ID   RGS3_CAEEL              Reviewed;         363 AA.
AC   Q18312;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Regulator of G-protein signaling rgs-3;
GN   Name=rgs-3; ORFNames=C29H12.3;
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 [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   [2]
RP   GENE NAME.
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   [3]
RP   FUNCTION.
RX   PubMed=21173231; DOI=10.1073/pnas.1017354108;
RA   Hallem E.A., Spencer W.C., McWhirter R.D., Zeller G., Henz S.R., Ratsch G.,
RA   Miller D.M., Horvitz H.R., Sternberg P.W., Ringstad N.;
RT   "Receptor-type guanylate cyclase is required for carbon dioxide sensation
RT   by Caenorhabditis elegans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:254-259(2011).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   SER-154.
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: Modulates chemotaxis responses by regulating positively the
CC       sensitivity to CO2 levels in BAG neurons and by regulating negatively
CC       the sensitivity to quinine in ASH sensory neurons.
CC       {ECO:0000269|PubMed:21173231, ECO:0000269|PubMed:23874221}.
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; FO080715; CCD66106.1; -; Genomic_DNA.
DR   PIR; T15700; T15700.
DR   RefSeq; NP_495223.1; NM_062822.3.
DR   AlphaFoldDB; Q18312; -.
DR   SMR; Q18312; -.
DR   STRING; 6239.C29H12.3a; -.
DR   PaxDb; Q18312; -.
DR   PeptideAtlas; Q18312; -.
DR   PRIDE; Q18312; -.
DR   EnsemblMetazoa; C29H12.3a.1; C29H12.3a.1; WBGene00004346.
DR   EnsemblMetazoa; C29H12.3a.2; C29H12.3a.2; WBGene00004346.
DR   GeneID; 174020; -.
DR   KEGG; cel:CELE_C29H12.3; -.
DR   UCSC; C29H12.3a; c. elegans.
DR   CTD; 174020; -.
DR   WormBase; C29H12.3a; CE29201; WBGene00004346; rgs-3.
DR   eggNOG; KOG3589; Eukaryota.
DR   InParanoid; Q18312; -.
DR   OMA; SYAEKWA; -.
DR   OrthoDB; 1037598at2759; -.
DR   PRO; PR:Q18312; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004346; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q18312; baseline and differential.
DR   GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0050913; P:sensory perception of bitter taste; IMP:UniProtKB.
DR   Gene3D; 1.10.167.10; -; 2.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   Pfam; PF00615; RGS; 2.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 2.
DR   SUPFAM; SSF48097; SSF48097; 2.
DR   PROSITE; PS50132; RGS; 2.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; Signal transduction inhibitor.
FT   CHAIN           1..363
FT                   /note="Regulator of G-protein signaling rgs-3"
FT                   /id="PRO_0000204239"
FT   DOMAIN          112..225
FT                   /note="RGS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          240..359
FT                   /note="RGS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         154
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   363 AA;  41407 MW;  BDB200D079399348 CRC64;
     MWRSYKAETP ELADETQEVD LNLHDSSESD HEGRQSRSAS ITSSTSAPAS NDVTLQVPIT
     NSSATSPTPS TGSMYFIAGM FDGKEKVNRE QPPMPTTDGV EYPRAASWAA GNCANVLNDD
     KGKQLFRVFL FQSLAEENLA FLEAMEKLKK MKISDEKVAY AKEILETYQG SINLSSSSMK
     SLRNAVASET LDMEEFAPAI KEVRRLLEND QFPRFRRSEL YLEYLEELLP RSYAEKWAQS
     FEGLLGNHVG RHHFRIFLRS IHAEENLRFW EAVVEFRSSR HKANAMNNLG KVILSTYLAE
     GTTNEVFLPF GVRQVIERRI QDNQIDITLF DEAIKHVEQV LRNDPYVRFL QSSQYIDLLS
     KLK