDAWPWTPIASEKDRANMLLLGFTQGGLEVLSSVRTEWNPLDVHFGTRQPYQVFTVECSFSVDQEPMADSCIYESVRNKLHCVSVTRIPLRSKAISCCKNSTEDKLIVGCEDSSVILYEAHRGVTLLAQAELMPSLISCHPSGAILLVGSNQGELQVFDIALSPINIQLLAEDCLPKETLQFNKFFDFSSSLVHMQWIAPPIVFQKPKRGEICDLLFLRFNRGPLGVLLFKLGVLRRGQLGLVDLIFQYIHCDEVYEAVSVLSSMNWDTLGQQCFISMSTIVNHLLRQRLTPEREAQLEASLGTFYAPARPLLDTTVLAYRDPVGTYARRLFHHLLRYQRFEKAFLLAVDIGARDLFMDIHYLALDMGELALAEVARRRADDIDVESVCSGVELLGPLDRRDMLNEGFAGSALTPEGGNPFPDLLPSSGSTPKHTIQQKIPNGPSNRRAIERKNEVMEETEEEEEEEEEAAACTDSSVATTWDAEGELREDHRRQDTEDVGSLRMVHFGLV | null | null | auditory receptor cell morphogenesis [GO:0002093]; camera-type eye development [GO:0043010]; cilium assembly [GO:0060271]; cilium organization [GO:0044782]; circulatory system development [GO:0072359]; digestive system development [GO:0055123]; embryonic digit morphogenesis [GO:0042733]; embryonic organ development [GO:0048568]; establishment of protein localization [GO:0045184]; kidney development [GO:0001822]; nervous system development [GO:0007399]; podocyte cell migration [GO:0090521]; regulation of embryonic cell shape [GO:0016476]; regulation of establishment of cell polarity [GO:2000114]; regulation of fibroblast migration [GO:0010762]; regulation of focal adhesion assembly [GO:0051893]; regulation of protein localization [GO:0032880]; regulation of ruffle assembly [GO:1900027]; respiratory system development [GO:0060541]; roof of mouth development [GO:0060021]; septin cytoskeleton organization [GO:0032185]; smoothened signaling pathway [GO:0007224]; tongue morphogenesis [GO:0043587] | axonemal basal plate [GO:0097541]; axoneme [GO:0005930]; plasma membrane [GO:0005886] | null | PF11768; | 2.130.10.10; | WD repeat fritz family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q32NR9}. | null | null | null | null | null | FUNCTION: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). {ECO:0000250|UniProtKB:Q32NR9, ECO:0000250|UniProtKB:Q8C456}. | Rattus norvegicus (Rat) |
B1WC40 | NCBP2_RAT | MSGGLLKALRSDSYVELSEYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYREDYDAGRGGYGKLAQKQ | null | null | histone mRNA metabolic process [GO:0008334]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA export from nucleus [GO:0006406]; mRNA metabolic process [GO:0016071]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transcription by RNA polymerase II [GO:0042789]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of RNA export from nucleus [GO:0046833]; regulation of translational initiation [GO:0006446]; regulatory ncRNA-mediated gene silencing [GO:0031047]; RNA splicing [GO:0008380]; snRNA export from nucleus [GO:0006408] | cytoplasm [GO:0005737]; nuclear cap binding complex [GO:0005846]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA cap binding complex [GO:0034518] | DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA cap binding [GO:0000339]; snRNA binding [GO:0017069] | PF00076; | 3.30.70.330; | RRM NCBP2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm {ECO:0000250|UniProtKB:P52298}. | null | null | null | null | null | FUNCTION: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (By similarity). {ECO:0000250|UniProtKB:P52298}. | Rattus norvegicus (Rat) |
B1WC58 | CTIP_RAT | MSISGSSCGSPNSTDISSDFKELWTKLKEYHDKEVQGLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRLITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELECEENIIPDSPITSFSFSGINRLRRKENLHVRYVEQTHTKLEHSACTSELRKFSKGSTPAPVNSEEHEILVADTCDQSHSPLSKICGTSSYPADKLSSNLDAVVAETLGLDGQEESEPQGPVSPLGNELYHCLKEDHKKQPFMESAIRNEDNVRFSDSASKAPPRELTTRGSSPVFGPTSTVKTHLGLKTSFSPSLLDSGKKNLLSTAPFSSISVSRSEKVRSKSEDNALFTQQSAGSEVKVISQSFPSKQILTSKNVSDSVDEQGGADHMKDAVSDKHLVPLKSLGGKASKRKRTEEEGEHAVHCPQTCFDKENALPFPMENQFPVNGDHVMDKPLDLSDRFAANQRQEKNHGDETCKHKLKQVTIYEALKPVPKGSSSGRKALSGACTLAQDSAETYCLQQRTLQCSSKFSPDHNTQLQIKEENPVFKTPPRSQESLETENLFGDVKGIGSLVPIKVKGRSAHGGCELASVLQLNPCRVAKTKSLPSNHDMSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETMLLKMKKQEQREKSPNGDIKMNDSLEDMFDRTTHEEYESCLADNFSQVPDEEELSDTTKKPNIHGDKQDGIKQKAFVEPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPTNTPENFWEVGFPSTQTCLERGYIKEDLDPCPRPKRRQPYNAVFSPKGKEQRT | 3.1.-.- | null | blastocyst hatching [GO:0001835]; cell division [GO:0051301]; DNA double-strand break processing involved in repair via single-strand annealing [GO:0010792]; double-strand break repair via homologous recombination [GO:0000724]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic cell cycle [GO:0051321]; response to estradiol [GO:0032355] | BRCA1-C complex [GO:0070533]; chromosome [GO:0005694]; transcription repressor complex [GO:0017053] | damaged DNA binding [GO:0003684]; identical protein binding [GO:0042802]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]; transcription corepressor activity [GO:0003714] | PF10482;PF08573; | null | COM1/SAE2/CtIP family | PTM: Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylation at Thr-843 and Thr-855 promote interaction with NBN and recruitment to double-strand breaks (DSBs). Phosphorylated on Ser-326 as cells enter G2 phase. Phosphorylated on Ser-326 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (By similarity). Phosphorylation at Ser-276 may serve as a PIN1 isomerization site (By similarity). Phosphorylation is not required for tetramerization (By similarity). Binds to DNA more strongly when dephosphorylated (By similarity). {ECO:0000250|UniProtKB:Q99708}.; PTM: Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteasomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation (By similarity). Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q99708}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chromatin following DNA damage. {ECO:0000250|UniProtKB:Q99708}. | null | null | null | null | null | FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (By similarity). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (By similarity). {ECO:0000250|UniProtKB:Q80YR6, ECO:0000250|UniProtKB:Q99708}. | Rattus norvegicus (Rat) |
B1WC61 | ACAD9_RAT | MSGYVLFSRGATAAAAAARASRVLRVFTERRRTLHTSLQSCSFAKELFLGHIQQKGVFPFPEVSQEELSEINQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQHAGRILTSRIKELKSGNVTTVMETIGRKLRDSLGRTVDLGLSSNIAVVHPSLGDSANKLEENVHYFGRTVETLLLRFGKTIVEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLKNHDHEILLANMFCVEAYFQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRAS | 1.3.8.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9H845}; | leucine catabolic process [GO:0006552]; long-chain fatty acid metabolic process [GO:0001676]; medium-chain fatty acid metabolic process [GO:0051791]; mitochondrial respiratory chain complex I assembly [GO:0032981] | dendrite [GO:0030425]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991] | PF21343;PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H845}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H845}; Matrix side {ECO:0000250|UniProtKB:Q9H845}. Note=Essentially associated with membranes. {ECO:0000250|UniProtKB:Q9H845}. | CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + nonanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-nonenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48208, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:76291, ChEBI:CHEBI:76292; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48209; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentadecanoyl-CoA = (2E)-pentadecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48204, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74309, ChEBI:CHEBI:77545; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48205; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + undecanoyl-CoA = reduced [electron-transfer flavoprotein] + trans-2-undecenoyl-CoA; Xref=Rhea:RHEA:48200, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77547, ChEBI:CHEBI:77548; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48201; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47304, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61540, ChEBI:CHEBI:77549; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47305; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + heptadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = reduced [electron-transfer flavoprotein] + trans-2-heptadecenoyl-CoA; Xref=Rhea:RHEA:48196, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74307, ChEBI:CHEBI:77551; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48197; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9E)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48192, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77537, ChEBI:CHEBI:77552; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48193; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,9Z,12Z)-octadecatrienoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48188, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57383, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77558; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48189; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E,4Z,7Z,10Z,13Z,16Z,19Z)-docosaheptaenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48184, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74298, ChEBI:CHEBI:77559; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48185; Evidence={ECO:0000250|UniProtKB:Q9H845}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; Evidence={ECO:0000250|UniProtKB:Q9H845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; Evidence={ECO:0000250|UniProtKB:Q9H845}; | null | null | null | null | FUNCTION: As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation. This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs. However, in vivo, it does not seem to play a primary role in fatty acid oxidation. In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein. {ECO:0000250|UniProtKB:Q9H845}. | Rattus norvegicus (Rat) |
