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SHC-transforming protein homolog 1 (Src homology 2 domain adapter homolog 1)

 SHCH1_CAEEL             Reviewed;         316 AA.
Q9TYT3; H2KZG0; H2KZG2;
22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
05-DEC-2018, entry version 135.
RecName: Full=SHC-transforming protein homolog 1 {ECO:0000250|UniProtKB:P29353};
AltName: Full=Src homology 2 domain adapter homolog 1 {ECO:0000305};
Name=shc-1 {ECO:0000312|WormBase:F54A5.3a};
ORFNames=F54A5.3 {ECO:0000312|WormBase:F54A5.3a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, INTERACTION WITH DAF-2 AND MEK-1, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=18832074; DOI=10.1101/gad.478408;
Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R.,
Hertweck M.;
"SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to
modulate life span and stress response in C. elegans.";
Genes Dev. 22:2721-2735(2008).
[3] {ECO:0000305}
FUNCTION, INTERACTION WITH MEK-1 AND MLK-1, TISSUE SPECIFICITY, AND
MUTAGENESIS OF ARG-136 AND ARG-234.
PubMed=18809575; DOI=10.1128/MCB.00938-08;
Mizuno T., Fujiki K., Sasakawa A., Hisamoto N., Matsumoto K.;
"Role of the Caenorhabditis elegans Shc adaptor protein in the c-Jun
N-terminal kinase signaling pathway.";
Mol. Cell. Biol. 28:7041-7049(2008).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MLK-1.
PubMed=23072806; DOI=10.1038/ncomms2136;
Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
Hisamoto N.;
"Endocannabinoid-Goalpha signalling inhibits axon regeneration in
Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
Nat. Commun. 3:1136-1136(2012).
[5]
FUNCTION, INTERACTION WITH SVH-2 AND SVH-4, AND MUTAGENESIS OF
ARG-234.
PubMed=27984580; DOI=10.1371/journal.pgen.1006475;
Hisamoto N., Nagamori Y., Shimizu T., Pastuhov S.I., Matsumoto K.;
"The C. elegans discoidin domain receptor DDR-2 modulates the Met-like
RTK-JNK signaling pathway in axon regeneration.";
PLoS Genet. 12:E1006475-E1006475(2016).
-!- FUNCTION: Scaffold protein which plays an important role in the
activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1;
by bringing together mek-1 and mlk-1, promotes mlk-1-mediated
phosphorylation and activation of mek-1 which in turn
phosphorylates kgb-1 (PubMed:18832074, PubMed:18809575). In
addition, negatively modulates the activation of the insulin/IGF-
1-like signaling (IIS) probably by inhibiting the insulin receptor
daf-2. Positively regulates the activity of the transcription
factor daf-16/FOXO by both inhibiting IIS and activating the JNK
pathway (PubMed:18832074). Involved in the response to several
environmental stresses including heavy metal ions (Cu(2+) and
Cd(2+)), heat, oxidative and protein misfolding (ER) stresses
(PubMed:18832074, PubMed:18809575). Plays a role in life span and
egg laying (PubMed:18832074, PubMed:23072806). Plays a role in
axon regeneration after injury (PubMed:23072806, PubMed:27984580).
{ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:23072806, ECO:0000269|PubMed:27984580}.
-!- SUBUNIT: Interacts (via PID domain) with daf-2 (via cytoplasmic
domain) (PubMed:18832074). Interacts with mek-1; the interaction
is independent of mek-1 catalytic activity and is constitutive
(PubMed:18832074, PubMed:18809575). Interacts (via N-terminus)
with mlk-1 (via NPQY motif when phosphorylated on tyrosine
residue) (PubMed:18809575, PubMed:23072806). Does not interact
with jkk-1 or sek-1 (PubMed:18809575). Interacts (via SH2 domain)
with svh-2 (PubMed:27984580). Interacts with svh-4
(PubMed:27984580). {ECO:0000269|PubMed:18809575,
ECO:0000269|PubMed:18832074, ECO:0000269|PubMed:23072806,
ECO:0000269|PubMed:27984580}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832074}.
Nucleus {ECO:0000269|PubMed:18832074}. Cell membrane
{ECO:0000269|PubMed:18832074}; Peripheral membrane protein
{ECO:0000269|PubMed:18832074}. Note=In intestinal cells, enriched
in the nucleus. {ECO:0000269|PubMed:18832074}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:F54A5.3a};
IsoId=Q9TYT3-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:F54A5.3b};
IsoId=Q9TYT3-2; Sequence=VSP_057798, VSP_057801;
Note=No experimental confirmation available. {ECO:0000305};
Name=d {ECO:0000312|WormBase:F54A5.3d};
IsoId=Q9TYT3-3; Sequence=VSP_057799, VSP_057800;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in hypodermis, intestine, head and
tail neurons, pharynx, gonads, vulva and body muscles.
{ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074}.
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EMBL; BX284601; CCD68061.1; -; Genomic_DNA.
EMBL; BX284601; CCD68062.1; -; Genomic_DNA.
EMBL; BX284601; CCD68064.1; -; Genomic_DNA.
PIR; T33836; T33836.
RefSeq; NP_490799.2; NM_058398.4. [Q9TYT3-1]
RefSeq; NP_490800.2; NM_058399.4.
UniGene; Cel.23038; -.
ProteinModelPortal; Q9TYT3; -.
SMR; Q9TYT3; -.
DIP; DIP-25661N; -.
IntAct; Q9TYT3; 2.
STRING; 6239.F54A5.3a; -.
EPD; Q9TYT3; -.
PaxDb; Q9TYT3; -.
PeptideAtlas; Q9TYT3; -.
EnsemblMetazoa; F54A5.3a; F54A5.3a; WBGene00018788. [Q9TYT3-1]
GeneID; 3565745; -.
KEGG; cel:CELE_F54A5.3; -.
UCSC; F54A5.3a; c. elegans. [Q9TYT3-1]
CTD; 3565745; -.
WormBase; F54A5.3a; CE30804; WBGene00018788; shc-1.
WormBase; F54A5.3b; CE20862; WBGene00018788; shc-1.
WormBase; F54A5.3d; CE29391; WBGene00018788; shc-1.
eggNOG; KOG3697; Eukaryota.
eggNOG; ENOG410XTJN; LUCA.
GeneTree; ENSGT00940000153127; -.
HOGENOM; HOG000017678; -.
InParanoid; Q9TYT3; -.
KO; K06279; -.
OMA; CHQLGIC; -.
OrthoDB; EOG091G0LW2; -.
PhylomeDB; Q9TYT3; -.
Reactome; R-CEL-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-CEL-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-CEL-167044; Signalling to RAS.
Reactome; R-CEL-180336; SHC1 events in EGFR signaling.
Reactome; R-CEL-2424491; DAP12 signaling.
Reactome; R-CEL-2428933; SHC-related events triggered by IGF1R.
Reactome; R-CEL-2871796; FCERI mediated MAPK activation.
Reactome; R-CEL-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-CEL-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-CEL-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
Reactome; R-CEL-74749; Signal attenuation.
Reactome; R-CEL-74751; Insulin receptor signalling cascade.
Reactome; R-CEL-8851805; MET activates RAS signaling.
SignaLink; Q9TYT3; -.
PRO; PR:Q9TYT3; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00018788; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:WormBase.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:WormBase.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:WormBase.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:WormBase.
GO; GO:0010038; P:response to metal ion; IMP:WormBase.
CDD; cd09925; SH2_SHC; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035676; SHC_SH2.
Pfam; PF00640; PID; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00462; PTB; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS01179; PID; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Nucleus; Reference proteome; SH2 domain; Stress response.
CHAIN 1 316 SHC-transforming protein homolog 1.
{ECO:0000305}.
/FTId=PRO_0000433512.
DOMAIN 16 158 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 211 307 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
SITE 234 234 Required for interaction with svh-2.
{ECO:0000269|PubMed:27984580}.
VAR_SEQ 71 81 VIGEVKKENFP -> PTLHGSMKKPR (in isoform
b). {ECO:0000305}.
/FTId=VSP_057798.
VAR_SEQ 72 76 IGEVK -> DQKSR (in isoform d).
{ECO:0000305}.
/FTId=VSP_057799.
VAR_SEQ 77 316 Missing (in isoform d). {ECO:0000305}.
/FTId=VSP_057800.
VAR_SEQ 82 316 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_057801.
MUTAGEN 136 136 R->K: Partial sensitivity to Cu(2+). May
prevent interaction with mlk-1 when
phosphorylated at Tyr-209 which in turn
may prevent the interaction between mlk-1
and mek-1. No effect on the association
with mek-1. Severe sensitivity to Cu(2+)
and no effect on the association with
mek-1; when associated with K-234.
{ECO:0000269|PubMed:18809575}.
MUTAGEN 234 234 R->K: Weak sensitivity to Cu(2+). Severe
sensitivity to Cu(2+) and no effect on
the association with mek-1; when
associated with K-136. Abolishes
interaction with svh-2.
{ECO:0000269|PubMed:18809575,
ECO:0000269|PubMed:27984580}.
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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