SHOC2_CAEEL
ID SHOC2_CAEEL Reviewed; 559 AA.
AC Q22875; O77472; Q8MPP6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Leucine-rich repeat protein soc-2;
DE AltName: Full=Suppressor of Clr protein 2;
DE AltName: Full=Suppressor of activated let-60 Ras protein 8;
GN Name=soc-2; Synonyms=sur-8; ORFNames=AC7.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH LET-60,
RP AND MUTAGENESIS OF CYS-233 AND GLU-430.
RC TISSUE=Vulva;
RX PubMed=9674433; DOI=10.1016/s0092-8674(00)81227-1;
RA Sieburth D.S., Sun Q., Han M.;
RT "SUR-8, a conserved Ras-binding protein with leucine-rich repeats,
RT positively regulates Ras-mediated signaling in C. elegans.";
RL Cell 94:119-130(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=9618511; DOI=10.1073/pnas.95.12.6903;
RA Selfors L.M., Schutzman J.L., Borland C.Z., Stern M.J.;
RT "Soc-2 encodes a leucine-rich repeat protein implicated in fibroblast
RT growth factor receptor signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6903-6908(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS A AND B).
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).
RN [4]
RP FUNCTION.
RX PubMed=10521400; DOI=10.1101/gad.13.19.2562;
RA Sieburth D.S., Sundaram M., Howard R.M., Han M.;
RT "A PP2A regulatory subunit positively regulates Ras-mediated signaling
RT during Caenorhabditis elegans vulval induction.";
RL Genes Dev. 13:2562-2569(1999).
RN [5]
RP FUNCTION.
RC STRAIN=Bristol N2;
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 [6]
RP FUNCTION.
RX PubMed=14685271; DOI=10.1038/sj.emboj.7600025;
RA Yoder J.H., Chong H., Guan K.-L., Han M.;
RT "Modulation of KSR activity in Caenorhabditis elegans by Zn ions, PAR-1
RT kinase and PP2A phosphatase.";
RL EMBO J. 23:111-119(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLU-430.
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).
CC -!- FUNCTION: Acts as a Ras effector and participates in MAPK pathway
CC activation (PubMed:9674433, PubMed:9618511). Probably acts as a
CC regulatory subunit of protein phosphatase that specifically
CC dephosphorylates Raf kinase and stimulates Raf activity at specialized
CC signaling complexes upon Ras activation (PubMed:10521400,
CC PubMed:14685271). Required for vulval development (PubMed:10521400).
CC Involved in fluid homeostasis (PubMed:11689700). Plays a role in
CC nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to
CC nicotine (PubMed:15990870). {ECO:0000269|PubMed:10521400,
CC ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:14685271,
CC ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:9618511,
CC ECO:0000269|PubMed:9674433}.
CC -!- SUBUNIT: Interacts with let-60. {ECO:0000269|PubMed:9674433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q22875-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q22875-2; Sequence=VSP_038198;
CC -!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
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; AF068919; AAC39129.1; -; mRNA.
DR EMBL; AF054827; AAC25697.1; -; mRNA.
DR EMBL; FO080091; CCD61151.1; -; Genomic_DNA.
DR EMBL; FO080091; CCD61152.1; -; Genomic_DNA.
DR PIR; B88684; B88684.
DR PIR; T30947; T30947.
DR PIR; T42998; T42998.
DR RefSeq; NP_001021259.1; NM_001026088.3. [Q22875-1]
DR RefSeq; NP_741391.2; NM_171332.3. [Q22875-2]
DR AlphaFoldDB; Q22875; -.
DR SMR; Q22875; -.
DR BioGRID; 42412; 4.
DR IntAct; Q22875; 1.
DR MINT; Q22875; -.
DR STRING; 6239.AC7.2a.1; -.
DR EPD; Q22875; -.
DR PaxDb; Q22875; -.
DR EnsemblMetazoa; AC7.2a.1; AC7.2a.1; WBGene00004929. [Q22875-1]
DR EnsemblMetazoa; AC7.2b.1; AC7.2b.1; WBGene00004929. [Q22875-2]
DR GeneID; 177286; -.
DR UCSC; AC7.2b; c. elegans.
DR CTD; 177286; -.
DR WormBase; AC7.2a; CE25736; WBGene00004929; soc-2. [Q22875-1]
DR WormBase; AC7.2b; CE31275; WBGene00004929; soc-2. [Q22875-2]
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_23_1; -.
DR InParanoid; Q22875; -.