B1WC68 | HDAC8_RAT | MEIPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV | 3.5.1.-; 3.5.1.98 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q9BY41}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q9BY41}; | cellular response to forskolin [GO:1904322]; cellular response to trichostatin A [GO:0035984]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein modification process [GO:0031400]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of protein stability [GO:0031647]; regulation of telomere maintenance [GO:0032204]; response to 11-deoxycorticosterone [GO:1903496] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; deacetylase activity [GO:0019213]; histone deacetylase activity [GO:0004407]; histone decrotonylase activity [GO:0160009]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; metal ion binding [GO:0046872]; protein lysine deacetylase activity [GO:0033558] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 (By similarity). {ECO:0000250|UniProtKB:Q9BY41}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BY41}. Chromosome {ECO:0000250|UniProtKB:Q9BY41}. Cytoplasm {ECO:0000250|UniProtKB:Q9BY41}. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation. {ECO:0000250|UniProtKB:Q9BY41}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000250|UniProtKB:Q9BY41}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000250|UniProtKB:Q9BY41}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q9BY41}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; Evidence={ECO:0000250|UniProtKB:Q9BY41}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q9BY41}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; Evidence={ECO:0000250|UniProtKB:Q9BY41}; | null | null | null | null | FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones. {ECO:0000250|UniProtKB:Q9BY41}. | Rattus norvegicus (Rat) |
B1X6B7 | HCHA_ECODH | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli (strain K12 / DH10B) |
B1XJV9 | CRTE_PICP2 | MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN | 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | null | metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:32523588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409; Evidence={ECO:0000305|PubMed:32523588}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000269|PubMed:32523588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362; Evidence={ECO:0000305|PubMed:32523588}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:32523588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000305|PubMed:32523588}; | null | PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.; PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32523588}. | null | null | FUNCTION: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids. {ECO:0000269|PubMed:32523588}. | Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
B1YAL1 | FBPAP_PYRNV | MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEVTDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDPSMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVRAQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDLFDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTALPKILAKVKPYPADQYEKDRKKYIEAVVKGAKVEESQHD | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21983965}; | gluconeogenesis [GO:0006094] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287] | PF01950; | 6.10.250.1180; | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965}; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906}. | null | null | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965}. | Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus) |
B2AXJ5 | HETQ1_PODAN | MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA | null | null | programmed cell death [GO:0012501] | plasma membrane [GO:0005886] | wide pore channel activity [GO:0022829] | null | null | Gasdermin family | PTM: [Gasdermin-like protein het-Q1]: The precursor form is cleaved by het-Q2, generating the pore-forming protein (Gasdermin-like protein het-Q1, N-terminal). {ECO:0000269|PubMed:35135876}. | SUBCELLULAR LOCATION: [Gasdermin-like protein het-Q1, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:P57764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. | null | null | null | null | null | FUNCTION: [Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) (PubMed:35135876). In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09) (PubMed:35135876). This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N-terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death (PubMed:35135876). {ECO:0000269|PubMed:35135876}.; FUNCTION: [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming protein that causes membrane permeabilization and cell death (PubMed:35135876). Released upon cleavage and maturation by het-Q2 and binds to membrane inner leaflet lipids (PubMed:35135876). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering cell death (By similarity). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:35135876}. | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2B223 | ARO1_PODAN | MTSSTGSGPTRISILGKDDIIVDHGIWLDFVTHDLLQNIPSSTYVLITDTNLHDTYVPAFQEVFERAAGQDARLLTYTIPPGEYSKGRETKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLETLPVREFINGMAEVIKTAAIWNETEFTALEDNAPAILEAIRSKPTGTGARLAPIRDILKRIVLGSAGVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQVLHGECVAIGMVREAELARFLGVLPPGAVARLTKCIASYELPTSLHDKRIVKLTAGKECPVDVLLQKMGVDKKNDGRKKKVVLLSAIGKTYEPKATVVEDRAIRIVLSPSVRVTPGVPKGLNVSVTPPGSKSISNRALVLAAMGEGTTRIKGLLHSDDTHYMLTAIAQLQGATYTWEEAGEVLVVKGRGGKLLASNEPLYLGNAGTASRFLTSVVALCSPTDTTTSTVLTGNARMKVRPIGPLVDALRSNGVAVKYLEKENSLPVQVDAVSGFAGGVIELAATISSQYVSSILMAAPYARQPVVLKLVGGKPISQFYIDMTIAMMASFGVKVERDAEDPNTYHIPQGSYKNPEEYVVESDASSATYPLAVAAITGTTCTIPNIGRTSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPPVGALKAIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDELAKFGVHCSELEDGIEVTGKPYKELANPEPIYCYDDHRVAMSFSVLSVLAPHKVLILERECTAKTWPGWWDILSQKFNVHLEGEEDPTKKCTAKSSRPSTDRSIFIVGMRGAGKSTAGRWMSDILKRPLIDLDVELEKREKATIPEIIRSERGWEGFRKAELELLEDMIKNNSKGHVFSCGGGLVETEAARKLLISYQKNGGSVLLVHRDTDQVVEYLMRDKTRPAYSENIREVYYRRKPWFEEVSNFQYHSPHHNGSEEAPEDFSRFLSVISGSSTHFEDVLAKKHSFFVSLTVPNVAKALDIIPKVVVGSDAVELRVDLLESLNPEFVATQVALLRSAAKIPIVYTIRTISQGGKFPDDDYKRALELYQIGLRTGVEYLDLEMTMPEDVLQTVTETKGFTHIIASHHDPENKLSWKNGGWIPFYNKALQYGDVIKLVGMAREVSDNFDLTNFKMRMLEAHKKPIIALNMGTAGKLSRVLNGFLTPVSHPALPSKAAPGQLSAAEIRQALSLVGELEPKSFYLFGKPISSSRSPALHNGLFAQTGLPHQYSLFETDVAADVKDIIRSADFGGASVTIPLKLDIIPLLDEVSDAATAIGAVNTVIPVSPEGSDKTILRGDNTDWMGMVFSLRQAGIAPRTKTNPGAGMVVGSGGTTRAAVYALHDLGYSPIHIVARSPDRVKAIADSFPEDYNIQTLSTPEEVKAATDALPTVVISSIPADKPIDQSMREVLVASLRHPAKSEKEPRVLLEMAYTPRHTPLMQLAEDAGWKTIPGLEVLAAQGWYQFQLWTGVTPLYADARAAVMGDSE | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2B3C0 | MANA_PODAN | MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA | 3.2.1.78 | null | mannan catabolic process [GO:0046355] | extracellular region [GO:0005576] | mannan endo-1,4-beta-mannosidase activity [GO:0016985] | PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | PTM: Not glycosylated. {ECO:0000269|PubMed:23558681}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:21037302}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mg/ml for konjac glucomannan {ECO:0000269|PubMed:21037302}; KM=1.7 mg/ml for carob galactomannan {ECO:0000269|PubMed:21037302}; KM=4.7 mg/ml for locust bean gum galactomannan {ECO:0000269|PubMed:21037302}; KM=1.6 mg/ml for ivory nut mannan {ECO:0000269|PubMed:21037302}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:21037302}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:21037302}; | FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose (PubMed:21037302). Also has transglycosylation activity (PubMed:23558681). {ECO:0000269|PubMed:21037302, ECO:0000269|PubMed:23558681}. | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
B2C4D0 | TS23B_MAIZE | MAADEARSVSRLHSEEDMHGKHHSTLWGDFFLHHVPCRPGQYLIMKDNVEIMKEEVKKMLLDVGSSDLSHKLDCIDTLERLGLDYHYTKEIDELMCNVFEARDQDLDLTTTSQLFYLLRKHGYHISSDVFLKFRDDKGDIVTNDARCLLRMYEAAHVRVNGEEILDNILIHTKRQLQCIVDDLEPTLQEEVRYALETPLFRRLNRVQARQFISTYEKSTTRINMLLEFSKLDFNILLTLYCEELKDLTLWWKEFQAQANTTIYARDRMVEMHFWMMGVFFEPQYSYSRKMLTQLFMIVSVLDDLYDSHCTTEEGNAFTAALQRWDEEGVEQCPTYLRTLYTNIRATIKAIEEDLNFQNNKHAKLVKGLIIDMAMCYNAETEWRDKKYVPATVDEHLKISARSSGCMHLVSQGFISMGDVATSEALEWASTYPKIVRAVCIIARLANDIMSYKREASNNTMVSTVQTCAKEYGTTTVEQAIEKIRELIEEAWMDITHECLRQPQPKALLERAVNLARTMDFLYKDADGYTDSRSIKGILDSLYVHLID | 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18296628}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18296628}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q5GJ60}; | beta-caryophyllene biosynthetic process [GO:1901937]; defense response to insect [GO:0002213]; diterpenoid biosynthetic process [GO:0016102]; farnesyl diphosphate catabolic process [GO:0045339]; response to herbivore [GO:0080027]; response to insect [GO:0009625]; sesquiterpene biosynthetic process [GO:0051762]; terpenoid biosynthetic process [GO:0016114] | cytoplasm [GO:0005737] | (-)-E-beta-caryophyllene synthase activity [GO:0080016]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:18296628}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:18296628}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for farnesyl diphosphate (in the presence of MgCl(2)) {ECO:0000269|PubMed:18296628}; KM=1.1 uM for farnesyl diphosphate (in the presence of MnCl(2)) {ECO:0000269|PubMed:18296628}; Note=kcat is 0.00191 sec(-1) with farnesyl diphosphate (in the presence of MgCl(2)). kcat is 0.0013 sec(-1) with farnesyl diphosphate (in the presence of MnCl(2)). {ECO:0000269|PubMed:18296628}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000250|UniProtKB:Q84ZW8}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9.5. {ECO:0000269|PubMed:18296628}; | null | FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Sesquiterpene synthase that converts farnesyl diphosphate to (E)-beta-caryophyllene (PubMed:18296628). Involved in indirect defense by producing volatile signals that attract natural enemies of leaf herbivores such as Chilo partellus and root herbivores like the western corn rootworm (WCR, Diabrotica virgifera) and fall armyworm (Spodoptera littoralis and Spodoptera frugiperda) (PubMed:18296628, PubMed:28428873, PubMed:29151152). Deters leaf herbivores by triggering (E)-beta-caryophyllene production upon insect (stemborer C.partellus) egg deposition; (E)-beta-caryophyllene attracts the parasitic wasp Cotesia sesamiae which lays eggs on the larvae of C.partellus, which is ultimately fatal (PubMed:28428873). {ECO:0000269|PubMed:18296628, ECO:0000269|PubMed:28428873, ECO:0000269|PubMed:29151152, ECO:0000303|PubMed:30187155}. | Zea mays (Maize) |
