SOC1_CAEEL
ID SOC1_CAEEL Reviewed; 430 AA.
AC G5EDJ4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Multisubstrate adapter protein soc-1 {ECO:0000303|PubMed:11689700};
DE AltName: Full=Suppressor Of Clr protein 1 {ECO:0000312|WormBase:F41F3.2};
GN Name=soc-1 {ECO:0000312|WormBase:F41F3.2};
GN ORFNames=F41F3.2 {ECO:0000312|WormBase:F41F3.2};
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|EMBL:AAL15971.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, PHOSPHORYLATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF TYR-20; TYR-31; TYR-112; TRP-124; TYR-171;
RP TYR-181; PRO-200; TYR-202; TYR-220; TYR-232; 239-PRO-PRO-240; TYR-293;
RP TYR-306; TYR-340; TYR-354; TYR-365; TYR-378 AND TYR-408.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAL15971.1};
RX PubMed=11689700; DOI=10.1128/mcb.21.23.8104-8116.2001;
RA Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
RA Stern M.J.;
RT "The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like
RT multisubstrate adaptor protein in fibroblast growth factor signal
RT transduction.";
RL Mol. Cell. Biol. 21:8104-8116(2001).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
RA Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III,
RA Schafer W.R.;
RT "Identification and characterization of novel nicotinic receptor-associated
RT proteins in Caenorhabditis elegans.";
RL EMBO J. 24:2566-2578(2005).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SEM-5, AND DISRUPTION PHENOTYPE.
RX PubMed=16547100; DOI=10.1534/genetics.106.055822;
RA Hopper N.A.;
RT "The adaptor protein soc-1/Gab1 modifies growth factor receptor output in
RT Caenorhabditis elegans.";
RL Genetics 173:163-175(2006).
CC -!- FUNCTION: Adapter protein which modulates signaling mediated by several
CC receptor tyrosine kinases. Plays a role in fluid homeostasis, probably
CC downstream of receptor egl-15 and upstream of let-60/Ras
CC (PubMed:11689700). Involved in nicotinic acetylcholine receptor
CC (nAChR)-mediated sensitivity to nicotine and levamisole and gamma-
CC aminobutyric acid (GABA)receptor-mediated sensitivity to muscimol
CC (PubMed:15990870). Regulates synaptic levels of nAchR receptor subunit
CC lev-1 and unc-38, and GABA receptor subunit unc-49 in the nerve cord,
CC probably downstream of egl-15 (PubMed:15990870). Regulates motility
CC (PubMed:15990870). During the formation of neuromuscular junctions at
CC the larval stage, down-regulates membrane protrusion from body wall
CC muscles, probably downstream of egl-15 (PubMed:16495308). Promotes
CC vulva induction and down-regulates fertility, probably downstream of
CC receptor let-23 (PubMed:16547100). Down-regulates daf-2-mediated
CC repression of dauer formation and positively regulates daf-2-mediated
CC aging (PubMed:16547100). May be involved in the recruitment of
CC phosphatase ptp-2 to egl-15 (PubMed:11689700).
CC {ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100}.
CC -!- SUBUNIT: Interacts (via C-terminus) with sem-5 (probably via SH3 domain
CC 2) (PubMed:16547100). Interacts with nicotinic acetylcholine receptor
CC (PubMed:15990870). {ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:16547100}.
CC -!- DOMAIN: The PH domain is required for fluid homeostasis.
CC {ECO:0000269|PubMed:11689700}.
CC -!- DOMAIN: The C-terminal domain is required for fluid homeostasis.
CC {ECO:0000269|PubMed:11689700}.
CC -!- PTM: May be phosphorylated. {ECO:0000269|PubMed:11689700}.
CC -!- DISRUPTION PHENOTYPE: Causes a decrease in synaptic levels of lev-1,
CC unc-38 and unc-49, a moderate resistance to paralysis induced by
CC nicotine and levamisole (PubMed:15990870) and a mild increase in
CC uncoordinated movements. In addition, forms ectopic muscle membrane
CC extension during larval stage (PubMed:16495308). Rescues fluid
CC accumulation in clr-1 e1745ts mutant (PubMed:11689700). Partially
CC suppresses multi-vulva formation and partially restores fertility in
CC let-60 1046gf mutant (PubMed:16547100). Prevents constitutive dauer
CC formation in daf-2 m577 mutant (PubMed:16547100).
CC {ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF419335; AAL15971.1; -; mRNA.
DR EMBL; BX284605; CCD71016.1; -; Genomic_DNA.
DR PIR; T29729; T29729.
DR RefSeq; NP_504250.2; NM_071849.4.
DR AlphaFoldDB; G5EDJ4; -.
DR IntAct; G5EDJ4; 1.
DR MINT; G5EDJ4; -.
DR STRING; 6239.F41F3.2; -.
DR EPD; G5EDJ4; -.
