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STAT1_CAEEL
ID   STAT1_CAEEL             Reviewed;         706 AA.
AC   Q9NAD6; A5HWB4; Q29TW4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Signal transducer and activator of transcription 1;
GN   Name=sta-1 {ECO:0000303|PubMed:16401427}; ORFNames=Y51H4A.17;
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 [MRNA] (ISOFORM C), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2;
RX   PubMed=16401427; DOI=10.1016/j.cub.2005.11.061;
RA   Wang Y., Levy D.E.;
RT   "C. elegans STAT cooperates with DAF-7/TGF-beta signaling to repress dauer
RT   formation.";
RL   Curr. Biol. 16:89-94(2006).
RN   [2]
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).
CC   -!- FUNCTION: Carries out a dual function: signal transduction and
CC       activation of transcription. Activated STAT proteins play a role in
CC       repression of dauer formation. Neuronal expression is held in check by
CC       negative signals through the TGF-beta pathway that target the daf-3
CC       transcription factor. {ECO:0000269|PubMed:16401427}.
CC   -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC       member. {ECO:0000250|UniProtKB:P51692}.
CC   -!- INTERACTION:
CC       Q9NAD6; O44400: F37C4.5; NbExp=2; IntAct=EBI-312137, EBI-312011;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16401427}. Nucleus
CC       {ECO:0000269|PubMed:16401427}. Note=Translocated into the nucleus in
CC       response to phosphorylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a;
CC         IsoId=Q9NAD6-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q9NAD6-2; Sequence=VSP_038159, VSP_038160;
CC       Name=c;
CC         IsoId=Q9NAD6-3; Sequence=VSP_038161;
CC   -!- TISSUE SPECIFICITY: Expressed in adult and larval pharynx, head
CC       ganglia, tail ganglia, ventral nerve cord and body muscles.
CC       {ECO:0000269|PubMed:16401427}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000255}.
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DR   EMBL; AY943817; AAY18583.1; -; mRNA.
DR   EMBL; AL132952; CAB61149.2; -; Genomic_DNA.
DR   EMBL; AL132952; CAN86928.1; -; Genomic_DNA.
DR   EMBL; AL132952; CAN99759.1; -; Genomic_DNA.
DR   RefSeq; NP_001122814.1; NM_001129342.2. [Q9NAD6-2]
DR   RefSeq; NP_001122815.1; NM_001129343.2. [Q9NAD6-3]
DR   RefSeq; NP_502974.2; NM_070573.4. [Q9NAD6-1]
DR   AlphaFoldDB; Q9NAD6; -.
DR   SMR; Q9NAD6; -.
DR   BioGRID; 43543; 19.
DR   DIP; DIP-24746N; -.
DR   IntAct; Q9NAD6; 8.
DR   STRING; 6239.Y51H4A.17a; -.
DR   iPTMnet; Q9NAD6; -.
DR   EPD; Q9NAD6; -.
DR   PaxDb; Q9NAD6; -.
DR   PeptideAtlas; Q9NAD6; -.
DR   PRIDE; Q9NAD6; -.
DR   EnsemblMetazoa; Y51H4A.17a.1; Y51H4A.17a.1; WBGene00013111. [Q9NAD6-1]
DR   EnsemblMetazoa; Y51H4A.17b.1; Y51H4A.17b.1; WBGene00013111. [Q9NAD6-2]
DR   EnsemblMetazoa; Y51H4A.17c.1; Y51H4A.17c.1; WBGene00013111. [Q9NAD6-3]
DR   GeneID; 178465; -.
DR   KEGG; cel:CELE_Y51H4A.17; -.
DR   UCSC; Y51H4A.17a; c. elegans.
DR   CTD; 178465; -.
DR   WormBase; Y51H4A.17a; CE35668; WBGene00013111; sta-1. [Q9NAD6-1]
DR   WormBase; Y51H4A.17b; CE41061; WBGene00013111; sta-1. [Q9NAD6-2]
DR   WormBase; Y51H4A.17c; CE22342; WBGene00013111; sta-1. [Q9NAD6-3]
DR   eggNOG; KOG3667; Eukaryota.
DR   GeneTree; ENSGT01050000244905; -.
DR   InParanoid; Q9NAD6; -.