B2C4J0 | GLYC_CHAVB | MGQLVSFFQEIPNIIQEAINIALIAVSLIAILKGLVNLWKSGLFQLLVFLILAGRSCSFKIGRSTELQNITINMLKVFEDHPISCTVNKTLYYIRESENATWCVEIAALDMSVLLSPHDPRVMGNLSNCVHPDIKHRSELLGLLEWILRALKYDFLNYPPLLCEKVTSSVNETRIQINVSDSAGSHDFKETMLQRLAILFGTKLMFDKTPKQFIVIRNQTWVNQCKSNHVNTLHLMMANAGHAVKLRRLQGVFTWTITDAAGNDMPGGYCLERWMLVTSDLKCFGNTALAKCNLNHDSEFCDMLKLFEFNKKAIESLNDNTKNKVNLLTHSINALISDNLLMKNRLKELLDTPYCNYTKFWYVNHTITGEHSLPRCWMVKNNSYLNESEFRNDWILESDHLLSEMLNKEYFDRQGKTPITLVDICFWSTLFFTTTLFLHLVGFPTHRHIQGEPCPLPHKLNSNGGCRCGRYPELKKPTTWHRKH | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase. {ECO:0000255|HAMAP-Rule:MF_04084}. | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. {ECO:0000255|HAMAP-Rule:MF_04084}. | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: Glycoprotein G1: Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor leading to virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: [Glycoprotein G2]: Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification. {ECO:0000255|HAMAP-Rule:MF_04084}. | Chapare mammarenavirus (isolate Human/Bolivia/810419/2003) |
B2C6R6 | TAFCL_ARATH | MAEPIPSSSLSPKSLQSPNPMEPSPASSTPLPSSSSQQQQLMTAPISNSVNSAASPAMTVTTTEGIVIQNNSQPNISSPNPTSSNPPIGAQIPSPSPLSHPSSSLDQQTQTQQLVQQTQQLPQQQQQIMQQISSSPIPQLSPQQQQILQQQHMTSQQIPMSSYQIAQSLQRSPSLSRLSQIQQQQQQQQHQGQYGNVLRQQAGLYGTMNFGGSGSVQQSQQNQQMVNPNMSRAALVGQSGHLPMLNGAAGAAQMNIQPQLLAASPRQKSGMVQGSQFHPGSSGQQLQGMQAMGMMGSLNLTSQMRGNPALYAQQRINPGQMRQQLSQQNALTSPQVQNLQRTSSLAFMNPQLSGLAQNGQAGMMQNSLSQQQWLKQMSGITSPNSFRLQPSQRQALLLQQQQQQLSSPQLHQSSMSLNQQQISQIIQQQQQQSQLGQSQMNQSHSQQQLQQMQQQLQQQPQQQMQQQQQQQQQMQINQQQPSPRMLSHAGQKSVSLTGSQPEATQSGTTTPGGSSSQGTEATNQLLGKRKIQDLVSQVDVHAKLDPDVEDLLLEVADDFIDSVTSFACSLAKHRKSSVLEPKDILLHLEKNLHLTIPGFSSEDKRQTKTVPTDLHKKRLAMVRALLESSKPETNASNSKETMRQAMVNPNGPNHLLRPSQSSEQLVSQTSGPHILQHMTRY | null | null | RNA polymerase II preinitiation complex assembly [GO:0051123] | SAGA complex [GO:0000124]; SLIK (SAGA-like) complex [GO:0046695]; transcription factor TFIID complex [GO:0005669] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; TBP-class protein binding [GO:0017025] | PF03847; | 1.10.20.10; | TAF12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21357579}. | null | null | null | null | null | FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Required for the expression of a subset of ethylene-responsive genes (By similarity). Involved in the negative regulation of cytokinin sensitivity. {ECO:0000250, ECO:0000269|PubMed:21357579}. | Arabidopsis thaliana (Mouse-ear cress) |
B2D6K9 | PPH6R_CAEEL | MFWAKEEEENSLMRLLKTDNFTLEDVLLNEFVVQESRYGKAELVQYITSRENMKALLELSLNPKINTDLPMKQQYRLSFIASEILTIRGTDVFQKQIVTTEETRKCLVDFLNDKTPLNHLVAGFFAKIMECLLSRHFDLFQTFSLLQETKFFDKCLRNINLGAIECLLENLVRIPTTSEGTRIVKEWMISENLFEKIVDRMRESETDDEKECLAEVYCEILRELRDKLYIMESKVDELHAKSMDETLIAKIADNLIVEEGCPAEELVKKSALISASAKILEAFIKTNFVSNAPAQQLEEIERNLIEERHYSYGLMRPCMDNDPYEHSYQPDPERIVEGILANRLPNILQTVLRDIEANGSVWQPLLRLIIELCNTNCMSTHEKIAVAFRSLPFINLIKAAKMLPRASVLHCLLVKVVILLLHSSFPCDELSPAAEYLLTEGGLIQNIYDTATSPNPGSSVACSGLRSFNQNLGDAINRAKKAGIPNQKLLAILSADNTWTELEDIIHLYNLKHRPQMQHDFNDSSVVSSIRNDSHGFNDSEEWTDASTKFAEMDATSSAKQAFSGFSSPFEPNMQRFSDFEGQFDDTPDEDEFRKLCSERANSSSCAGISFETSPIKWPGEAEKTSEKASEPPSVVASTYPQQTNGNQAFLEQEEGDGEWVWPTVPPLGETEVVTQTGHRPENNWVDETAPDFSHLDMAPPKEDDMWADFSSFPTISPTAAANSASSSSSDAWPGSDIHLQGEASDWPLNNSHESKASDPVMVGLAASISHPGDSSEA | null | null | actomyosin contractile ring contraction [GO:0000916]; cortical actin cytoskeleton organization [GO:0030866]; establishment of mitotic spindle localization [GO:0040001]; first cell cycle pseudocleavage [GO:0030590]; positive regulation of mitotic cell cycle [GO:0045931]; spindle localization [GO:0051653] | astral microtubule [GO:0000235]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; phosphatase complex [GO:1903293]; spindle pole [GO:0000922] | protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888] | PF04499; | null | SAPS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20040490}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes mainly to the cytoplasm and to a lesser extent with microtubule asters. {ECO:0000269|PubMed:20040490}. | null | null | null | null | null | FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6) (Probable). In complex with pph-6, promotes actomyosin contractility during cytokinesis by regulating the organization of cortical non-muscle myosin II nmy-2 and thus contributing to correct spindle positioning (PubMed:20040490). Also required for the proper generation of pulling forces on spindle poles during anaphase by regulating the cortical localization of gpr-1, gpr-2 and lin-5 (PubMed:20040490). Negatively regulates kinase air-1 localization at the cell cortex (PubMed:27335426). {ECO:0000269|PubMed:20040490, ECO:0000269|PubMed:27335426, ECO:0000305|PubMed:20040490}. | Caenorhabditis elegans |
B2D6M2 | LIN61_CAEEL | MLKLVILCFALFYNTVSSTRFLFGVEVKCDFDEVFQLTVSHWEDDGNTFWDRDEDITGRMTMFARKKIFFYQDGHHGFEFGKLEPYGWFLHNCTKNGNFREYRHGLSSTSGSNGLEYIEYTMSEFLKIVRANKKSDRKLDKTYLWESYLHQFEKGKTSFIPVEAFNRNLTVNFNECVKEGVIFETVVHDYDKNCDSIQVRWFARIEKVCGYRVLAQFIGADTKFWLNILSDDMFGLANAAMSDPNMDKIVYAPPLAINEEYQNDMVNYVNNCIDGEIVGQTSLSPKFDEGKALLSKHRFKVGQRLELLNYSNSTEIRVARIQEICGRRMNVSITKKDFPESLPDADDDRQVFSSGSQYWIDEGSFFIFPVGFAAVNGYQLNAKKEYIEHTNKIAQAIKNGENPRYDSDDVTFDQLAKDPIDPMIWRKVKVGQKFELIDPLAQQFNNLHVASILKFCKTEGYLIVGMDGPDALEDSFPIHINNTFMFPVGYAEKYNLELVPPDEFKGTFRWDEYLEKESAETLPLDLFKPMPSQERLDKFKVGLRLEAADMCENQFICPATVKSVHGRLINVNFDGWDEEFDELYDVDSHDILPIGWCEAHSYVLQPPKKYNY | null | null | negative regulation of DNA-templated transcription [GO:0045892]; vulval development [GO:0040025] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; methylated histone binding [GO:0035064] | PF02820; | 2.30.30.140; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409073}. Chromosome {ECO:0000269|PubMed:17409073}. | null | null | null | null | null | FUNCTION: Synthetic multivulva class B (synMuvB) protein required to repress the induction of vulval development by Ras signaling. Unlike other synMuv proteins it does not associate with the multiprotein DRM complex and the NuRD-like complex. Interaction with methylated histone H3 is essential for vulva development. It has a role in maintaining genome stability. {ECO:0000269|PubMed:17409073, ECO:0000269|PubMed:21437264}. | Caenorhabditis elegans |
B2D6P4 | TBPL1_CAEEL | MQMGDHQMMGNQRYYRTYVQKVMPAQAGGAVSQNATYVQTAGIRTVHHDGNGQQRIVQLPPGVRQIQQNGVGPAYVRQVPGGQPMQVNFGHPGTIAGRNVAVGVQMRPVQGHNVQQGYQRQQVANQIQQQNRAVFMAQNQQGQQQISYAQAQHRQQQQNQQQHHQQPQHFNHPSQQNQMIMQHRQPQMHHNQQHQMVQPQMTRHQMAQHHAQQPHPQIYVPRDMNLAVPLREPSPEPIPVKIEVPDVPPEGTSAANEEPMPDDGDIDIQIRNVVCNYTLPLHIDLRKLAMNTHNVTYEREKGVMMKQKRSPGCYIKVYSSGKVYIVGCRSEADCKRAARSIARHVQRVMGKTKERVSIRNYRVNNVLATCRLPFGIKIEEVAAKYPSESTYEPELSVGLVWRSVTPKATLRIHTTGSITVTGAQSEADVLEVLSKIYPIVLEFRCLERAKGNVAAQKKRKRKAPVNRGPPIKRERFDDSNYRNSGVINNQVYFSDEDEDLYDELDLEE | null | null | DNA-templated transcription initiation [GO:0006352]; embryo development ending in birth or egg hatching [GO:0009792]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA binding [GO:0003677]; general transcription initiation factor activity [GO:0140223] | PF00352; | 3.30.310.10; | TBP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11030349, ECO:0000269|PubMed:11030350, ECO:0000269|PubMed:14726532}. | null | null | null | null | null | FUNCTION: May be a general transcription factor (PubMed:11030349, PubMed:11030350). Plays an essential role for RNA polymerase II/ama-1 transcription in early embryos whereby it activates a subset of RNA polymerase II promoters and facilitates the reestablishment of transcription after mitosis (PubMed:14726532). {ECO:0000269|PubMed:11030349, ECO:0000269|PubMed:11030350, ECO:0000269|PubMed:14726532}. | Caenorhabditis elegans |
B2DBE9 | GGS4_PHOAM | MDFPIRSQARLYPAQCVTFCLYVRVPPLSEWNFLKMQTDARPSATWPSVPKVHKRNRSTSLSDQQTAKKAHANHARLHLPQPIEPVYESQNGSVSQSEEKSSAVEINNSAAGDPQRFAVADLNFSWAEEEEKVVLAPYDYVASNSGKEFRTLILNAFNAWFRVPPESLTIICDVVRMLHTSSLLIDDIQDNSLLRRGRPVAHSIYGVAQTINTGNYVYFLAAKELNKLRNAASALEVFTAEMLNLHRGQGQELYWRDTLKCPTEDEYLKMVSNKTGGLFRMAVKLMQAESPAGPMAPVCDKLVQLLGLVYQIADDYKNLTAVEYTTSKGFCEDLTEGKFSFPVVHSIQSRPEDRRLYQILAQKTTEVEVKKYAVSYIESTGSLEYTKQVVRVLVQRARDELSRIDQGRERNQEMHALLGKMALE | 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | alcohol biosynthetic process [GO:0046165]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:18391465}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000269|PubMed:18391465}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:18391465}; | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. | null | null | FUNCTION: Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGDP). {ECO:0000269|PubMed:18391465}. | Phomopsis amygdali (Fusicoccum amygdali) |
B2DCZ9 | ARHG2_PIG | MKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTTRERPSSAIYPSDSFRQSLLGSRRGRSPLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEGAEVIYNELMSDFEMGEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELQLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSPRNFVIHRLGDLLITQFSGPSADQMRKTYSEFCSRHTKALKLYKELYARDKRFQQFIRKVTRSAVLKRHGVQECILLVTQRITKYPVLISRILQHTHGIEEERQDLTTALGLVKELLSNVDQDVHELEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLLWKTAAGRFKDVLMLLMTDVLVFLQEKDQKYIFPALDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRVCPSREDFPLIETEDEAYLRRIKMELQQKDRALVELLQEKVGLFAEMTHFQVEEDGGGGMPLPTLPRGLFRSESLESPRGERLLQDAIREVEGLKDLLVGPGVELLLTSREPALPVETDSGGNTSPGVTANGEARTFNGSIELCRADSDSSQKDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLTRANSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLRESEQARALLEREVEEARRQLAALGHTEPLPAEAPWARRPLDPRRRSLPAGDALYLSFTPPQPSRGHDRLDLPVTIRSVHRPFEDRERQELGSPDERLQDSSDPDTGSEEEGSSSRLSPPHSPRDFTRMQDIPEETESRDGEPVASES | null | null | actin filament organization [GO:0007015]; asymmetric neuroblast division [GO:0055059]; cell cycle [GO:0007049]; cell morphogenesis [GO:0000902]; cellular response to muramyl dipeptide [GO:0071225]; innate immune response [GO:0045087]; negative regulation of microtubule depolymerization [GO:0007026]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of metalloendopeptidase activity [GO:1904685]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron migration [GO:2001224]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of wound healing [GO:0090303]; regulation of Rho protein signal transduction [GO:0035023]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; protein-containing complex [GO:0032991]; ruffle membrane [GO:0032587]; spindle [GO:0005819]; vesicle [GO:0031982] | guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; small GTPase binding [GO:0031267] | PF17838;PF00621; | 3.30.60.20;1.20.900.10;2.30.29.30; | null | PTM: Phosphorylation of Ser-860 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosphorylation by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on serine, threonine and tyrosine residues in a RIPK2-dependent manner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cytoplasm {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Golgi apparatus {ECO:0000250|UniProtKB:Q92974}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q92974}. Note=Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization. Colocalized with NOD2 and RIPK2 in vesicles and with the cytoskeleton. {ECO:0000250|UniProtKB:Q92974}. | null | null | null | null | null | FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability. Involved in neuronal progenitor cell division and differentiation. Involved in the migration of precerebellar neurons. {ECO:0000250|UniProtKB:Q60875, ECO:0000250|UniProtKB:Q865S3}. | Sus scrofa (Pig) |
