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Sex muscle abnormal protein 5

 SEM5_CAEEL              Reviewed;         228 AA.
P29355;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
07-JUN-2017, entry version 147.
RecName: Full=Sex muscle abnormal protein 5;
Name=sem-5; ORFNames=C14F5.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF PRO-49;
GLU-90; SER-91 AND GLY-201.
PubMed=1372395; DOI=10.1038/356340a0;
Clark S.G., Stern M.J., Horvitz H.R.;
"C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and
SH3 domains.";
Nature 356:340-344(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
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).
[3]
FUNCTION.
PubMed=9073451; DOI=10.1006/dbio.1996.8473;
Chen E.B., Branda C.S., Stern M.J.;
"Genetic enhancers of sem-5 define components of the gonad-independent
guidance mechanism controlling sex myoblast migration in
Caenorhabditis elegans hermaphrodites.";
Dev. Biol. 182:88-100(1997).
[4]
FUNCTION, AND MUTAGENESIS OF ARG-87.
PubMed=11689700; DOI=10.1128/MCB.21.23.8104-8116.2001;
Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
Stern M.J.;
"The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-
like multisubstrate adaptor protein in fibroblast growth factor signal
transduction.";
Mol. Cell. Biol. 21:8104-8116(2001).
[5]
FUNCTION.
PubMed=12169634; DOI=10.1093/emboj/cdf430;
Hajnal A., Berset T.;
"The C.elegans MAPK phosphatase LIP-1 is required for the G(2)/M
meiotic arrest of developing oocytes.";
EMBO J. 21:4317-4326(2002).
[6]
FUNCTION, AND MUTAGENESIS OF GLU-90.
PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D.,
Yates J.R. III, Schafer W.R.;
"Identification and characterization of novel nicotinic receptor-
associated proteins in Caenorhabditis elegans.";
EMBO J. 24:2566-2578(2005).
[7]
FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
GLU-90.
PubMed=16495308; DOI=10.1242/dev.02300;
Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
"FGF negatively regulates muscle membrane extension in Caenorhabditis
elegans.";
Development 133:1263-1275(2006).
[8]
FUNCTION, INTERACTION WITH SOC-1, AND MUTAGENESIS OF GLY-201.
PubMed=16547100; DOI=10.1534/genetics.106.055822;
Hopper N.A.;
"The adaptor protein soc-1/Gab1 modifies growth factor receptor output
in Caenorhabditis elegans.";
Genetics 173:163-175(2006).
[9]
FUNCTION, INTERACTION WITH MIG-2; MIG-13 AND WSP-1, AND SUBCELLULAR
LOCATION.
PubMed=27780040; DOI=10.1016/j.devcel.2016.09.029;
Zhu Z., Chai Y., Jiang Y., Li W., Hu H., Li W., Wu J.W., Wang Z.X.,
Huang S., Ou G.;
"Functional coordination of WAVE and WASP in C. elegans neuroblast
migration.";
Dev. Cell 39:224-238(2016).
[10]
STRUCTURE BY NMR OF 153-214.
PubMed=7802869; DOI=10.1038/372375a0;
Lim W.A., Richards F.M., Fox R.O.;
"Structural determinants of peptide-binding orientation and of
sequence specificity in SH3 domains.";
Nature 372:375-379(1994).
[11]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 155-214.
PubMed=9851931; DOI=10.1126/science.282.5396.2088;
Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.;
"Exploiting the basis of proline recognition by SH3 and WW domains:
design of N-substituted inhibitors.";
Science 282:2088-2092(1998).
-!- FUNCTION: Adapter protein which modulates signaling mediated by
several receptor tyrosine kinases such as egl-15 and let-23
probably acting upstream of let-60/ras. Negatively regulates vulva
induction probably downstream of let-23 (PubMed:1372395,
PubMed:16547100). Involved in sex myoblast migration
(PubMed:1372395, PubMed:9073451). Negatively regulates fluid
homeostasis probably downstream of egl-15 (PubMed:1372395,
PubMed:11689700). During the formation of neuromuscular junctions
at the larval stage, negatively regulates membrane protrusion from
body wall muscles probably downstream of egl-15 (PubMed:16495308).
