RGS8_MOUSE
ID RGS8_MOUSE Reviewed; 180 AA.
AC Q8BXT1; Q505F2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Regulator of G-protein signaling 8;
DE Short=RGS8;
GN Name=Rgs8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:P49804}.
CC -!- SUBUNIT: Interacts with GNAO1 and GNAI3.
CC {ECO:0000250|UniProtKB:P49804}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49804};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P49804}. Membrane
CC {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49804}. Perikaryon
CC {ECO:0000250|UniProtKB:P49804}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P49804}. Nucleus {ECO:0000250|UniProtKB:P49804}.
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:0000250|UniProtKB:P49804}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK044337; BAC31874.1; -; mRNA.
DR EMBL; AK142301; BAE25020.1; -; mRNA.
DR EMBL; BC065056; AAH65056.1; -; mRNA.
DR EMBL; BC094577; AAH94577.1; -; mRNA.
DR CCDS; CCDS15375.1; -.
DR RefSeq; NP_080656.2; NM_026380.3.
DR RefSeq; XP_006529881.1; XM_006529818.3.
DR RefSeq; XP_006529882.1; XM_006529819.3.
DR RefSeq; XP_006529883.1; XM_006529820.3.
DR RefSeq; XP_006529884.1; XM_006529821.3.
DR AlphaFoldDB; Q8BXT1; -.
DR SMR; Q8BXT1; -.
DR BioGRID; 212446; 1.
DR STRING; 10090.ENSMUSP00000045715; -.
DR iPTMnet; Q8BXT1; -.
DR PhosphoSitePlus; Q8BXT1; -.
DR SwissPalm; Q8BXT1; -.
DR PaxDb; Q8BXT1; -.
DR PRIDE; Q8BXT1; -.
DR ProteomicsDB; 255195; -.
DR Antibodypedia; 34440; 130 antibodies from 21 providers.
DR DNASU; 67792; -.
DR Ensembl; ENSMUST00000041776; ENSMUSP00000045715; ENSMUSG00000042671.
DR Ensembl; ENSMUST00000111810; ENSMUSP00000107441; ENSMUSG00000042671.
DR Ensembl; ENSMUST00000111812; ENSMUSP00000107443; ENSMUSG00000042671.
DR GeneID; 67792; -.
DR KEGG; mmu:67792; -.
DR UCSC; uc007dad.1; mouse.
DR CTD; 85397; -.
DR MGI; MGI:108408; Rgs8.
DR VEuPathDB; HostDB:ENSMUSG00000042671; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154304; -.
DR HOGENOM; CLU_059863_3_1_1; -.
DR InParanoid; Q8BXT1; -.
DR OMA; WSESFDS; -.
DR OrthoDB; 1295370at2759; -.
DR PhylomeDB; Q8BXT1; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 67792; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rgs8; mouse.
DR PRO; PR:Q8BXT1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BXT1; protein.
DR Bgee; ENSMUSG00000042671; Expressed in cerebellum lobe and 87 other tissues.
DR ExpressionAtlas; Q8BXT1; baseline and differential.
DR Genevisible; Q8BXT1; MM.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
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; GTPase activation; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..180
FT /note="Regulator of G-protein signaling 8"
FT /id="PRO_0000204200"
FT DOMAIN 56..171
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49804"
SQ SEQUENCE 180 AA; 20963 MW; 00FC35E572785856 CRC64;
MAALLMPRRN KGMRTRLGCL SHKSDSCSDF TAILPDKPNR ALKRLSTEEA TRWAESFDVL
LSHKYGVAAF RAFLKTEFSE ENLEFWLACE EFKKTRSTAK LVTKAHRIFE EFVDVQAPRE
VNIDFQTREA TRKNMQEPSL TCFDQAQGKV HSLMEKDSYP RFLRSKMYLD LLSQSQRRLS
