RGS8_RAT
ID RGS8_RAT Reviewed; 180 AA.
AC P49804;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Regulator of G-protein signaling 8;
DE Short=RGS8;
GN Name=Rgs8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GNAO1 AND GNAI3,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Hippocampus;
RX PubMed=9394004; DOI=10.1038/37385;
RA Saitoh O., Kubo Y., Miyatani Y., Asano T., Nakata H.;
RT "RGS8 accelerates G-protein-mediated modulation of K+ currents.";
RL Nature 390:525-528(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-153.
RC TISSUE=Brain;
RX PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA Koelle M.R., Horvitz H.R.;
RT "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT shares a conserved domain with many mammalian proteins.";
RL Cell 84:115-125(1996).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12880183; DOI=10.1080/14734220309409;
RA Saitoh O., Masuho I., Itoh M., Abe H., Komori K., Odagiri M.;
RT "Distribution of regulator of G protein signaling 8 (RGS8) protein in the
RT cerebellum.";
RL Cerebellum 2:154-160(2003).
RN [5]
RP FUNCTION.
RX PubMed=19609226; DOI=10.1097/wnr.0b013e32832fd93e;
RA Kurogi M., Nagatomo K., Kubo Y., Saitoh O.;
RT "Effects of spinophilin on the function of RGS8 regulating signals from M2
RT and M3-mAChRs.";
RL NeuroReport 20:1134-1139(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC including signaling via muscarinic acetylcholine receptor CHRM2 and
CC dopamine receptor DRD2. Inhibits signal transduction by increasing the
CC GTPase activity of G protein alpha subunits, thereby driving them into
CC their inactive GDP-bound form. Modulates the activity of potassium
CC channels that are activated in response to DRD2 and CHRM2 signaling.
CC {ECO:0000269|PubMed:19609226, ECO:0000269|PubMed:9394004}.
CC -!- SUBUNIT: Interacts with GNAO1 and GNAI3. {ECO:0000269|PubMed:9394004}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12880183};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Membrane {ECO:0000269|PubMed:9394004}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Perikaryon {ECO:0000269|PubMed:12880183}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12880183}. Nucleus {ECO:0000269|PubMed:12880183}.
CC Note=Detected in Purkinje cell soma and dendrites. Associated with
CC Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected
CC in the nucleus after heterologous expression. Recruited to the cell
CC membrane in the presence of GNAO1. {ECO:0000269|PubMed:12880183}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain. Very little
CC expression detected in other tissues (PubMed:9394004). Detected in
CC Purkinje cells in the cerebellum (PubMed:12880183).
CC {ECO:0000269|PubMed:12880183, ECO:0000269|PubMed:9394004}.
CC -!- DEVELOPMENTAL STAGE: Detected in 13-day old embryos. Expression
CC increases gradually in later embryos and markedly in neonates to
CC adults. {ECO:0000269|PubMed:9394004}.
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DR EMBL; AB006013; BAA23680.1; -; mRNA.
DR EMBL; BC089064; AAH89064.1; -; mRNA.
DR EMBL; U32432; AAC52369.1; -; mRNA.
DR RefSeq; NP_062217.1; NM_019344.2.
DR RefSeq; XP_006250078.1; XM_006250016.3.
DR AlphaFoldDB; P49804; -.
DR SMR; P49804; -.
DR STRING; 10116.ENSRNOP00000003239; -.
DR iPTMnet; P49804; -.
DR PhosphoSitePlus; P49804; -.
DR SwissPalm; P49804; -.
DR PaxDb; P49804; -.
DR Ensembl; ENSRNOT00000003239; ENSRNOP00000003239; ENSRNOG00000002369.
DR GeneID; 54297; -.
DR KEGG; rno:54297; -.
DR UCSC; RGD:3571; rat.
DR CTD; 85397; -.
DR RGD; 3571; Rgs8.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154304; -.
DR HOGENOM; CLU_059863_3_1_1; -.
DR InParanoid; P49804; -.
DR OMA; WSESFDS; -.
DR PhylomeDB; P49804; -.
DR TreeFam; TF315837; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P49804; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002369; Expressed in cerebellum and 5 other tissues.
DR ExpressionAtlas; P49804; baseline and differential.
DR Genevisible; P49804; RN.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR CDD; cd08711; RGS_RGS8; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034948; RGS8.
DR InterPro; IPR034949; RGS_RGS8.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF147; PTHR10845:SF147; 1.
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 Cell membrane; Cell projection; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..180
FT /note="Regulator of G-protein signaling 8"
FT /id="PRO_0000204201"
FT DOMAIN 56..171
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 180 AA; 20949 MW; 00FC35E4C278E857 CRC64;
MAALLMPRRN KGMRTRLGCL SHKSDSCSDF TAILPDKPNR ALKRLSTEEA TRWADSFDVL
LSHKYGVAAF RAFLKTEFSE ENLEFWLACE EFKKTRSTAK LVTKAHRIFE EFVDVQAPRE
VNIDFQTREA TRKNMQEPSL TCFDQAQGKV HSLMEKDSYP RFLRSKMYLD LLSQSQRRLS