Involved in cytoskeleton dynamics and is recruited by mig-13 to
the leading edge of Q neuroblasts and their descendants to signal
downstream to activate the wsp-1 pathway and direct migration
along the anteroposterior body axis during larval development
(PubMed:27780040). Involved in let-23-mediated regulation of
fertility independently of let-60/Ras (PubMed:16547100).
Negatively regulates daf-2-mediated repression of dauer formation
(PubMed:16547100). Plays a role in nicotinic acetylcholine
receptor (nAChR)-mediated sensitivity to nicotine
(PubMed:15990870). Regulates synaptic levels of nAchR subunit lev-
1 in the nerve cord (PubMed:15990870). May play a role in oocyte
development upstream of let-60/Ras and the MAP kinase pathway
(PubMed:12169634). {ECO:0000269|PubMed:11689700,
ECO:0000269|PubMed:12169634, ECO:0000269|PubMed:1372395,
ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16495308,
ECO:0000269|PubMed:16547100, ECO:0000269|PubMed:27780040,
ECO:0000269|PubMed:9073451}.
-!- SUBUNIT: Interacts (probably via SH3 domain 2) with soc-1 (via C-
terminus) (PubMed:16547100). Interacts with mig-2 (active GTP-
bound form) and wsp-1 (PubMed:27780040). Interacts with mig-13;
the interaction is direct (PubMed:27780040).
{ECO:0000269|PubMed:16547100, ECO:0000269|PubMed:27780040}.
-!- INTERACTION:
Q62245:Sos1 (xeno); NbExp=2; IntAct=EBI-315286, EBI-1693;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27780040}.
Note=Targeted to the leading edge of Q neuroblasts by mig-13.
{ECO:0000269|PubMed:27780040}.
-!- TISSUE SPECIFICITY: Expressed in body wall muscles, pharynx,
intestine and hypodermis. {ECO:0000269|PubMed:16495308}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown or RNAi-mediated
knockdown in body wall muscles causes ectopic membrane extensions
from body wall muscles. {ECO:0000269|PubMed:16495308}.
-!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S88446; AAB21850.1; -; mRNA.
EMBL; FO080456; CCD63850.1; -; Genomic_DNA.
PIR; S25730; S25730.
RefSeq; NP_509342.1; NM_076941.5.
UniGene; Cel.19703; -.
PDB; 1K76; NMR; -; A=155-214.
PDB; 1KFZ; NMR; -; A=155-214.
PDB; 1SEM; X-ray; 2.00 A; A/B=155-212.
PDB; 2SEM; X-ray; 2.20 A; A/B=155-214.
PDB; 3SEM; X-ray; 2.20 A; A/B=155-214.
PDBsum; 1K76; -.
PDBsum; 1KFZ; -.
PDBsum; 1SEM; -.
PDBsum; 2SEM; -.
PDBsum; 3SEM; -.
ProteinModelPortal; P29355; -.
SMR; P29355; -.
BioGrid; 45979; 113.
DIP; DIP-27394N; -.
IntAct; P29355; 27.
MINT; MINT-114046; -.
STRING; 6239.C14F5.5; -.
EPD; P29355; -.
PaxDb; P29355; -.
PeptideAtlas; P29355; -.
PRIDE; P29355; -.
EnsemblMetazoa; C14F5.5; C14F5.5; WBGene00004774.
GeneID; 181055; -.
KEGG; cel:CELE_C14F5.5; -.
UCSC; C14F5.5; c. elegans.
CTD; 181055; -.
WormBase; C14F5.5; CE01784; WBGene00004774; sem-5.
eggNOG; KOG3601; Eukaryota.
eggNOG; ENOG410XR1G; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000251625; -.
InParanoid; P29355; -.
KO; K04364; -.
OMA; HWWHGEI; -.
OrthoDB; EOG091G0HWS; -.
PhylomeDB; P29355; -.
Reactome; R-CEL-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-CEL-167044; Signalling to RAS.
Reactome; R-CEL-179812; GRB2 events in EGFR signaling.
Reactome; R-CEL-180292; GAB1 signalosome.
Reactome; R-CEL-180336; SHC1 events in EGFR signaling.
Reactome; R-CEL-182971; EGFR downregulation.
Reactome; R-CEL-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-CEL-210993; Tie2 Signaling.
Reactome; R-CEL-2179392; EGFR Transactivation by Gastrin.