B2DD29 | BRSK1_RAT | MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGVGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRPDPDLSSSPRRGPSKDKKLLATNGTPLP | 2.7.11.1; 2.7.11.26 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | associative learning [GO:0008306]; axonogenesis [GO:0007409]; centrosome duplication [GO:0051298]; DNA damage response [GO:0006974]; establishment of cell polarity [GO:0030010]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule cytoskeleton organization involved in establishment of planar polarity [GO:0090176]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; neuron differentiation [GO:0030182]; neuron projection morphogenesis [GO:0048812]; neurotransmitter secretion [GO:0007269]; protein autophosphorylation [GO:0046777]; regulation of axonogenesis [GO:0050770]; regulation of neuron projection development [GO:0010975]; regulation of synaptic plasticity [GO:0048167]; response to UV [GO:0009411]; synaptic vesicle cycle [GO:0099504] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; distal axon [GO:0150034]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynaptic active zone [GO:0048786]; synaptic vesicle [GO:0008021] | ATP binding [GO:0005524]; gamma-tubulin binding [GO:0043015]; magnesium ion binding [GO:0000287]; molecular function inhibitor activity [GO:0140678]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF21122;PF00069;PF21115; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-189 by PP2C. May be autophosphorylated. {ECO:0000269|PubMed:18324781}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Synapse {ECO:0000269|PubMed:16630837}. Presynaptic active zone {ECO:0000269|PubMed:16630837}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:16630837}. Note=Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage (By similarity). {ECO:0000250}. | 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; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C (By similarity). In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. {ECO:0000250, ECO:0000269|PubMed:16630837}. | Rattus norvegicus (Rat) |
B2DEU7 | MSHMT_PARSX | MNELTRTFFNSSVHDTDPLIAQALDDERARQKNQIELIASENIVSQAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLVKPGDRILSLDLAAGGHLSHGMKGNLSGRWFEAHNYNVDPQNEVINYDEMERIAEEVKPKLLITGGSAYPRELDFARMAQIAKKVGAFFMVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQTAVFPGVQGSLHSNVLAAKAICLGEALRPEFRDYVAQVVKNAKVLAETLTSRGIRIVSGGTDTHIVLLDLSSKGLNGKQAEDALARANITSNKNPIPNDSPRPAEWVGMRLGVSAATTRGMKEDEFRKLGNVVADLLEAESAGNGPEAAEKAKVTVRELTEAFPVYAH | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.1}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=540 uM for alpha-methyl-L-serine {ECO:0000269|Ref.1}; KM=73 uM for tetrahydrofolate {ECO:0000269|Ref.1}; Vmax=8.15 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|Ref.1}; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-8.0. {ECO:0000269|Ref.1}; | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|Ref.1}. | Paracoccus sp |
B2DEU8 | MSHMT_AMISX | MTEQTKAYFNTPVHERDPLVAQALDNERKRQQDQIELIASENIVSRAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKELFGCAYANVQPHSGTQANLAVFFLLLKPGDKVLSLDLAAGGHLSHGMKGNLSGRWFESHNYNVDPETEVIDYDEMERIAEEVRPTLLITGGSAYPRELDFERMGKIAKKVGAWFLVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEAWFKKLQSAVFPGVQGSLHSNVLAAKAVCLGEALRPDFKVYAAQVKANARVLAETLIARGVRIVSGGTDTHIVLVDLSSKGLNGKQAEDLLARANITANKNPIPNDSPRPAEWVGMRLGVSAATTRGMKEDEFRTLGTVIADLIEAEAAGNADGVVEGAKAKVATLTAAFPVYAH | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1500 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407}; KM=90 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407}; Vmax=22.1 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|PubMed:18997407}; Vmax=7.75 umol/min/mg enzyme with D-alanine as substrate {ECO:0000269|PubMed:18997407}; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | null | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|PubMed:18997407}. | Aminobacter sp |
B2DEV1 | MSHMT_ENSSX | MDHATRAHFTMTVGEVDPLLADALASERGRQQNQIELIASENIVSRAVLDALGHEITNKTLEGYPGNRFHGGGQFVDIAEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLLKPGEKVLSLDLAAGGHLSHGMKANLSGRWFDATNYNVNPQNEVIDLDEMERLAEEIRPKLLITGGSAYPRELDFERMSRIAKKVGAYFLVDMAHIAGLVAGGVHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQAAVFPGVQGSLHSNVLAAKAICLGEAMLDDFKVYARQVVANAKVLANTLAERGVRIVSGGTDTHIVLLDLASKGLLGKQAETLLAKANITSNKNPIPGDSPRPPEWVGMRLGSSAATTRGLKEAEFRVLGTVIADLIDAEVAGKADDVVEGAKAKIAELTNTFPVYGQ | 2.1.2.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; D-alanine 2-hydroxymethyltransferase activity [GO:0050413]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine; Xref=Rhea:RHEA:10064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:57416, ChEBI:CHEBI:57453, ChEBI:CHEBI:58275; EC=2.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:18997407}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1880 uM for alpha-methyl-L-serine {ECO:0000269|PubMed:18997407}; KM=228 uM for tetrahydrofolate {ECO:0000269|PubMed:18997407}; Vmax=15.4 umol/min/mg enzyme with alpha-methyl-L-serine as substrate {ECO:0000269|PubMed:18997407}; Vmax=5.48 umol/min/mg enzyme with D-alanine as substrate {ECO:0000269|PubMed:18997407}; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}. | null | null | FUNCTION: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|PubMed:18997407}. | Ensifer sp |
B2DFG5 | DTHAD_DELSH | MQDTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHVKTSKSVPVAAAQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRLPQALQLRRRGCDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRSGVGADDTPLLLAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERERAGCVQAAEALRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFDLVMRNIGVCAAEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQKQDFGYGQVCDLQGRVMPGFVLTGANQEHGILARADGAAEADIATRFPLGTRLRILPNHACATGAQFPAYQALAADGSVQTWERLHGW | 4.3.1.27 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20843822}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20843822}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:20843822}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:20843822}; Note=Divalent metal ions, such as manganese, cobalt and nickel. {ECO:0000269|PubMed:20843822}; | D-serine catabolic process [GO:0036088] | null | ammonia-lyase activity [GO:0016841]; D-serine ammonia-lyase activity [GO:0008721]; pyridoxal phosphate binding [GO:0030170] | PF01168;PF14031; | 3.20.20.10;2.40.37.20; | DSD1 family | null | null | CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxy-D-aspartate = NH4(+) + oxaloacetate; Xref=Rhea:RHEA:27942, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:60898; EC=4.3.1.27; Evidence={ECO:0000269|PubMed:20843822}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 mM for D-THA {ECO:0000269|PubMed:20843822}; KM=6.16 mM for L-THA {ECO:0000269|PubMed:20843822}; KM=0.16 mM for L-EHA {ECO:0000269|PubMed:20843822}; KM=0.15 mM for D-serine {ECO:0000269|PubMed:20843822}; Note=kcat is 10.93 sec(-1) for D-THA. kcat is 3.03 sec(-1) for L-THA. kcat is 8.68 sec(-1) for L-EHA. kcat is 0.89 sec(-1) for D-serine.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:20843822}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20843822}; | FUNCTION: Catalyzes the deamination of D-threo-3-hydroxyaspartate (D-THA). Also exhibits dehydratase activity towards L-threo-3-hydroxyaspartate (L-THA), L-erythro-3-hydroxyaspartate (L-EHA) and D-serine. {ECO:0000269|PubMed:20843822}. | Delftia sp. (strain HT23) |
B2FDA8 | SMC3_CAEEL | MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLPGEINFFPMNRVSAPRQRDLSNNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLDQAARDLRNEGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKLILSRYSIKTRKNQFSYEISDSEEVGAKREPIEHRKLKISTFCLEYRAKLEKVHSNMRLLGALPTDTFSKWQNVKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDDGDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRFRNKVSHIDSVTREQAYDFVEDDTTHG | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; establishment of mitotic sister chromatid cohesion [GO:0034087]; mitotic sister chromatid cohesion [GO:0007064] | chromatin [GO:0000785]; cohesin complex [GO:0008278]; MIS12/MIND type complex [GO:0000444]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC3 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158, ECO:0000269|PubMed:21957461}. Chromosome {ECO:0000269|PubMed:12827206}. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues. {ECO:0000269|PubMed:12827206}. | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair (PubMed:21957461). Involved in the repair of double strand breaks during mitosis and meiosis (PubMed:21957461). Required for chromosome segregation during mitosis (PubMed:12808038). Central component of cohesin complex (PubMed:12808038, PubMed:12827206, PubMed:21957461). The cohesin complex is required for the cohesion of sister chromatids after DNA replication (PubMed:12827206). The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity). Required for the localization of lab-1 to meiotic and mitotic chromosomes (PubMed:22927794). {ECO:0000250|UniProtKB:Q9UQE7, ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21957461, ECO:0000269|PubMed:22927794}. | Caenorhabditis elegans |