DR OMA; NQFTSYP; -.
DR PhylomeDB; Q22875; -.
DR Reactome; R-CEL-5673000; RAF activation.
DR SignaLink; Q22875; -.
DR PRO; PR:Q22875; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004929; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q22875; baseline and differential.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0031344; P:regulation of cell projection organization; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0040025; P:vulval development; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027036; SHOC2.
DR PANTHER; PTHR48051:SF9; PTHR48051:SF9; 1.
DR Pfam; PF13855; LRR_8; 4.
DR SMART; SM00369; LRR_TYP; 17.
DR PROSITE; PS51450; LRR; 17.
PE 1: Evidence at protein level;
KW Alternative splicing; Leucine-rich repeat; Reference proteome; Repeat.
FT CHAIN 1..559
FT /note="Leucine-rich repeat protein soc-2"
FT /id="PRO_0000385631"
FT REPEAT 74..95
FT /note="LRR 1"
FT REPEAT 97..118
FT /note="LRR 2"
FT REPEAT 120..142
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT REPEAT 166..187
FT /note="LRR 5"
FT REPEAT 189..210
FT /note="LRR 6"
FT REPEAT 212..233
FT /note="LRR 7"
FT REPEAT 235..256
FT /note="LRR 8"
FT REPEAT 258..279
FT /note="LRR 9"
FT REPEAT 281..302
FT /note="LRR 10"
FT REPEAT 305..326
FT /note="LRR 11"
FT REPEAT 329..350
FT /note="LRR 12"
FT REPEAT 353..374
FT /note="LRR 13"
FT REPEAT 376..397
FT /note="LRR 14"
FT REPEAT 399..420
FT /note="LRR 15"
FT REPEAT 422..443
FT /note="LRR 16"
FT REPEAT 445..466
FT /note="LRR 17"
FT REPEAT 468..489
FT /note="LRR 18"
FT REPEAT 491..513
FT /note="LRR 19"
FT REPEAT 515..536
FT /note="LRR 20"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..60
FT /note="METSKEFEFRPAKETSRSKSPGGIVGRLSNFARNKARHSLSEKGSNSVGGSG
FT GAGFDKPR -> MRVLQKLGFCLEKQKRETPPTTANTGVSATKRVSVIATDRDRAYFLR
FT QKNMRNNKGHAE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_038198"
FT MUTAGEN 233
FT /note="C->Y: In ku242; suppresses an activated ras mutation
FT and dramatically enhances phenotypes of mpk-1 MAP kinase
FT and ksr-1 mutations. Abolishes interaction with let-60."
FT /evidence="ECO:0000269|PubMed:9674433"
FT MUTAGEN 430
FT /note="E->K: In ku167; suppresses an activated ras mutation
FT and dramatically enhances phenotypes of mpk-1 MAP kinase
FT and ksr-1 mutations. Moderate increase in resistance to
FT nicotine-induced paralysis."
FT /evidence="ECO:0000269|PubMed:15990870,
FT ECO:0000269|PubMed:9674433"
SQ SEQUENCE 559 AA; 62483 MW; ED68F9771998C456 CRC64;
METSKEFEFR PAKETSRSKS PGGIVGRLSN FARNKARHSL SEKGSNSVGG SGGAGFDKPR
KDLLKEFHKC KEAQDQRLDL SSIEITSIPS PIKELTQLTE LFLYKNKLTC LPTEIGQLVN
LKKLGLSENA LTSLPDSLAS LESLETLDLR HNKLTEVPSV IYKIGSLETL WLRYNRIVAV
DEQIGNLSKL KMLDVRENKI RELPSAIGKL TSLVVCLVSY NHLTRVPEEI GDCHSLTQLD
LQHNDLSELP YSIGKLVNLV RIGIRYNKIR CIPSELESCQ QLEEFIVESN HLQLLPPNLL
TMLPKIHTVN LSRNELTAFP AGGPQQFVST VTINMEHNQI SKIPIGIFSK ATRLTKLNLK
ENELVSLPLD MGSWTSITEL NLSTNQLKVL PEDIEKLVNL EILVLSNNQL KKLPNQIGNL
NKLRELDLEE NELETVPTEI GFLQHLTKLW VQSNKILTLP RSIGNLCSLQ DLRLGENNLT
AIPEEIGHLD SLKSLYLNDN SSLHNLPFEL ALCQSLEIMS IENSPLSQIP PEITAGGPSL
VIQYLKMQGP YRGVVMNSQ