DR PaxDb; G5EDJ4; -.
DR PRIDE; G5EDJ4; -.
DR EnsemblMetazoa; F41F3.2.1; F41F3.2.1; WBGene00004928.
DR GeneID; 178855; -.
DR KEGG; cel:CELE_F41F3.2; -.
DR CTD; 178855; -.
DR WormBase; F41F3.2; CE30786; WBGene00004928; soc-1.
DR eggNOG; ENOG502TGXK; Eukaryota.
DR GeneTree; ENSGT00940000175323; -.
DR HOGENOM; CLU_639732_0_0_1; -.
DR InParanoid; G5EDJ4; -.
DR OMA; WVNEICK; -.
DR OrthoDB; 1273571at2759; -.
DR Reactome; R-CEL-109704; PI3K Cascade.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-180292; GAB1 signalosome.
DR Reactome; R-CEL-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-CEL-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-CEL-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-CEL-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-CEL-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-CEL-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-CEL-8875656; MET receptor recycling.
DR SignaLink; G5EDJ4; -.
DR PRO; PR:G5EDJ4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004928; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046355; Gab1-4-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45960; PTHR45960; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..430
FT /note="Multisubstrate adapter protein soc-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435953"
FT DOMAIN 7..133
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 192..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-31; F-112; F-171; F-181; F-
FT 220; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-31; F-112; F-171; F-181; F-220; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 31
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-112; F-171; F-181; F-
FT 220; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-112; F-171; F-181; F-220; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 112
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-171; F-181; F-
FT 220; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-171; F-181; F-220; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 124
FT /note="W->A: No rescue of fluid accumulation in clr-1
FT e1745ts mutant."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 171
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-181; F-
FT 220; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-181; F-220; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 181
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 220; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-220; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 200
FT /note="P->A: Rescues fluid accumulation in clr-1 e1745ts
FT mutant; when associated with A-239 and A-240."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 202
FT /note="Y->F: Likely abolishes phosphorylation. Rescues
FT fluid accumulation in clr-1 e1745ts mutant; when associated
FT with F-340."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 220
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-232; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-232; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 232
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-293; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 293; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 239..240
FT /note="PP->AA: Rescues fluid accumulation in clr-1 e1745ts
FT mutant; when associated with A-200."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 293
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-232; F-306; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 232; F-306; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 306
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-232; F-293; F-354; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 232; F-293; F-354; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 340
FT /note="Y->F: Likely abolishes phosphorylation. Rescues
FT fluid accumulation in clr-1 e1745ts mutant; when associated
FT with F-202."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 354
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-232; F-293; F-306; F-365 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 232; F-293; F-306; F-365; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 365
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-232; F-293; F-306; F-354 and F-378. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 232; F-293; F-306; F-354; F-378 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 378
FT /note="Y->F: Likely abolishes phosphorylation. Almost
FT complete rescue of fluid accumulation in clr-1 e1745ts
FT mutant; when associated with F-20; F-31; F-112; F-171; F-
FT 181; F-220; F-232; F-293; F-306; F-354 and F-365. No rescue
FT of fluid accumulation in clr-1 e1745ts mutant; when
FT associated with F-20; F-31; F-112; F-171; F-181; F-220; F-
FT 232; F-293; F-306; F-354; F-365 and F-408."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 408
FT /note="Y->F: Likely abolishes phosphorylation. Weak rescue
FT of fluid accumulation in clr-1 e1745ts mutant. No rescue of
FT fluid accumulation in clr-1 e1745ts mutant; when associated
FT with F-20; F-31; F-112; F-171; F-181; F-220; F-232; F-293;
FT F-306; F-354; F-365 and F-378."
FT /evidence="ECO:0000269|PubMed:11689700"
SQ SEQUENCE 430 AA; 48954 MW; 655A3C5D72E7A7F4 CRC64;
MSIPDENIIL EGSLKRCKKY KLFKTKWVEH YFVLHCRDRE RNLFAIDEFK TSRKNDLKKR
FKLEFVIRVE SNLSVSDPSI LCTAGGGHQE ESMLNCIFGV GFRFENIVKD LYLVAKNDEE
MTLWVNEICK LCKLHRQHDE GDSSHAAESS ISGMSMSSQS LDMSIIEQQQ YAENIPESKQ
YHRMHHFKSV ISHNSLPSNP NYNNLPDPLE SSRSETSSMY SSRRTEDDSV SYTSGPPVPP
PRTRHTLNRF VKNGQVGRLH MIPASTSMGQ VVKVEDAEDS SGETLKLDTP EQYPESVTSS
EGFPVYERNG KTLIRRAPPP VDRSNKPKNL RGEEEAGTRY RNLSRNGVNE NGNYSATFSS
RTSNYQQSET SKRRNLDYFE PTQMIENSSL STLAATSTRS PTPSDIEYIS VDVDRTLAFK
QMRRAAQSTD