B2FHL8 | PL_STRMK | MSLPLRLALLPTLLASASAFAACPAPPPGQPDIRAIGYYTDKAGSVIDPALQQQNKDATAPLDRYAADVARMSDDYLRNGDPAAAQCTLSWLGAWADDGAMLGQMIRVNNDQSFYMRQWMLDAVAMAYLKVHDQANPQQRARIDPWLQKLARANLAYWDNPKRRRNNHYYWGGLGVLATGLATDDDALWQAGHAAFQKGIDDIQDDGSLPLEMARGQRALHYHDYALAPLVMMAELARLRGQDWYASRNHAIDRLARRVIEGSRDPAWFNQHTGAAQLPLQASGWVEFYRLRSPDGGVFDAAHARGPFHSPRLGGDLTLMATHGIVRTPLR | 4.2.2.-; 4.2.2.1; 4.2.2.14; 4.2.2.3 | null | polysaccharide catabolic process [GO:0000272] | cell outer membrane [GO:0009279]; periplasmic space [GO:0042597] | glucuronan lyase activity [GO:0033994]; hyaluronate lyase activity [GO:0030340]; poly(beta-D-mannuronate) lyase activity [GO:0045135] | PF05426; | 1.50.10.100; | Polysaccharide lyase 5 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:24257754}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:24257754}. | CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.; EC=4.2.2.3; Evidence={ECO:0000269|PubMed:24257754}; CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA-COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151, ChEBI:CHEBI:132153; EC=4.2.2.1; Evidence={ECO:0000269|PubMed:24257754}; CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.; EC=4.2.2.14; Evidence={ECO:0000269|PubMed:24257754}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.14 mg/ml for poly-GlcA {ECO:0000269|PubMed:24257754}; KM=0.26 mg/ml for poly-ManA {ECO:0000269|PubMed:24257754}; KM=0.55 mg/ml for hyaluronan {ECO:0000269|PubMed:24257754}; KM=0.17 mM for poly-GlcA (at pH 7) {ECO:0000269|PubMed:24808176}; KM=0.35 mM for poly-ManA (at pH 9) {ECO:0000269|PubMed:24808176}; Note=Vmax for poly-GlcA is about 10-fold greater versus poly-ManA or HA (PubMed:24257754). kcat is 31.9 sec(-1) with poly-GlcA as substrate (at pH 7) (PubMed:24808176). kcat is 3.3 sec(-1) with poly-ManA as substrate (at pH 9) (PubMed:24808176). {ECO:0000269|PubMed:24257754, ECO:0000269|PubMed:24808176}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for enzymatic activity is substrate-dependent, with optimal hyaluronate degradation at pH 5, poly-beta-D-glucuronate degradation at pH 7, and alginate degradation at pH 9. {ECO:0000269|PubMed:24257754}; | null | FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of several anionic polysaccharides via a beta-elimination mechanism. Exhibits broad substrate specificity, catalyzing the degradation of not only alginate and poly-beta-D-mannuronate (poly-ManA), but poly-beta-D-glucuronate (poly-GlcA or poly-GlcUA) and hyaluronate (HA) as well. The oligosaccharide products formed by enzymatic cleavage are comprised mainly of disaccharides, with a lower abundance of trimers and pentamers. Is not active on poly-D-galacturonate, heparin and heparin sulfate. {ECO:0000269|PubMed:24257754}. | Stenotrophomonas maltophilia (strain K279a) |
B2FSW8 | EALGL_STRMK | MRLQPLFVSLALAAPCALLPTASLSAAPAAAARQADTAPVLVTAAQWQQMASEGRRYPWFAKEQARTEATLKKMMKAGIDVPVPRDKGGGRTHEQHKRNYQALLAAGTLYRLTGDRAYVDYARDMLLQYAQLYPTLGPHPEGRGQIPGRVFWQVLNDSVWLVNAIQGYDAIRDALSAEDRNTIESKVFRPMAEFLVSEPKNYDQIHNHATWAVAATGMTGYVLRDQELVEKSLRGSQKDDKFGFLRQIDLLFSPDGYYEEGPYYQRYALAPFLLFANAIERNEPQRKIFARRDGVLLKAVDVLVQSSYGGLFFPINDAILDKGIDTEELVAGIGIAYARTGDDRLLSVAEQQKRLLLSPEGLQVAQALAANKAKPFDYHPMLLRDGPDGDRGGLAILRMNGERGQALVQKDTMQGMGHGHFDKLNWLFYDNGNPVVTDYGAARFLNVEAKRGGIYLAENRSWAKQTVAHNTLVVDEQSHFNGNWKRGEAHAPQVRFFQADADTQIASATMRDAYPGVAFTRTQALLRHPDLGLPVVLDLLQVHGDKAARYDLPLHFNGHIVTTGFEAEHFPSQRPVLGKDNGYQHLWLDARSKPGSEPRSLAWLLDGRFYTYRFGSSAPAQALLVESGANDPEFNLRREPALLQRVDGQKDVTFFSVLEPHGEYNGTAEYVHGADSRIREIVRTRGSDAEVIELRLASGARIALGVADNSATTSEHSVTVDGHVYRWNGSHARLDRSKGDGK | 4.2.2.26 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q21FJ0}; Note=The zinc ion likely plays a structural role. {ECO:0000250|UniProtKB:Q21FJ0}; | polysaccharide catabolic process [GO:0000272] | periplasmic space [GO:0042597] | exo-oligoalginate lyase activity [GO:0052764]; metal ion binding [GO:0046872] | PF05426;PF07940; | 2.70.98.70;1.50.10.100; | Polysaccharide lyase 17 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Cleavage of 4-deoxy-alpha-L-erythro-hex-4-enopyranuronoside oligosaccharides into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides.; EC=4.2.2.26; Evidence={ECO:0000305|PubMed:26913076}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 mM for alginate {ECO:0000269|PubMed:26913076}; KM=0.41 mM for poly-ManA {ECO:0000269|PubMed:26913076}; KM=5.99 mM for poly-GulA {ECO:0000269|PubMed:26913076}; KM=0.57 mM for poly-MG {ECO:0000269|PubMed:26913076}; KM=1.4 mM for poly-GlcA {ECO:0000269|PubMed:26913076}; Note=kcat is 34.8 sec(-1) with alginate as substrate. kcat is 62.2 sec(-1) with poly-ManA as substrate. kcat is 34.6 sec(-1) with poly-GulA as substrate. kcat is 22.2 sec(-1) with poly-MG as substrate. kcat is 0.4 sec(-1) with poly-GlcA as substrate. {ECO:0000269|PubMed:26913076}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26913076}; | null | FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly-alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate. {ECO:0000269|PubMed:26913076}. | Stenotrophomonas maltophilia (strain K279a) |
B2G331 | VKT2B_HETCR | MKGTFLICLILIAGFSFKSTQAGSICLEPKVVGPCTAYFRRFYFDSETGKCTVFIYGGCEGNGNNFETLRACRAICRA | null | null | modulation of sensory perception of pain in another organism [GO:0044465] | extracellular region [GO:0005576]; nematocyst [GO:0042151] | ion channel inhibitor activity [GO:0008200]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729] | PF00014; | 4.10.410.10; | Venom Kunitz-type family, Sea anemone type 2 potassium channel toxin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18579526}. Nematocyst {ECO:0000269|PubMed:18579526}. | null | null | null | null | null | FUNCTION: This protease inhibitor shows two different activities, it inhibits both the capsaicin receptor TRPV1 and serine proteases. It partially (max 50%) and reversibly inhibits capsaicin-induced response of TRPV1 (IC(50)=54 nM), a receptor of the pain pathway (PubMed:18579526, PubMed:24351908). The second activity is a weak inhibition of trypsin and chymotrypsin activity (Ki=1 uM and Ki=5 uM, respectively) (PubMed:18579526). In vivo, it shows antinociceptive and analgesic activities (PubMed:24351908). It significantly prolongs tail-flick latency and reduces capsaicin-induced acute pain (PubMed:18579526, PubMed:24351908). In vivo, unlike other TRPV1 antagonists whose activity is associated with hyperthermia, this protein has the remarkable feature of dropping core body temperature (PubMed:24351908). {ECO:0000269|PubMed:18579526, ECO:0000269|PubMed:22982418, ECO:0000269|PubMed:24351908}. | Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus) |
B2GM84 | ALL21_DERFA | MKFIIFCAIVMAVSVSGFIVDVDTEDKWRNAFDHMLMEEFEEKMDQIEHGLLMLSEQYKELEKTKSKELKEQILRELTIAENYLRGALKFMQQEAKRTDLNMFERYNFETAVSTIEILVKDLAELAKKVKAVKSDD | null | null | null | null | protein homodimerization activity [GO:0042803] | PF11642; | 1.20.58.970; | Mite group 5 allergen family | null | null | null | null | null | null | null | null | Dermatophagoides farinae (American house dust mite) |
B2GUB3 | TTLL3_XENTR | MAHHTAVNPDRLKHAKALVEKAIKQKKIFAIHGPYPVIRSCLRSRGWVEKKFPKSGKAKQKKEKASDEDMEDDDGDGSSNDDDDGENSDEEENGDPDGTCDLMSRLLRNEDPNFFWTTKRDAVDCRFLKKDQMLNHYAKAGSFTTKVGLCLNLRNLHWFDDADPDSFFPRCYRLGAEDEKQSFKEDFWHTAARSILKRVANRRDICSPAATGGAKASHREPGANNGAQLLAKRGSRKRAESVPVQIILTALEACERYLNSLEHNDIDMETEATPAMTDTQWEEFLHGYYQVIHDGATIEHSEYYVDQCSEVLHKLEAVNPQLDIEGGRNIWIVKPGAKSRGRGIICMDRLEEILKLVDCDPMIVKDGKWVVQKYIERPLLIFGTKFDVRQWFLVTDWNPLTIWFYKECYVRFSSQPFSLENLDTSIHLCNNSIQKHYENSQSRHPLVPTDNMWSSRQLQVHLHKLGAPHAWEAVIVPGMKAAIIHAMQSAQDIVEYRKSSFELYGADFMFGENFHPWLIEINASPTMAASTTVTSRLCAEVQEDTLRIVLDRKLDRNCDIGAFELIYKQCAVDIPQYLGINLLVEGSMVKKPRQLQQPNPNGAFNLSIVQSNKRSVSLLNAKTSGSNPGVGSQDSVKVAVPTRTAPAVMGNDFWTSRTHGTIGRAKTTAAGKENKAAEGGQRNSVMVELVRLPSKRALEQSKEGTNPRQRLFPAPKSCTLEKPIRVRQPIRLKNGGFVDLKFTSLDSGQVQLLRNMKTGMTDPNKMPCLFCKGPSSLTGLHAMCSCSRAGKQAAKPTCLKLSKRIIIGKFHGSSAALSARGTAILTSLLP | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; microtubule [GO:0005874]; motile cilium [GO:0031514] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28576883}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}. | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:28576883}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181; Evidence={ECO:0000305|PubMed:28576883}; | null | null | null | null | FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (PubMed:28576883). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (PubMed:28576883). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (PubMed:28576883). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity). {ECO:0000250|UniProtKB:A4Q9E5, ECO:0000269|PubMed:28576883}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B2GUT4 | WNT11_XENTR | MKIYFLLGIFLTFLLHTRICQGIKWLALAKTPLSLALNQSQHCKQLEGLVSSQMQLCRSNLELMQTIIHAAKEVKKTCIKAFTDMRWNCSSIELAPTFHQDLERGTRESAFVYALSAAAISHTIARACTTGDIPGCSCAPIPGESPGPGYRWGGCADNLNYGILMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWRGLQELREIALDLKTKYLSATKVVHRPMGTRKQLVPKDIDIRPVQETEMIYLQSSPDYCLKNEKMGSHGTHERQCNKTSNGSDSCDLMCCGRGYNPYMDKVVERCHCKYHWCCYVTCKKCERTVERYVCK | null | null | canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell migration involved in gastrulation [GO:0042074]; dorsal fin development [GO:0033337]; embryonic viscerocranium morphogenesis [GO:0048703]; heart looping [GO:0001947]; heart morphogenesis [GO:0003007]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA-templated transcription [GO:0045892]; neural crest cell migration [GO:0001755]; neuroendocrine cell differentiation [GO:0061101]; neuromast development [GO:0048884]; non-canonical Wnt signaling pathway [GO:0035567]; pharyngeal system development [GO:0060037]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of GTPase activity [GO:0043547]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein kinase C signaling [GO:0090037]; positive regulation of stress fiber assembly [GO:0051496]; pronephros development [GO:0048793]; protein localization to cell surface [GO:0034394]; protein phosphorylation [GO:0006468]; regulation of gastrulation [GO:0010470]; secondary palate development [GO:0062009]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein kinase activator activity [GO:0030295] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Glycosylation is required for protein secretion. {ECO:0000250|UniProtKB:P49893}.; PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q670P5}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N-terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural crest migration, probably acting as an extracellular signal from surrounding tissue, but is not required for neural crest induction. Acts redundantly with wnt11b during pronephros induction. Regulates cardiac morphogenesis through the activation of JNK, but is not required for cardiac differentiation. Essential for dorsal fin development; required for an epithelial to mesenchymal transformation event prior to migration of cells into the fin, and ultimately for maintenance of fin structure. Mediates dorsal fin development through a non-canonical pathway mediated by Ca(2+) (By similarity). {ECO:0000250|UniProtKB:Q670P5}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B2GUV7 | IF2P_RAT | MGKKQKNKSEDSTKDDTDLGALAAEIEGAGAAKEQEPQKGKGKKKKEKKKQDFDENDILRELEELSLEAQGIGADRDAATVKPTENNEEESASKQDKKKKGQKGKKTSFDENDSEELEDKDSKSKKPARPNSEVLLSGSEDADDPNKLSKKGKKAQKSTKKRDGSEEDEDNSKRSKERSRVNSSGESGGESDEFLQSRKGQKKNQKNKSVPTIDSGNEDDDSSFKIKTVAQKKAEKKERERKKREEEKAKLRKVKEKEELEKGRKEQSKQREPQKRPDEEVLVLRGTPDAGAASEEKGDIAATLEDDNEGDKKKKDKKKKKTEKDDKEKEKKKGPSKSTVKAIQEALAKLREEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEVTLRHLQAQGVEVPSKDSLPKKRPVYEDKKKKKTPQQLESKEALETVEVSAPVEVVDQGVPEKEETPPSVDAEEDEETEDAGLDDWEAMASDEEREKEGNMIHIEVEENPEEEEEEEEDEDEEDSEDEEDEGDSEGSDGDEEDYKLSDEKDLGKAGDTKPNKDASSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHGKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKDDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII | 3.6.5.3 | COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250|UniProtKB:G0S8G9}; Note=Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction. {ECO:0000250|UniProtKB:G0S8G9}; | regulation of translational initiation [GO:0006446]; ribosome assembly [GO:0042255]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; synapse [GO:0045202] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; translation initiation factor activity [GO:0003743]; tRNA binding [GO:0000049] | PF00009;PF14578;PF11987; | 3.40.50.300;2.40.30.10;3.40.50.10050; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, IF-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}. | 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; EC=3.6.5.3; Evidence={ECO:0000250|UniProtKB:O60841}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:O60841}; | null | null | null | null | FUNCTION: Plays a role in translation initiation. Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex. Is released after formation of the 80S initiation complex. Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes. In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit. {ECO:0000250|UniProtKB:O60841}. | Rattus norvegicus (Rat) |
B2GUY0 | MA1B1_RAT | MYPPPPAPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLQVSDQWKALSGSRAEVEKMKLEVLPVLPAPQKESAEPEGFADILSQKRQRHLRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATEPPSKRAEASIKPLFLASRIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKEARKWVSENLDFQKNVDVNLFESTIRILGGLLSAYHLSGDSLFLSKAEDFGNRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVRAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTKDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLGLDTCVFNTEAHPLPIWSPA | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; | carbohydrate metabolic process [GO:0005975]; ERAD pathway [GO:0036503]; mannoprotein catabolic process [GO:0006058]; protein glycosylation [GO:0006486] | cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; endosome [GO:0005768]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
B2GUY1 | PLK4_RAT | MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSESEARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSTKSKDLGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANNRGRGRVIEDAEERPHSRYLRRAHSSDRSNPSNQSRAKTYSIERCHSVEMLSKPRRSSLDETKHSSNHHCLGKTPFPFADQTPQMEIVQQWFGNLQMNGETSEHNTISPNRDFQDYPDVQDTLRNTWTDTRASKNSDNSANVHPAKQLSTMKYMTAHHHKPEIMQQELAIHPHSEQNKSRSMESTLGYRKPTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELLKECTSEGHVKEVLQISSDGTTITVYYPNDGRGFPLADRPPLPTDNISRYSFDSLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTEDVIHIIEKTGLSYTLKNENDFTSLKEEVKIYMDHANEGHRTCLALESVISEEEKRSRGSSFFPIIVGRKPGTTSSPKALSPPPVDPGYSKGEQASSSRLSANSAAFPTQTPVLSPSAVTVEGPGQTAATTGTSISSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPSFQ | 2.7.11.21 | null | centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast giant cell differentiation [GO:0060707] | centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]; spindle pole [GO:0000922]; XY body [GO:0001741] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000250|UniProtKB:Q64702}. | 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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444}; 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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000250|UniProtKB:Q64702}. | Rattus norvegicus (Rat) |
B2GUZ1 | UBP4_RAT | MAEGRGTHERPDVETQKTELGALMGTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSSKPSASPYSSMSASLIANGDSTNSSGMHNSGVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLEPKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPIQYRVTVPLMGAISDLCEALSKLSGIAAENMVVTDVYNHRFHKIFQMDEGLSHITPRDDIFVYEICTTPMDGSEYITLPVYFREKKSRPSSTSSGAVLYGQPLLVSVPKHRLTLESLYQAVCERISRYIKQPLPEEFLSSPLEPGACNGSRGSYEGDEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKAKGPPRHKRLFTFSLVNSCGTADINSLATDGKLLKLNSRSTLAIDWDSETRSLYFDEQESEACEKHTSMSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQRRDDECPSTSSPVSFPGSDGGAKLSSSQQDLGEEEAYTMDTN | 3.4.19.12 | null | negative regulation of protein ubiquitination [GO:0031397]; positive regulation of TORC1 signaling [GO:1904263]; protein deubiquitination [GO:0016579]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; regulation of protein stability [GO:0031647]; spliceosomal tri-snRNP complex assembly [GO:0000244] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | adenosine receptor binding [GO:0031685]; cysteine-type deubiquitinase activity [GO:0004843]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06337;PF14836;PF00443; | 3.90.70.10;3.30.2230.10; | Peptidase C19 family, USP4 subfamily | PTM: Phosphorylated at Ser-445 by PKB/AKT1 in response to EGF stimulus, promoting its ability deubiquitinate RHEB. {ECO:0000250|UniProtKB:Q13107}.; PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Nucleus {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type. {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. | 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:Q13107}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. Deubiquitinates RHEB in response to EGF signaling, promoting mTORC1 signaling. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000250|UniProtKB:Q13107}. | Rattus norvegicus (Rat) |
B2GV06 | SCOT1_RAT | MAALKLLSSGLRLCASARNSRGALHKGCACYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFRGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGEGKAKSGKPGEDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIRKSTGCDFAVSPNLMPMQQIST | 2.8.3.5 | null | adipose tissue development [GO:0060612]; cellular ketone body metabolic process [GO:0046950]; heart development [GO:0007507]; ketone body catabolic process [GO:0046952]; ketone catabolic process [GO:0042182]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; response to activity [GO:0014823]; response to ethanol [GO:0045471]; response to hormone [GO:0009725]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; response to xenobiotic stimulus [GO:0009410] | mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; succinyl-CoA:3-oxo-acid CoA-transferase activity [GO:0008260] | PF01144; | 3.40.1080.10; | 3-oxoacid CoA-transferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19343716}. | CATALYTIC ACTIVITY: Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate; Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973, ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5; Evidence={ECO:0000250|UniProtKB:P55809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565; Evidence={ECO:0000250|UniProtKB:P55809}; CATALYTIC ACTIVITY: Reaction=acetoacetate + succinyl-CoA = acetoacetyl-CoA + succinate; Xref=Rhea:RHEA:25480, ChEBI:CHEBI:13705, ChEBI:CHEBI:30031, ChEBI:CHEBI:57286, ChEBI:CHEBI:57292; EC=2.8.3.5; Evidence={ECO:0000250|UniProtKB:P55809}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481; Evidence={ECO:0000250|UniProtKB:P55809}; | null | PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P55809}. | null | null | FUNCTION: Key enzyme for ketone body catabolism. Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl-CoA thiolase into two acetyl-CoA molecules which enter the citric acid cycle for energy production (By similarity). Forms a dimeric enzyme where both of the subunits are able to form enzyme-CoA thiolester intermediates, but only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl-CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). {ECO:0000250|UniProtKB:P55809, ECO:0000250|UniProtKB:Q29551}. | Rattus norvegicus (Rat) |
