RGS2_MOUSE
ID RGS2_MOUSE Reviewed; 211 AA.
AC O08849; Q544S7; Q91WX1; Q9JL24;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Regulator of G-protein signaling 2;
DE Short=RGS2;
GN Name=Rgs2;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9079700; DOI=10.1074/jbc.272.13.8679;
RA Chen C., Zheng B., Han J., Lin S.-C.;
RT "Characterization of a novel mammalian RGS protein that binds to Galpha
RT proteins and inhibits pheromone signaling in yeast.";
RL J. Biol. Chem. 272:8679-8685(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10779778; DOI=10.4049/jimmunol.164.9.4720;
RA Reif K., Cyster J.G.;
RT "RGS molecule expression in murine B lymphocytes and ability to down-
RT regulate chemotaxis to lymphoid chemokines.";
RL J. Immunol. 164:4720-4729(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Shen Q.-X., Wang J., Huang Z.-P.;
RT "Identification of novel endometrial and embryonic factors involved in
RT mouse embryo implantation.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14608379; DOI=10.1038/nm958;
RA Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P.,
RA Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E.;
RT "Regulator of G-protein signaling-2 mediates vascular smooth muscle
RT relaxation and blood pressure.";
RL Nat. Med. 9:1506-1512(2003).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form (By similarity). It is involved in the negative regulation
CC of the angiotensin-activated signaling pathway (By similarity). Plays a
CC role in the regulation of blood pressure in response to signaling via G
CC protein-coupled receptors and GNAQ. Plays a role in regulating the
CC constriction and relaxation of vascular smooth muscle
CC (PubMed:14608379). Binds EIF2B5 and blocks its activity, thereby
CC inhibiting the translation of mRNA into protein (By similarity).
CC {ECO:0000250|UniProtKB:P41220, ECO:0000269|PubMed:14608379}.
CC -!- SUBUNIT: Interacts with GNAQ. Does not interact with GNAI1 and GNAI3.
CC Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha).
CC {ECO:0000250|UniProtKB:P41220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41220}.
CC Cytoplasm {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P41220}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
CC {ECO:0000269|PubMed:9079700}.
CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads
CC to activation of RGS2 activity. {ECO:0000250|UniProtKB:P41220}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice display increased blood pressure and
CC impaired relaxation of vascular smooth muscle.
CC {ECO:0000269|PubMed:14608379}.
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DR EMBL; U67187; AAB50617.1; -; mRNA.
DR EMBL; AF215668; AAF34625.1; -; mRNA.
DR EMBL; AF432916; AAL28114.1; -; mRNA.
DR EMBL; AK031603; BAC27471.1; -; mRNA.
DR EMBL; AK077922; BAC37065.1; -; mRNA.
DR EMBL; AK162276; BAE36830.1; -; mRNA.
DR EMBL; BC023001; AAH23001.1; -; mRNA.
DR CCDS; CCDS15347.1; -.
DR RefSeq; NP_033087.2; NM_009061.4.
DR AlphaFoldDB; O08849; -.
DR SMR; O08849; -.
DR BioGRID; 202883; 2.
DR IntAct; O08849; 2.
DR MINT; O08849; -.
DR STRING; 10090.ENSMUSP00000115558; -.
DR iPTMnet; O08849; -.
DR PhosphoSitePlus; O08849; -.
DR MaxQB; O08849; -.
DR PaxDb; O08849; -.
DR PRIDE; O08849; -.
DR ProteomicsDB; 255253; -.
DR Antibodypedia; 34461; 288 antibodies from 30 providers.
DR DNASU; 19735; -.
DR Ensembl; ENSMUST00000127206; ENSMUSP00000115558; ENSMUSG00000026360.
DR GeneID; 19735; -.
DR KEGG; mmu:19735; -.
DR UCSC; uc007cxg.2; mouse.
DR CTD; 5997; -.
DR MGI; MGI:1098271; Rgs2.
DR VEuPathDB; HostDB:ENSMUSG00000026360; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157937; -.
DR HOGENOM; CLU_059863_3_2_1; -.
DR InParanoid; O08849; -.
DR OMA; GRMKRTI; -.
DR OrthoDB; 1246872at2759; -.
DR PhylomeDB; O08849; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 19735; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rgs2; mouse.
DR PRO; PR:O08849; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O08849; protein.
DR Bgee; ENSMUSG00000026360; Expressed in cumulus cell and 274 other tissues.
DR ExpressionAtlas; O08849; baseline and differential.
DR Genevisible; O08849; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IMP:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:BHF-UCL.
DR GO; GO:0010855; F:adenylate cyclase inhibitor activity; IMP:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
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:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0140194; P:negative regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway involved in heart process; IMP:BHF-UCL.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:1900924; P:negative regulation of glycine import across plasma membrane; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
DR GO; GO:0010519; P:negative regulation of phospholipase activity; IMP:BHF-UCL.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:UniProtKB.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034947; RGS2.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF43; PTHR10845:SF43; 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 2: Evidence at transcript level;
KW Cell cycle; Cell membrane; Cytoplasm; GTPase activation; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW Translation regulation.
FT CHAIN 1..211
FT /note="Regulator of G-protein signaling 2"
FT /id="PRO_0000204179"
FT DOMAIN 83..199
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 32..66
FT /note="Necessary for membrane association"
FT /evidence="ECO:0000250|UniProtKB:P41220"
FT REGION 79..116
FT /note="Necessary to inhibit protein synthesis"
FT /evidence="ECO:0000250|UniProtKB:P41220"
FT CONFLICT 39..40
FT /note="KD -> NH (in Ref. 1; AAB50617)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..79
FT /note="QL -> DV (in Ref. 3; AAL28114)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..79
FT /note="QL -> HV (in Ref. 1; AAB50617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24294 MW; 5D6E255C2BC7E7FA CRC64;
MQSAMFLAVQ HDCVPMDKSA GNGPKVEEKR EKMKRTLLKD WKTRLSYFLQ NSSAPGKPKT
GKKSKQQTFI KPSPEEAQLW AEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK
KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKSLIAQ NIQEATSGCF TTAQKRVYSL
MENNSYPRFL ESEFYQDLCK KPQITTEPHA T
