RGS20_BOVIN
ID RGS20_BOVIN Reviewed; 374 AA.
AC P79348;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Regulator of G-protein signaling 20;
DE Short=RGS20;
DE AltName: Full=Retina-specific regulator of G-protein signaling 1;
DE Short=Ret-RGS1;
GN Name=RGS20;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9096326; DOI=10.1073/pnas.94.7.2945;
RA Faurobert E., Hurley J.B.;
RT "The core domain of a new retina specific RGS protein stimulates the GTPase
RT activity of transducin in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2945-2950(1997).
RN [2]
RP PROTEIN SEQUENCE OF 312-325.
RC TISSUE=Brain;
RX PubMed=9748280; DOI=10.1074/jbc.273.40.26014;
RA Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.;
RT "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
RT association, regulation by Galphaz phosphorylation, and relationship to a
RT Gz GTPase-activating protein subfamily.";
RL J. Biol. Chem. 273:26014-26025(1998).
RN [3]
RP INHIBITION.
RX PubMed=9353196; DOI=10.1126/science.278.5340.1132;
RA Tu Y., Wang J., Ross E.M.;
RT "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G
RT protein alpha subunits.";
RL Science 278:1132-1135(1997).
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 -!- TISSUE SPECIFICITY: Retinal-specific. Expressed throughout the retina,
CC including photoreceptors.
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: Serine phosphorylated in synapsomal membranes. {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2 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; U89254; AAC48721.1; -; mRNA.
DR RefSeq; XP_005215480.1; XM_005215423.3.
DR AlphaFoldDB; P79348; -.
DR SMR; P79348; -.
DR STRING; 9913.ENSBTAP00000004487; -.
DR PaxDb; P79348; -.
DR Ensembl; ENSBTAT00000004487; ENSBTAP00000004487; ENSBTAG00000003454.
DR VEuPathDB; HostDB:ENSBTAG00000003454; -.
DR VGNC; VGNC:33919; RGS20.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159123; -.
DR HOGENOM; CLU_059863_0_0_1; -.
DR InParanoid; P79348; -.
DR OMA; HQTMENE; -.
DR OrthoDB; 1409647at2759; -.
DR TreeFam; TF315837; -.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-418597; G alpha (z) signalling events.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000003454; Expressed in retina and 68 other tissues.
DR ExpressionAtlas; P79348; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor; Ubl conjugation.
FT CHAIN 1..374
FT /note="Regulator of G-protein signaling 20"
FT /id="PRO_0000204232"
FT DOMAIN 248..364
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41917 MW; 23B39C2DC4A0617F CRC64;
MPRLSQDNQQ GHQKHFSRPS RRIQFLPPPW TEAYNVNVHQ TVENEGCATA MHNVKLLGSP
AAPTLLSLLS GTLSGFARFF ALLLRRPPPE APLRRRDFSA LIPALPAAVL SPGHEERPGR
LSLLLRAALA LPGRPPGGRL PREVDASAGQ SSSIPPMGSE WMEMRKRPVC AAQEPTACAP
GQPGVENQGS NACCFCWCCC CSCSCLTVRN QEEQRLRRTS YEARTEDLPT CEESPGPTLE
EASAWAQSFD KLMLTPAGRN AFREFLRTEF SEENMLFWMA CEELKKEANK ATIEEKARII
YEDYISILSP KEVSLDSRVR ETINRSMAEP SRNIFDDAQL QIYTLMHRDS YPRFMNSALY
KDLLRSLSEK AVEA