B2GV17 | CBPC5_RAT | MELRCGGLLFSSRFDSGNLAHVEKVETVPSDGEGVGGAATAPTSGSASSPDYEFNVWTRPDCAETEYENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPSRPRWERIRERPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLSQLDQRFPENYSAHSSPLDSIYYHRELLCYSLDGLRVDLLTITSCHGLRDDREPRLEQLFPDVGTPRPFRFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNSKNPSNQQPSSLHLPPEVPLSDLEKANNLHNELHLGQSPDGENHDRWTETEPTEEKTDPVWIMPQPIPELEEPAPDAIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPTFPSRYTVELFEQVGRALAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRNSRGLTSTANVGLNKKRGSRTPPKSNNGLPVSCSENALSRARSFSTGTSTGGSSSQQNSPQMKNSPSFPFHGSRPAGLPGLGSSTQKVSHRVLGPVREPRCPDRRRRQQQQQQQQQQQQQQQQQPLNQRSTTSSLAPSPTLASASPTSSRNMGSCLLPNSLSLSGSSCPFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQTCQRRVSARRGPGFPRLGPGWAGAHRRLAEG | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed. Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis. {ECO:0000250|UniProtKB:Q09M02, ECO:0000250|UniProtKB:Q8NDL9}. | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation. {ECO:0000250|UniProtKB:Q09M02}. | Rattus norvegicus (Rat) |
B2GV24 | UFL1_RAT | MADAWEEIRRLAADFQRAQFAESTQRLSERNCIEIVNKLISQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLTHIENRVGDIIKSEKHVQMVLGQLVDENYLDRLSEEVNDKLQESGQVTVSELCKTYDLPGDFLTQALTQRLGRIINGHLDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLVSKYGFQEQLLYSVLEELVSTGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVNYIKKRYKNTPLLFLKATCVGQGLVDQVEASVEEAISSGTWVDVSPLLPSSLSVEDAAMLLQQVMRPFGKHASATVFSDTVVVSEKFINDCTKLFSERMHQKAEKEMKNNPVHLITEEDLKQISILESVNTNKKDKKDERRKKATEGSGSVRGGGGGNAREYKIKKVKKKGRKDEDSDDESQSSHAGKKKPDITFMFQDEIEGCLRKHIPDAPEEFISELAEHLIKPLNKMYLEVVRSVFMSSTSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKYFADDTQTALTKHLLKTVCTDITNLMFNFLASDLMMAVEDPATITSDMRKKILSKLTEETKVALTKLHNSLNEKSIEDFLSCLDSATEACDIMVKKGDKKRERQILFQHRQALADQLKVTEDPALILHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLHNKIPEDQHTLLVKYQGLVVKQLVSQNKKSGQGEDPSSDDLDKEQHDVTNTTRKELQELSLSIKDLVLKPRKSSVTEE | 2.3.2.- | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of apoptotic process [GO:0043066]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of autophagy [GO:0010508]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of glial cell proliferation [GO:0060252]; protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of gene expression [GO:0010468]; regulation of inflammatory response [GO:0050727]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of protein localization [GO:0032880]; response to endoplasmic reticulum stress [GO:0034976]; response to L-glutamate [GO:1902065]; reticulophagy [GO:0061709] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; site of double-strand break [GO:0035861] | protein kinase binding [GO:0019901]; UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568] | PF09743; | null | UFL1 family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome. {ECO:0000250|UniProtKB:O94874}.; PTM: Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and promoting ATM activation in a positive feedback loop. {ECO:0000250|UniProtKB:O94874}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20531390}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O94874}. Nucleus {ECO:0000250|UniProtKB:O94874}. Chromosome {ECO:0000250|UniProtKB:O94874}. Note=Recruited to double-strand breaks by the MRE11-RAD50-NBN (MRN) complex following DNA damage. {ECO:0000250|UniProtKB:O94874}. | null | null | null | null | null | FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets. Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha. Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (By similarity). Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (By similarity). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (By similarity). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition. Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 and ufmylation of MRE11. Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (By similarity). Required for hematopoietic stem cell function and hematopoiesis. Required for cardiac homeostasis (By similarity). {ECO:0000250|UniProtKB:A1A4I9, ECO:0000250|UniProtKB:O94874, ECO:0000250|UniProtKB:Q8CCJ3}. | Rattus norvegicus (Rat) |
B2GV46 | FFAR3_RAT | MDTSFFPGNHWLFFSVDLLVFLVGLPLNVMALVVFVNKLRRRPVAVDLLLLNLTISDLLLLLFLPFRIVEAACGMKWILPFIFCPLSGFLFFTTIYLTSLFLMTVSIERFLSVAYPLWYKTRPRLAQAGLVSGICWFLASAHCSVIYVTEYWGNATYSQGTNGTCYLEFREDQLAILLPVRLEMAVVLFMVPLCITSYCYSRLVWILSQGASRRRRKRVMGLLVATLLIFFVCFGPYNMSHVVGYVRGESPTWRSYVLLLSTLNSCIDPLVFYFSSSKFQADFHQLLSRLIRACVPWTQEVSLELKVKNGEEPSKECPS | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to fatty acid [GO:0071398]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; inflammatory response [GO:0006954]; mucosal immune response [GO:0002385]; negative regulation of blood pressure [GO:0045776]; negative regulation of insulin secretion [GO:0046676]; neuronal action potential [GO:0019228]; positive regulation of acute inflammatory response to non-antigenic stimulus [GO:0002879]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production involved in immune response [GO:0002720]; positive regulation of neuronal action potential [GO:1904457]; regulation of heart rate by chemical signal [GO:0003062]; regulation of hormone biosynthetic process [GO:0046885]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of norepinephrine secretion [GO:0014061]; regulation of peptide hormone secretion [GO:0090276] | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases (PubMed:24305827). Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis (PubMed:24412651). May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells. {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:24305827, ECO:0000269|PubMed:24412651}. | Rattus norvegicus (Rat) |
B2GV50 | RFX2_RAT | MQNSEGGADSPATVALRPAAQPVPASPQRVLVQAAGSTPKGTPMQTLTLPRVQPVPPQVQHVYPAQVQYVEGGDAVYANGAIRAAYTYNPDPQLYAPSSAASYFETPGGAQVTVAASSPPAVPSHGMVGITMDVSGTPIVSGAGTYLIHGGMDSTRHSLAHTARSSPATLQWLLDNYETAEGVSLPRSSLYNHYLRHCQEHKLEPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRLQEDTQYMAMRQQPTHQKPRYRPAQKSDSLGDGSAHSNMHSTPEQAMAAQGQHHQQYIDVSHVFPEFPAPDLGSTLLQESVTLHDVKALQLVYRRHCEATLDVVMNLQFQYIEKLWLSFWNCKATSSDGRASLPASDEEPEVTLLPKDKLISLCKCEPILQWMRSCDHILYQALVETLIPDVLRPVPSSLTQAIRNFAKSLEGWLINAMSGFPQQVIQTKVGVVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLSDLNRVDFANVQEQASWVCQCEESLVQRLEHDFKVTLQQQSSLDQWASWLDNVVTQVLKQHAGSPSFPKAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAQATGETPIAVMGEFNDLASLSLTLLDKEDIGDGHSSEADVDGRSLGEPLVKRERSDPSHPLQGI | null | null | acrosome assembly [GO:0001675]; cellular response to leukemia inhibitory factor [GO:1990830]; cilium assembly [GO:0060271]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatid development [GO:0007286] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF04589;PF02257; | 1.10.10.10; | RFX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:16676351}. Cytoplasm {ECO:0000269|PubMed:16676351}. Note=Mainly expressed in the nucleus and at lower level in cytoplasm. {ECO:0000269|PubMed:16676351}. | null | null | null | null | null | FUNCTION: Transcription factor that acts as a key regulator of spermatogenesis (By similarity). Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (By similarity). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters (PubMed:14743396, PubMed:15526285, PubMed:16676351, PubMed:18247329). Probably activates transcription of the testis-specific histone gene H1-6 (PubMed:14743396, PubMed:15526285, PubMed:16676351, PubMed:18247329). {ECO:0000250|UniProtKB:P48379, ECO:0000269|PubMed:14743396, ECO:0000269|PubMed:15526285, ECO:0000269|PubMed:16676351, ECO:0000269|PubMed:18247329}. | Rattus norvegicus (Rat) |
B2GV72 | CRB3_RAT | MSSCSRVALVTGANKGIGFAITRDLCRKFSGDVVLTARDEARGRAAVKQLQAEGLSPRFHQLDIDNPQSIRALRDFLRKEYGGLNVLVNNAGIAFRMDDPTPFDVQAEVTLKTNFFATRNVCTELLPIMKPHGRVVNVSSLQGLKALENCSEDLQERFRCDTLTEGDLVDLMKKFVEDTKNEVHEREGWPDSAYGVSKLGVTVLTRILARQLDEKRKADRILLNACCPGWVKTDMARDQGSRTVEEGAETPVYLALLPPDATEPHGQLVRDKVVQTW | 1.1.1.184; 1.6.5.10 | null | cognition [GO:0050890]; phylloquinone catabolic process [GO:0042376] | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | 3-keto sterol reductase activity [GO:0000253]; carbonyl reductase (NADPH) activity [GO:0004090]; NADPH binding [GO:0070402]; NADPH dehydrogenase (quinone) activity [GO:0008753] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75828}. | CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:18983987}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259; Evidence={ECO:0000250|UniProtKB:O75828}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.10; Evidence={ECO:0000250|UniProtKB:O75828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165; Evidence={ECO:0000250|UniProtKB:O75828}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 nM for 4-benzoylpyridine {ECO:0000269|PubMed:18983987}; Note=kcat is 14 min(-1) with 4-benzoylpyridine as substrate (PubMed:18983987). kcat is 0.030 min(-1) with menadione as substrate (PubMed:18983987). {ECO:0000269|PubMed:18983987}; | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity (PubMed:18983987). Acts on several orthoquinones, as well as on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones. Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified (By similarity). {ECO:0000250|UniProtKB:O75828, ECO:0000269|PubMed:18983987}. | Rattus norvegicus (Rat) |
B2GV87 | PTPRE_RAT | MEPFCPLLLASFSLSLATAGQGNDTTPTESNWTSTTAGPPDPGTSQPLLTWLLLPLLLLLFLLAAYFFRFRKQRKAVVNSNDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGDTELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK | 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of insulin receptor signaling pathway [GO:0046627]; regulation of mast cell activation [GO:0033003]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 4 subfamily | PTM: A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3. {ECO:0000250}.; PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}. Note=Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin can induce translocation to the membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {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: Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity). Acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver. {ECO:0000250}.; FUNCTION: Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity). {ECO:0000250}.; FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+). {ECO:0000250}. | Rattus norvegicus (Rat) |
