ID   RGS2_CAEEL              Reviewed;         169 AA.
AC   P49808;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Regulator of G-protein signaling rgs-2;
GN   Name=rgs-2; ORFNames=F16H9.1;
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], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10950865;
RA   Dong M.-Q., Chase D., Patikoglou G.A., Koelle M.R.;
RT   "Multiple RGS proteins alter neural G protein signaling to allow C. elegans
RT   to rapidly change behavior when fed.";
RL   Genes Dev. 14:2003-2014(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [3]
RP   FUNCTION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   SER-126.
RX   PubMed=23874221; DOI=10.1371/journal.pgen.1003619;
RA   Krzyzanowski M.C., Brueggemann C., Ezak M.J., Wood J.F., Michaels K.L.,
RA   Jackson C.A., Juang B.T., Collins K.D., Yu M.C., L'etoile N.D.,
RA   Ferkey D.M.;
RT   "The C. elegans cGMP-dependent protein kinase EGL-4 regulates nociceptive
RT   behavioral sensitivity.";
RL   PLoS Genet. 9:E1003619-E1003619(2013).
CC   -!- FUNCTION: Weakly inhibits G protein signaling in nervous system,
CC       interacting preferentially with the G(O) subfamily member goa-1. In
CC       vitro, it acts as a GTPase activator of goa-1. Rgs-1 and rgs-2
CC       redundantly adjust signaling when worms are fed to allow rapid
CC       induction of egg-laying behavior (PubMed:10950865). Modulates
CC       chemotaxis responses by regulating negatively the sensitivity to
CC       quinine in ASH sensory neurons (PubMed:23874221).
CC       {ECO:0000269|PubMed:10950865, ECO:0000269|PubMed:23874221}.
CC   -!- TISSUE SPECIFICITY: Expressed in a subset of neurons including ventral
CC       cord and head- and tail-ganglia neurons. Also expressed in non-neuronal
CC       cells including pharyngeal and uterine muscles.
CC       {ECO:0000269|PubMed:10950865}.
CC   -!- PTM: May be phosphorylated and activated by egl-4.
CC       {ECO:0000269|PubMed:23874221}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in ASH sensory neurons
CC       results in hypersensitivity to dilute quinine.
CC       {ECO:0000269|PubMed:23874221}.
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DR   EMBL; AF220265; AAF33782.1; -; mRNA.
DR   EMBL; Z50005; CAA90295.1; -; Genomic_DNA.
DR   EMBL; Z67882; CAA90295.1; JOINED; Genomic_DNA.
DR   PIR; T21034; T21034.
DR   RefSeq; NP_510124.2; NM_077723.3.
DR   AlphaFoldDB; P49808; -.
DR   SMR; P49808; -.
DR   BioGRID; 46318; 3.
DR   DIP; DIP-26991N; -.
DR   STRING; 6239.F16H9.1b; -.
DR   PaxDb; P49808; -.
DR   EnsemblMetazoa; F16H9.1a.1; F16H9.1a.1; WBGene00004345.
DR   GeneID; 181414; -.
DR   UCSC; F16H9.1b; c. elegans.
DR   CTD; 181414; -.
DR   WormBase; F16H9.1a; CE03211; WBGene00004345; rgs-2.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00970000196738; -.
DR   InParanoid; P49808; -.
DR   OrthoDB; 1409647at2759; -.
DR   Reactome; R-CEL-416476; G alpha (q) signalling events.
DR   Reactome; R-CEL-418594; G alpha (i) signalling events.
DR   PRO; PR:P49808; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00004345; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; P49808; baseline and differential.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:WormBase.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.167.10; -; 1.
DR   Gene3D; 1.10.196.10; -; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; SSF48097; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..169
FT                   /note="Regulator of G-protein signaling rgs-2"
FT                   /id="PRO_0000204238"
FT   DOMAIN          39..158
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   MUTAGEN         126
FT                   /note="S->A: Hypersensitivity to quinine which may be due
FT                   to loss of phosphorylation at this site."
FT                   /evidence="ECO:0000269|PubMed:23874221"
SQ   SEQUENCE   169 AA;  19594 MW;  2A9415538238D91D CRC64;
     MRLLTCDCTF MGQKHSGSVS VEKKNQENDG PPTYEIVFGW SQSFENLMKH RAGQKYFAEF
     LKGEYSDENI LFWQACEELK REKNAEKIEE KARIIYEDFI SILSPKEVSL DSRVREIVNT
     NMGRPSASTF DEAQNQIYTL MQRDSYPRFL ASNIYKTVMG TFGIKEEAV