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SHCH1_CAEEL
ID   SHCH1_CAEEL             Reviewed;         316 AA.
AC   Q9TYT3; H2KZG0; H2KZG2;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=SHC-transforming protein homolog 1 {ECO:0000250|UniProtKB:P29353};
DE   AltName: Full=Src homology 2 domain adapter homolog 1 {ECO:0000305};
GN   Name=shc-1 {ECO:0000312|WormBase:F54A5.3a};
GN   ORFNames=F54A5.3 {ECO:0000312|WormBase:F54A5.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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, INTERACTION WITH DAF-2 AND MEK-1, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=18832074; DOI=10.1101/gad.478408;
RA   Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R.,
RA   Hertweck M.;
RT   "SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to
RT   modulate life span and stress response in C. elegans.";
RL   Genes Dev. 22:2721-2735(2008).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH MEK-1 AND MLK-1, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF ARG-136 AND ARG-234.
RX   PubMed=18809575; DOI=10.1128/mcb.00938-08;
RA   Mizuno T., Fujiki K., Sasakawa A., Hisamoto N., Matsumoto K.;
RT   "Role of the Caenorhabditis elegans Shc adaptor protein in the c-Jun N-
RT   terminal kinase signaling pathway.";
RL   Mol. Cell. Biol. 28:7041-7049(2008).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH MLK-1.
RX   PubMed=23072806; DOI=10.1038/ncomms2136;
RA   Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
RA   Hisamoto N.;
RT   "Endocannabinoid-Goalpha signalling inhibits axon regeneration in
RT   Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
RL   Nat. Commun. 3:1136-1136(2012).
RN   [5]
RP   FUNCTION, INTERACTION WITH SVH-2 AND SVH-4, AND MUTAGENESIS OF ARG-234.
RX   PubMed=27984580; DOI=10.1371/journal.pgen.1006475;
RA   Hisamoto N., Nagamori Y., Shimizu T., Pastuhov S.I., Matsumoto K.;
RT   "The C. elegans discoidin domain receptor DDR-2 modulates the Met-like RTK-
RT   JNK signaling pathway in axon regeneration.";
RL   PLoS Genet. 12:E1006475-E1006475(2016).
CC   -!- FUNCTION: Scaffold protein which plays an important role in the
CC       activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1; by
CC       bringing together mek-1 and mlk-1, promotes mlk-1-mediated
CC       phosphorylation and activation of mek-1 which in turn phosphorylates
CC       kgb-1 (PubMed:18832074, PubMed:18809575). In addition, negatively
CC       modulates the activation of the insulin/IGF-1-like signaling (IIS)
CC       probably by inhibiting the insulin receptor daf-2. Positively regulates
CC       the activity of the transcription factor daf-16/FOXO by both inhibiting
CC       IIS and activating the JNK pathway (PubMed:18832074). Involved in the
CC       response to several environmental stresses including heavy metal ions
CC       (Cu(2+) and Cd(2+)), heat, oxidative and protein misfolding (ER)
CC       stresses (PubMed:18832074, PubMed:18809575). Plays a role in life span
CC       and egg laying (PubMed:18832074, PubMed:23072806). Plays a role in axon
CC       regeneration after injury (PubMed:23072806, PubMed:27984580).
CC       {ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074,
CC       ECO:0000269|PubMed:23072806, ECO:0000269|PubMed:27984580}.
CC   -!- SUBUNIT: Interacts (via PID domain) with daf-2 (via cytoplasmic domain)
CC       (PubMed:18832074). Interacts with mek-1; the interaction is independent
CC       of mek-1 catalytic activity and is constitutive (PubMed:18832074,
CC       PubMed:18809575). Interacts (via N-terminus) with mlk-1 (via NPQY motif
CC       when phosphorylated on tyrosine residue) (PubMed:18809575,
CC       PubMed:23072806). Does not interact with jkk-1 or sek-1
CC       (PubMed:18809575). Interacts (via SH2 domain) with svh-2
CC       (PubMed:27984580). Interacts with svh-4 (PubMed:27984580).
CC       {ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074,
CC       ECO:0000269|PubMed:23072806, ECO:0000269|PubMed:27984580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832074}. Nucleus
CC       {ECO:0000269|PubMed:18832074}. Cell membrane
CC       {ECO:0000269|PubMed:18832074}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:18832074}. Note=In intestinal cells, enriched in
CC       the nucleus. {ECO:0000269|PubMed:18832074}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:F54A5.3a};
CC         IsoId=Q9TYT3-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F54A5.3b};
CC         IsoId=Q9TYT3-2; Sequence=VSP_057798, VSP_057801;
CC       Name=d {ECO:0000312|WormBase:F54A5.3d};
CC         IsoId=Q9TYT3-3; Sequence=VSP_057799, VSP_057800;
CC   -!- TISSUE SPECIFICITY: Expressed in hypodermis, intestine, head and tail
CC       neurons, pharynx, gonads, vulva and body muscles.