B2HIL7 | MSL7_MYCMM | MTTSGESADQQNDKLFRYLKKVAVELDEARARLREYEQRATEPVAVVGIGCRFPGGADGPEGLWDLVSQGRDAVTEFPNDRGWDTEGLFDPDPDAEGKTYTRWGAFVENATNFDAGFFGIPPSEVLAMDPQQRLMLEVSWEALEHAGIDPMSLRGSSTGVFTGIFAPSYGGKDVGALQGYGLTGSPVSVASGRVAYVLGLEGPALSVDTACSSSLVAIHWAMASLRSGECDMALAGGVTVMGLPSIFVGFSRQRGLAADGRCKAFAAAADGTGWGEGAGVLVLERLSDAQRNGHNVLAVVRGSAINQDGASNGLTAPNGLAQQRVIQAALANCGLTSADVDVVEAHGTATTLGDPIEAEALLATYGQGRPTDQPLWVGSIKSNMGHTQAAAGVAGVIKMVQAMRHGLMPASLHVDEPSKRVDWESGAVSVLAEARDWPDAGRPRRAGVSSFGISGTNAHVILEEAPAPEAVPDSESNKGEPSLPVVPWVISARSAEALTAQAGRLLAHVQADPQSNPVDIGFSLAGRSAFEHRAVVVGADRQQLLTGLATLADGAPGAGVVTGQAGSVGKTAVVFPGQGSQRIGMARELHDQLPVFAEAFDAVADELDRHLRIPLREVMWGSDAALLDSTEFAQPALFAVEVALFAALQRWGLQPDFVMGHSVGELSAAYVAGVLTLADAAMLVVARGRLMQALPAGGAMVAVAAAEDEVLPSLTDGVGIAAINAPKSVVISGAEAAVTAISDQFAQQGRRVHRLAVSHAFHSPLMEPMLEEFARIAAQVEAREPQIALVSNVTGELASADGGFGSAQYWVEHVRRAVRFADSARQLHTLGVTHFVEVGPGSGLTGSIEQSLAPAEAVVVSMLGKDRPEVASVLTAFGQLFSTGMSVDWPAVFAGSGATRVDLPTYAFQRRRFWEVPGADGPADATGLGLGGAEHALLGAVVERPDSGGVVLTGRLALADQPWLADHVIGGVVLFPGAGFVELAIRAGDEVGCAVVEELVLAAPLVLHPGMGVQVQVIVGAADDSGNRALSVYSRGDQSEDWLLNAEGMLGVEAASSGADLSVWPPEGAESVDISDGYAQLADRGYAYGPGFQGLVGVWRRDSELFAEVVAPSGVAVDKMGMHPVVLDAVLHALGLTAEQNPDSDETKLPFCWRGVSLHAGGAGRVRARLTMSGPDSISVEIADAAGLPVLTVGALVTRAMSAAQLRAAVAAAGGGAPDQGPLDVIWSPIPLSGSGTNGSAQPAVVSWADFCAGGDGGAAGDAGVVVWEPNPAGEDVVGSVYAATHAALEVLQSWFDGDRAGTLVVLTHGAVAMPGENVSDLAGAAVWGIVRSAQAENPGRIVLVDADAAVEAAELVAVGEPQLVVRSGAAHAARLAPAAPLLAVPADESAWRLAAGGGGTLEDLVIEPCPEVQAPLAAGQVRVAVRAVGVNFRDVVAALGMYPGEAPPLGAEGAGVVLEVGPQVSGVAVGDSVMGFLGGAGPLSVVDQQLITRMPQGWSFAQAAAVPVVFLTALFGLQDLAKIQPGESVLIHAGTGGVGMAAVQLARHWGVEIFVTASRGKWDTLRAMGFDDDHIGDSRTLDFEEKFLAVTDGRGVDVVLDSLAGDFVDASLRLLVRGGRFLEMGKTDIRDADKIAANYPGVWYRAFDLSEAGPVRMQEMLAEVRELFDTAVLHRLPVTTWDVRCAPAAFRFMSQARHIGKVVLTMPSALADGLADATVLITGATGAVGAVLARHMLDAYGVRHLVLASRRGDRAEGAAELAAELSEAGANVQVVACDVADRDAVEAMLARLSGEYPPVRGVIHAAGVLDDAVISSLTPERIDTVLRAKVDAAWNLHEATLDLDLSMFVLCSSIAATVGSPGQGNYSAANSFLDGLAAHRQAAGLAGISVAWGLWEQSGGMAAHLSSRDLARMSRSGLAPMNPEQAVGLLDAVLAINHPLMVATLLDRPALEARAQAGGLPPLFAGVVRRPRRRQIEDTGDAAQSKSALAERLNGLSAGERQDALVGLVCLQAAAVLGRPSPEDIDPEAGFQDLGFDSLTAVELRNRLKSATGLTLPPTVIFDHPTPTAIAEYVGRQIPDSQATQAEEEKLPESDGEMVSVTA | 2.3.1.41 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000250}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000250}; | Actinobacterium-type cell wall biogenesis [GO:0071766]; DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610] | plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.30.70.3290;3.40.47.10;6.10.40.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family | null | null | CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000255|PROSITE-ProRule:PRU10022}; | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). {ECO:0000269|PubMed:19799378}. | Mycobacterium marinum (strain ATCC BAA-535 / M) |
B2HN69 | CAR_MYCMM | MSPITREERLERRIQDLYANDPQFAAAKPATAITAAIERPGLPLPQIIETVMTGYADRPALAQRSVEFVTDAGTGHTTLRLLPHFETISYGELWDRISALADVLSTEQTVKPGDRVCLLGFNSVDYATIDMTLARLGAVAVPLQTSAAITQLQPIVAETQPTMIAASVDALADATELALSGQTATRVLVFDHHRQVDAHRAAVESARERLAGSAVVETLAEAIARGDVPRGASAGSAPGTDVSDDSLALLIYTSGSTGAPKGAMYPRRNVATFWRKRTWFEGGYEPSITLNFMPMSHVMGRQILYGTLCNGGTAYFVAKSDLSTLFEDLALVRPTELTFVPRVWDMVFDEFQSEVDRRLVDGADRVALEAQVKAEIRNDVLGGRYTSALTGSAPISDEMKAWVEELLDMHLVEGYGSTEAGMILIDGAIRRPAVLDYKLVDVPDLGYFLTDRPHPRGELLVKTDSLFPGYYQRAEVTADVFDADGFYRTGDIMAEVGPEQFVYLDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYIYGNSARAYLLAVIVPTQEALDAVPVEELKARLGDSLQEVAKAAGLQSYEIPRDFIIETTPWTLENGLLTGIRKLARPQLKKHYGELLEQIYTDLAHGQADELRSLRQSGADAPVLVTVCRAAAALLGGSASDVQPDAHFTDLGGDSLSALSFTNLLHEIFDIEVPVGVIVSPANDLQALADYVEAARKPGSSRPTFASVHGASNGQVTEVHAGDLSLDKFIDAATLAEAPRLPAANTQVRTVLLTGATGFLGRYLALEWLERMDLVDGKLICLVRAKSDTEARARLDKTFDSGDPELLAHYRALAGDHLEVLAGDKGEADLGLDRQTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNALGTAELLRLALTSKIKPYSYTSTIGVADQIPPSAFTEDADIRVISATRAVDDSYANGYSNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTTWAGQLNVPDMFTRMILSLAATGIAPGSFYELAADGARQRAHYDGLPVEFIAEAISTLGAQSQDGFHTYHVMNPYDDGIGLDEFVDWLNESGCPIQRIADYGDWLQRFETALRALPDRQRHSSLLPLLHNYRQPERPVRGSIAPTDRFRAAVQEAKIGPDKDIPHVGAPIIVKYVSDLRLLGLL | 1.2.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000305|PubMed:23248280}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000305|PubMed:23248280}; | organonitrogen compound biosynthetic process [GO:1901566] | membrane [GO:0016020] | ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor [GO:0016620]; phosphopantetheine binding [GO:0031177] | PF00501;PF07993;PF00550; | 1.10.1200.10;3.40.50.12780;3.40.50.720; | ATP-dependent AMP-binding enzyme family, Carboxylic acid reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde + diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:23248280}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=362 uM for benzoate {ECO:0000269|PubMed:23248280}; KM=48 uM for NADPH {ECO:0000269|PubMed:23248280}; KM=115 uM for ATP {ECO:0000269|PubMed:23248280}; Vmax=2.32 umol/min/mg enzyme with benzoate as substrate {ECO:0000269|PubMed:23248280}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23248280}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Displays in vitro half-lives of 73, 70, and 48 hours at 26, 30, and 37 degrees Celsius, respectively, indicating it is a relatively stable enzyme. {ECO:0000269|PubMed:23248280}; | FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (PubMed:23248280). Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor (PubMed:23248280). {ECO:0000269|PubMed:23248280}. | Mycobacterium marinum (strain ATCC BAA-535 / M) |
B2IZD3 | BDLP_NOSP7 | MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWAMGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGPIGFALLGLGVGFLQADQARRELVKTAKKELVKHLPQVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS | 3.6.5.5 | null | mitochondrial fusion [GO:0008053] | plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289] | PF21808;PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:17122778}; Peripheral membrane protein {ECO:0000305|PubMed:17122778}. Note=Probably inserts into the outer leaflet of the membrane only (Probable). Forms foci localized in the cell periphery, and occasionally in the cell interior. {ECO:0000305|PubMed:20064379}. | 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; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:17122778}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=68.6 uM for GTP {ECO:0000269|PubMed:17122778}; Note=kcat is 0.53 min(-1). {ECO:0000269|PubMed:17122778}; | null | null | null | FUNCTION: Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer; this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding. {ECO:0000269|PubMed:17122778}. | Nostoc punctiforme (strain ATCC 29133 / PCC 73102) |
B2J528 | PAL_NOSP7 | MNITSLQQNITRSWQIPFTNSSDSIVTVGDRNLTIDEVVNVARHGTQVRLTDNADVIRGVQASCDYINNAVETAQPIYGVTSGFGGMADVVISREQAAELQTNLIWFLKSGAGNKLSLADVRAAMLLRANSHLYGASGIRLELIQRIETFLNAGVTPHVYEFGSIGASGDLVPLSYITGALIGLDPSFTVDFDGKEMDAVTALSRLGLPKLQLQPKEGLAMMNGTSVMTGIAANCVYDAKVLLALTMGVHALAIQGLYGTNQSFHPFIHQCKPHPGQLWTADQMFSLLKDSSLVREELDGKHEYRGKDLIQDRYSLRCLAQFIGPIVDGVSEITKQIEVEMNSVTDNPLIDVENQVSYHGGNFLGQYVGVTMDRLRYYIGLLAKHIDVQIALLVSPEFSNGLPPSLVGNSDRKVNMGLKGLQISGNSIMPLLSFYGNSLADRFPTHAEQFNQNINSQGYISANLTRRSVDIFQNYMAIALMFGVQAVDLRTYKMKGHYDARTCLSPNTVQLYTAVCEVVGKPLTSVRPYIWNDNEQCLDEHIARISADIAGGGLIVQAVEHIFSSLKST | 4.3.1.24 | null | aromatic amino acid metabolic process [GO:0009072]; cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559]; phenylpropanoid biosynthetic process [GO:0009699]; protein homotetramerization [GO:0051289] | cytoplasm [GO:0005737] | phenylalanine ammonia-lyase activity [GO:0045548] | PF00221; | 1.20.200.10;1.10.275.10; | PAL/histidase family | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000269|PubMed:17240984}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.24; Evidence={ECO:0000269|PubMed:17240984}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.045 mM for phenylalanine {ECO:0000269|PubMed:17240984}; Note=kcat is 1.96 sec(-1) for phenylalanine. {ECO:0000269|PubMed:17240984}; | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.7-8.5. {ECO:0000269|PubMed:17240984}; | null | FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway. {ECO:0000269|PubMed:17240984}. | Nostoc punctiforme (strain ATCC 29133 / PCC 73102) |
B2KF05 | BRPF3_MOUSE | MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPAKSKKPSSKGKRKESCSKHASGTSFHLPQPSFRVVDTGSQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDIAWLDMVNEKRRADGHSSVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCVLCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPARWKLTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTTFTVRKTAYCEAHSPSVAVARRKGDSPRSLSEVGDEDGPKEGGGEEEQEEAEEEGQEGQGGVGSPLKGVSKKGKMSLKQKIKKEPEEAGREAPSITLPMVTVPQIPSYRLNKICSGLSFQRKTQFMQRLHNYWLLKRQARNGVPLIRRLHSHLQSQRNAEQREQDEKTSAVKEELKYWQKLRHDLERARLLIELIRKREKLKREQVKVQQAAMELELMPFTVLLRTTLDLLQEKDSAHIFAEPVSLSEVPDYLEFISKPMDFSTMRRKLESHLYHTLEEFEEDFNLIVTNCMKYNAKDTIFHRAAVRLRDLGGAILRHARRQAENIGYDPERGTHLPESPRLEDFYRFSWEDVDNILIPENRAHLSPEAQLKELLEKLDLVSTMRSSGARTRRVRMLRREINALRQKLAQPPPPQLLSLNKTVPNGELPAGSRGDTAVLEQAQQEEPEEEGDRDDSKLPAPPTLEPTGPAPSLSEQESPPDPPTLKPISDSKPSSRFLKSRKVEDEELLEKSALQLGSEPLQCLLSDNGIDRLSLTNPDSHPDTPLGTVGRRTSVLFKKAKNGVKLQRGPDGTLENGEDHGPEDDPASPASTEDEHYSRKRPRSRSCSDSEGERSPQQEEETGVTNGFGKHTESGSDSECSLGLSGGLAFEAGSGLTPPKRSRGKPALSRVPFLEGVNGDSDHSGSGRSLLMPFEDHGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGERLFLVLFFDNKRTWQWLPRDKVLPLGVEDTVDKLKMLEGRKTSIRKSVQVAYDRAMIHLSRVRGSHAFVTSSYL | null | null | positive regulation of DNA replication [GO:0045740]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357] | histone acetyltransferase complex [GO:0000123]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleus [GO:0005634] | histone H3K14 acetyltransferase activity [GO:0036408]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K5 acetyltransferase activity [GO:0043995]; histone H4K8 acetyltransferase activity [GO:0043996]; metal ion binding [GO:0046872] | PF00439;PF10513;PF13831;PF00855;PF13832; | 2.30.30.140;1.20.920.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULD4}. | null | null | null | null | null | FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity. Plays a role in DNA replication initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby facilitating the activation of replication origins. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000250|UniProtKB:Q9ULD4}. | Mus musculus (Mouse) |
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