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-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
Reactome; R-CEL-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-CEL-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-CEL-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-CEL-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-CEL-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-CEL-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-CEL-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-CEL-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-CEL-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-CEL-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-CEL-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-CEL-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
Reactome; R-CEL-6807004; Negative regulation of MET activity.
Reactome; R-CEL-74749; Signal attenuation.
Reactome; R-CEL-74751; Insulin receptor signalling cascade.
Reactome; R-CEL-8851805; MET activates RAS signaling.
Reactome; R-CEL-8851907; MET activates PI3K/AKT signaling.
Reactome; R-CEL-8865999; MET activates PTPN11.
Reactome; R-CEL-8875555; MET activates RAP1 and RAC1.
Reactome; R-CEL-8875656; MET receptor recycling.
SignaLink; P29355; -.
EvolutionaryTrace; P29355; -.
PRO; PR:P29355; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00004774; -.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:WormBase.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0005070; F:SH3/SH2 adaptor activity; ISS:WormBase.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030539; P:male genitalia development; IMP:WormBase.
GO; GO:0007517; P:muscle organ development; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0031344; P:regulation of cell projection organization; IMP:WormBase.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0040028; P:regulation of vulval development; IMP:WormBase.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Membrane;
Reference proteome; Repeat; SH2 domain; SH3 domain.
CHAIN 1 228 Sex muscle abnormal protein 5.
/FTId=PRO_0000088212.
DOMAIN 1 58 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 60 152 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 154 213 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MUTAGEN 49 49 P->L: In n1619; lethal at the larval
stage, mild defect in vulva development
and partially impaired sex myoblast
migration. Rescues fluid accumulation in
crl-1 e1745ts mutant.
{ECO:0000269|PubMed:1372395}.
MUTAGEN 87 87 R->Q: In ay73; partial rod-like larval
lethality. Surviving mutant have a thin
body and no vulva. Rescues fluid
accumulation in clr-1 e1745ts mutant.
{ECO:0000269|PubMed:11689700}.
MUTAGEN 90 90 E->K: In n1779; mild defect in vulva
development and partially impaired sex
myoblast migration. Causes ectopic muscle
membrane extension. Reduced lev-1
synaptic levels. Moderate increase in
resistance to nicotine-induced paralysis.
Rescues fluid accumulation in crl-1
e1745ts mutant.
{ECO:0000269|PubMed:1372395,
ECO:0000269|PubMed:15990870,
ECO:0000269|PubMed:16495308}.
MUTAGEN 91 91 S->N: In n1781; no obvious defects.
Partially rescues fluid accumulation in
crl-1 e1745ts mutant.
{ECO:0000269|PubMed:1372395}.
MUTAGEN 201 201 G->R: In n2195; loss of interaction with
soc-1. Partially restores normal vulva
induction in let-60 n1046gf mutant.
Partially rescues fluid accumulation in
crl-1 e1745ts mutant. Partially prevents
constitutive dauer formation in daf-2
m577 mutant. {ECO:0000269|PubMed:1372395,
ECO:0000269|PubMed:16547100}.
STRAND 158 163 {ECO:0000244|PDB:1SEM}.
STRAND 169 172 {ECO:0000244|PDB:1K76}.
STRAND 180 185 {ECO:0000244|PDB:1SEM}.
STRAND 187 196 {ECO:0000244|PDB:1SEM}.
STRAND 199 204 {ECO:0000244|PDB:1SEM}.
HELIX 205 207 {ECO:0000244|PDB:1SEM}.
STRAND 208 212 {ECO:0000244|PDB:1SEM}.
SEQUENCE 228 AA; 26210 MW; 2D684C9520646C41 CRC64;
MEAVAEHDFQ AGSPDELSFK RGNTLKVLNK DEDPHWYKAE LDGNEGFIPS NYIRMTECNW
YLGKITRNDA EVLLKKPTVR DGHFLVRQCE SSPGEFSISV RFQDSVQHFK VLRDQNGKYY
LWAVKFNSLN ELVAYHRTAS VSRTHTILLS DMNVETKFVQ ALFDFNPQES GELAFKRGDV
ITLINKDDPN WWEGQLNNRR GIFPSNYVCP YNSNKSNSNV APGFNFGN


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