DR   OMA; DKGHMSA; -.
DR   OrthoDB; 327469at2759; -.
DR   PhylomeDB; Q9NAD6; -.
DR   Reactome; R-CEL-1059683; Interleukin-6 signaling.
DR   Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-CEL-186763; Downstream signal transduction.
DR   Reactome; R-CEL-201556; Signaling by ALK.
DR   Reactome; R-CEL-3249367; STAT6-mediated induction of chemokines.
DR   Reactome; R-CEL-6783783; Interleukin-10 signaling.
DR   Reactome; R-CEL-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-CEL-877300; Interferon gamma signaling.
DR   Reactome; R-CEL-8854691; Interleukin-20 family signaling.
DR   Reactome; R-CEL-8983432; Interleukin-15 signaling.
DR   Reactome; R-CEL-8984722; Interleukin-35 Signalling.
DR   Reactome; R-CEL-8985947; Interleukin-9 signaling.
DR   Reactome; R-CEL-9008059; Interleukin-37 signaling.
DR   Reactome; R-CEL-9020591; Interleukin-12 signaling.
DR   Reactome; R-CEL-9020933; Interleukin-23 signaling.
DR   Reactome; R-CEL-9020956; Interleukin-27 signaling.
DR   Reactome; R-CEL-909733; Interferon alpha/beta signaling.
DR   Reactome; R-CEL-9701898; STAT3 nuclear events downstream of ALK signaling.
DR   SignaLink; Q9NAD6; -.
DR   PRO; PR:Q9NAD6; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00013111; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR   GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.60.40.630; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR013800; STAT_TF_alpha.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR013801; STAT_TF_DNA-bd.
DR   InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR   PANTHER; PTHR11801; PTHR11801; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF01017; STAT_alpha; 1.
DR   Pfam; PF02864; STAT_bind; 1.
DR   SUPFAM; SSF47655; SSF47655; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..706
FT                   /note="Signal transducer and activator of transcription 1"
FT                   /id="PRO_0000233906"
FT   DOMAIN          477..574
FT                   /note="SH2"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         557..567
FT                   /note="YMYPAIDKEEM -> LVLDAKSLPCC (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038159"
FT   VAR_SEQ         568..706
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038160"
FT   VAR_SEQ         602..604
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000303|PubMed:16401427"
FT                   /id="VSP_038161"
SQ   SEQUENCE   706 AA;  80581 MW;  39F3755A1573A03C CRC64;
     MMGSSSQELQ TALTDVSKTC HHLWEENKDL QGRFVNELGE LQRLQMVIAQ LEQQQRLENV
     FTVKQQMTEL QKRAATLYEH LTQKRNDIVI KLNDGTNFAT MLQTQLIGEK LFSWKNAQKL
     AQIGMPFDNR EQLLDEIQIE FEFLADQNWQ LNMFSCWMLD LLRRAPQLND GLAQATIGKL
     TAITEQLNKL LFMLVSQSFI VSVQPEPVLK TQHKFVTEVR LLIGDKLGIR QHLVNTNVSV
     KIIAEDEAKQ LSVDYDAHKE IRNNKTVGTI SNDFEKLTMN ERGHLAAKFN NSKLTRIAHR
     KPPPKGASDL KCAASMQAAT DQKYALLFFI TPFQMGNLSK EEQFDVWTLS LPIMVTVHGS
     QDCDAQVAIL WHRAFASISR NPNTTDVTAV TWDNLAIMLR NKFSLFTGAR RPLSDSDLAY
     LSEKMLMPNV ADQKPITFHR FAKQAMRDDL PFSFWEWFFS IMQLIKQKLL KFWDEGWCIG
     FISKNDASQS MMMCQHSSFL LRFSDSQTGA VSIGFVCEEA DGQKIPFHLA PFTIKDLDQL
     SLASRIASCP QLKDIRYMYP AIDKEEMLRF FESEERHRVG GGDSPTGYIQ SEIVMVAKTN
     GNFRRMSNAP SMFGADSPSP LSVQSKLDWS PGEVHQNHMM EMSDELGQIL TVSDMSGDVE
     TLLGPAFKNN ITNYNPHDGN HQHNLHFVDM SQQGMMQQHH NQFYPS
 
 
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