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RGS20_CHICK
ID   RGS20_CHICK             Reviewed;         218 AA.
AC   Q9PWA1;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Regulator of G-protein signaling 20;
DE            Short=RGS20;
DE   AltName: Full=Gz-selective GTPase-activating protein;
DE            Short=G(z)GAP;
DE            Short=Gz-GAP;
GN   Name=RGS20;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spinal ganglion;
RX   PubMed=10419452; DOI=10.1074/jbc.274.31.21507;
RA   Jordan J.D., Carey K.D., Stork P.J.S., Iyengar R.;
RT   "Modulation of rap activity by direct interaction of Galpha(o) with Rap1
RT   GTPase-activating protein.";
RL   J. Biol. Chem. 274:21507-21510(1999).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into their
CC       inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-
CC       i2 subunits, accelerates their GTPase activity and regulates their
CC       signaling activities. The G(z)-alpha activity is inhibited by the
CC       phosphorylation and palmitoylation of the G-protein. Negatively
CC       regulates mu-opioid receptor-mediated activation of the G-proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid
CC       receptors; the formation of this complex results in mu-opioid receptor
CC       desensitization. Interacts with OPRM1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm.
CC       Note=Shuttles between the cytoplasm/cell membrane and the nucleus.
CC       Anchored to the membrane through palmitoylation. {ECO:0000250}.
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000250}.
CC   -!- PTM: Sumoylated by SUMO1 and SUM02 in synaptosomes. The sumoylated
CC       forms act as a scaffold for sequestering mu-opioid receptor-activated
CC       G(alpha) subunits (By similarity). {ECO:0000250}.
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DR   EMBL; AF151967; AAD45947.1; -; mRNA.
DR   RefSeq; NP_990173.1; NM_204842.2.
DR   AlphaFoldDB; Q9PWA1; -.
DR   SMR; Q9PWA1; -.
DR   STRING; 9031.ENSGALP00000041794; -.
DR   PaxDb; Q9PWA1; -.
DR   Ensembl; ENSGALT00000051502; ENSGALP00000044202; ENSGALG00000025941.
DR   GeneID; 395646; -.
DR   KEGG; gga:395646; -.
DR   CTD; 8601; -.
DR   VEuPathDB; HostDB:geneid_395646; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000159123; -.
DR   HOGENOM; CLU_059863_0_2_1; -.
DR   InParanoid; Q9PWA1; -.
DR   OMA; HQTMENE; -.
DR   PhylomeDB; Q9PWA1; -.
DR   PRO; PR:Q9PWA1; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000025941; Expressed in brain and 7 other tissues.
DR   ExpressionAtlas; Q9PWA1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.167.10; -; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate;
KW   Reference proteome; Signal transduction inhibitor; Ubl conjugation.
FT   CHAIN           1..218
FT                   /note="Regulator of G-protein signaling 20"
FT                   /id="PRO_0000204235"
FT   DOMAIN          92..208
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  25141 MW;  188564BAA5868A38 CRC64;
     MGSERTEMRK RQMAATQETP GTAQAQHSVG NRGPNACCFC WCCCCSCSCL TVRNQEEERA
     RRTSHELQAE GIPNCEESPA PTLEEVNAWA QSFDKLMLTP AGRNAFREFL RTEFSEENML
     FWMACEELKQ ESNKSVIEEK ARLIYEDYIS ILSPKEVSLD SRVREVINRN MLEPSQHTFD
     DAQLQIYTLM HRDSYPRFMN SAIYKDLLRS LSEKSIEA
 
 
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