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STAM1_CAEEL
ID   STAM1_CAEEL             Reviewed;         457 AA.
AC   O01498; Q8I7I2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Signal transducing adapter molecule 1 {ECO:0000250|UniProtKB:Q92783};
DE            Short=STAM-1 {ECO:0000250|UniProtKB:Q92783};
DE   AltName: Full=Prion-like-(Q/N-rich) domain-bearing protein 19;
GN   Name=stam-1; Synonyms=pqn-19; ORFNames=C34G6.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16824915; DOI=10.1016/j.cub.2006.05.020;
RA   Govindan J.A., Cheng H., Harris J.E., Greenstein D.;
RT   "Galphao/i and Galphas signaling function in parallel with the MSP/Eph
RT   receptor to control meiotic diapause in C. elegans.";
RL   Curr. Biol. 16:1257-1268(2006).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH LOV-1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17581863; DOI=10.1091/mbc.e07-03-0239;
RA   Hu J., Wittekind S.G., Barr M.M.;
RT   "STAM and Hrs down-regulate ciliary TRP receptors.";
RL   Mol. Biol. Cell 18:3277-3289(2007).
CC   -!- FUNCTION: Binds, sorts and targets the polycystin complex (lov-1 and
CC       pkd-2) for lysosomal degradation, acting on early endosomes located at
CC       the ciliary base. Functions in the germline together with the ephrin
CC       receptor (vab-1) signaling pathway to negatively regulate MAPK
CC       activation. May have a role as a positive regulator of meiotic
CC       maturation in oocytes, acting independently of vab-1.
CC       {ECO:0000269|PubMed:16824915, ECO:0000269|PubMed:17581863}.
CC   -!- SUBUNIT: Isoform a, but not isoform b, interacts (via C-terminus) with
CC       lov-1 (via C-terminus). {ECO:0000269|PubMed:17581863}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000269|PubMed:17581863}. Endosome {ECO:0000269|PubMed:17581863}.
CC       Note=Located to early endosomes at the ciliary base but not cilium
CC       proper of male-specific sensory neurons. {ECO:0000269|PubMed:17581863}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000269|PubMed:9851916};
CC         IsoId=O01498-1; Sequence=Displayed;
CC       Name=b {ECO:0000269|PubMed:9851916};
CC         IsoId=O01498-2; Sequence=VSP_052896, VSP_052897, VSP_052898;
CC   -!- TISSUE SPECIFICITY: Widely expressed, including the pharyngeal
CC       intestinal valve, several head neurons, and phasmids in both males and
CC       hermaphrodites throughout development. In males, also expressed in the
CC       gonad and sensory neurons in the tail. Expressed in the male-specific
CC       ciliate CEM, ray B-type and hook HOB sensory neurons.
CC       {ECO:0000269|PubMed:17581863}.
CC   -!- SIMILARITY: Belongs to the STAM family. {ECO:0000255}.
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DR   EMBL; FO080778; CCD66687.1; -; Genomic_DNA.
DR   EMBL; FO080778; CCD66688.1; -; Genomic_DNA.
DR   PIR; G87789; G87789.
DR   RefSeq; NP_491710.2; NM_059309.6. [O01498-1]
DR   RefSeq; NP_871813.1; NM_182013.6. [O01498-2]
DR   AlphaFoldDB; O01498; -.
DR   SMR; O01498; -.
DR   BioGRID; 37718; 28.
DR   DIP; DIP-26020N; -.
DR   IntAct; O01498; 14.
DR   STRING; 6239.C34G6.7a; -.
DR   EPD; O01498; -.
DR   PaxDb; O01498; -.
DR   PeptideAtlas; O01498; -.
DR   PRIDE; O01498; -.
DR   EnsemblMetazoa; C34G6.7a.1; C34G6.7a.1; WBGene00004109. [O01498-1]
DR   EnsemblMetazoa; C34G6.7a.2; C34G6.7a.2; WBGene00004109. [O01498-1]
DR   EnsemblMetazoa; C34G6.7b.1; C34G6.7b.1; WBGene00004109. [O01498-2]
DR   GeneID; 172264; -.
DR   KEGG; cel:CELE_C34G6.7; -.
DR   CTD; 172264; -.
DR   WormBase; C34G6.7a; CE29700; WBGene00004109; stam-1. [O01498-1]
DR   WormBase; C34G6.7b; CE32816; WBGene00004109; stam-1. [O01498-2]
DR   eggNOG; KOG2199; Eukaryota.
DR   GeneTree; ENSGT00940000168664; -.
DR   InParanoid; O01498; -.
DR   OMA; AHALCQN; -.
DR   OrthoDB; 906159at2759; -.
DR   PhylomeDB; O01498; -.
DR   Reactome; R-CEL-182971; EGFR downregulation.
DR   Reactome; R-CEL-6807004; Negative regulation of MET activity.
DR   Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR   Reactome; R-CEL-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   PRO; PR:O01498; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00004109; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:WormBase.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0033565; C:ESCRT-0 complex; IPI:WormBase.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:WormBase.
DR   GO; GO:0043130; F:ubiquitin binding; IDA:WormBase.
DR   GO; GO:0008333; P:endosome to lysosome transport; IMP:WormBase.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IGI:UniProtKB.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0097499; P:protein localization to non-motile cilium; IMP:WormBase.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0034606; P:response to hermaphrodite contact; IMP:WormBase.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Developmental protein;
KW   Endosome; Protein transport; Reference proteome; SH3 domain; Transport.
FT   CHAIN           1..457
FT                   /note="Signal transducing adapter molecule 1"
FT                   /id="PRO_0000347284"
FT   DOMAIN          19..147
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          173..192
FT                   /note="UIM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          219..278
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          366..383
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255"
FT   REGION          196..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..435
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..8
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_052896"
FT   VAR_SEQ         397..405
FT                   /note="PNRAYYPPT -> VSFYSEKNI (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_052897"
FT   VAR_SEQ         406..457
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_052898"
SQ   SEQUENCE   457 AA;  50830 MW;  1AD9B1D83EBE2E16 CRC64;
     MKKQKSFPMS AYEDLLGKIT APTITVENWE GILAFCDMIN NDFEGSKTGI KSLRKRLNNR
     DPHVVLLAIS VLDSCWANCE ERFRKEVSSA QFINELKALC TSSQRQVAEK MRLTVQKWVD
     TECKTEQSLS LIVTLHKNLV ADGYSFVVDD PKSKTKAIDA KFANDPNYVG SAQEEEAIAK
     AIAASLADAE KQEKAKKSTS TMYPSAKASS PAVQTNSNIP EKNVRALYDF EAAESNELSF
     VAGDIITITD ESNPHWWTGR IGTQQGLFPS SFVTNQLDDL KSKETDSSQK APEVVASINE
     AILVRCLQVL HECDPTGERQ DPEDLAQLEA ASYAQGNLID AHLASIDRQS NSLAQIDVAI
     RDVLALYDDA IQKGGFQHQS QGMYQQPMQQ YNYQQPPNRA YYPPTGPVQQ QQPQQYPPQH
     YPAPGAQPQY ACPPNSVPQP QQQQQQWPAP SSQPQQY
 
 
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