CC       {ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074}.
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DR   EMBL; BX284601; CCD68061.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD68062.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD68064.1; -; Genomic_DNA.
DR   PIR; T33836; T33836.
DR   RefSeq; NP_490799.2; NM_058398.4. [Q9TYT3-1]
DR   RefSeq; NP_490800.2; NM_058399.4.
DR   AlphaFoldDB; Q9TYT3; -.
DR   SMR; Q9TYT3; -.
DR   DIP; DIP-25661N; -.
DR   IntAct; Q9TYT3; 2.
DR   STRING; 6239.F54A5.3a; -.
DR   EPD; Q9TYT3; -.
DR   PaxDb; Q9TYT3; -.
DR   PeptideAtlas; Q9TYT3; -.
DR   EnsemblMetazoa; F54A5.3a.1; F54A5.3a.1; WBGene00018788. [Q9TYT3-1]
DR   EnsemblMetazoa; F54A5.3b.1; F54A5.3b.1; WBGene00018788.
DR   EnsemblMetazoa; F54A5.3b.2; F54A5.3b.2; WBGene00018788.
DR   EnsemblMetazoa; F54A5.3b.3; F54A5.3b.3; WBGene00018788.
DR   GeneID; 3565745; -.
DR   KEGG; cel:CELE_F54A5.3; -.
DR   UCSC; F54A5.3a; c. elegans. [Q9TYT3-1]
DR   CTD; 3565745; -.
DR   WormBase; F54A5.3a; CE30804; WBGene00018788; shc-1.
DR   WormBase; F54A5.3b; CE20862; WBGene00018788; shc-1.
DR   WormBase; F54A5.3d; CE29391; WBGene00018788; shc-1.
DR   eggNOG; KOG3697; Eukaryota.
DR   GeneTree; ENSGT00950000182870; -.
DR   HOGENOM; CLU_861198_0_0_1; -.
DR   InParanoid; Q9TYT3; -.
DR   OMA; VKECINM; -.
DR   OrthoDB; 1351843at2759; -.
DR   PhylomeDB; Q9TYT3; -.
DR   SignaLink; Q9TYT3; -.
DR   PRO; PR:Q9TYT3; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00018788; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:WormBase.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:WormBase.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR   GO; GO:0033674; P:positive regulation of kinase activity; IDA:WormBase.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:WormBase.
DR   GO; GO:0010038; P:response to metal ion; IMP:WormBase.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd09925; SH2_SHC; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035676; SHC_SH2.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW   Reference proteome; SH2 domain; Stress response.
FT   CHAIN           1..316
FT                   /note="SHC-transforming protein homolog 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433512"
FT   DOMAIN          16..158
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          211..307
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          292..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            234
FT                   /note="Required for interaction with svh-2"
FT                   /evidence="ECO:0000269|PubMed:27984580"
FT   VAR_SEQ         71..81
FT                   /note="VIGEVKKENFP -> PTLHGSMKKPR (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057798"
FT   VAR_SEQ         72..76
FT                   /note="IGEVK -> DQKSR (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057799"
FT   VAR_SEQ         77..316
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057800"
FT   VAR_SEQ         82..316
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057801"
FT   MUTAGEN         136
FT                   /note="R->K: Partial sensitivity to Cu(2+). May prevent
FT                   interaction with mlk-1 when phosphorylated at Tyr-209 which
FT                   in turn may prevent the interaction between mlk-1 and mek-
FT                   1. No effect on the association with mek-1. Severe
FT                   sensitivity to Cu(2+) and no effect on the association with
FT                   mek-1; when associated with K-234."
FT                   /evidence="ECO:0000269|PubMed:18809575"
FT   MUTAGEN         234
FT                   /note="R->K: Weak sensitivity to Cu(2+). Severe sensitivity
FT                   to Cu(2+) and no effect on the association with mek-1; when
FT                   associated with K-136. Abolishes interaction with svh-2."
FT                   /evidence="ECO:0000269|PubMed:18809575,
FT                   ECO:0000269|PubMed:27984580"
SQ   SEQUENCE   316 AA;  35170 MW;  D370FF4B941F97E1 CRC64;
     MLNVEPSFAE ELRSSGVSLS ATYLGSVPVV ESINVMVSEM RVQVVSECIQ HVAATVGVTA
     AREINPVVSR VIGEVKKENF PVDINISSKM IKIIKQSRLI QRHPFSFFSF GAQGQKGTDT
     ELMFGYIAKN KDGTDRRCHV VFIEDVHKLI DVLTTAINVN TFDAQANAST SNDGFTVPAP
     PMRHRSSLHR QSFVSNCRAP TVTEDVVGKV WYHGNLSRED AQALLKTEGD FLVRQSDHTP
     GKYVLSGRTA ENEHKHLILL DNHNRVRTRD RTFSNISELI DYHVNNGMAV RSEGRDRETS
     LNLIRPVPCP GSDDIE
 
 
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