RGS5_MOUSE
ID RGS5_MOUSE Reviewed; 181 AA.
AC O08850; Q543B1; Q9D0Z2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Regulator of G-protein signaling 5;
DE Short=RGS5;
GN Name=Rgs5;
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].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, and Oviduct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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).
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 to G(i)-alpha and G(o)-alpha, but not to
CC G(s)-alpha.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15539}.
CC Membrane {ECO:0000250|UniProtKB:O15539}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and muscle.
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DR EMBL; U67188; AAB50618.1; -; mRNA.
DR EMBL; AK004165; BAB23201.1; -; mRNA.
DR EMBL; AK044096; BAC31773.1; -; mRNA.
DR EMBL; AK054098; BAC35655.1; -; mRNA.
DR EMBL; BC037683; AAH37683.1; -; mRNA.
DR CCDS; CCDS15464.1; -.
DR RefSeq; NP_033089.2; NM_009063.4.
DR AlphaFoldDB; O08850; -.
DR SMR; O08850; -.
DR ELM; O08850; -.
DR STRING; 10090.ENSMUSP00000027997; -.
DR PhosphoSitePlus; O08850; -.
DR PaxDb; O08850; -.
DR PRIDE; O08850; -.
DR ProteomicsDB; 253265; -.
DR Antibodypedia; 982; 412 antibodies from 30 providers.
DR DNASU; 19737; -.
DR Ensembl; ENSMUST00000027997; ENSMUSP00000027997; ENSMUSG00000026678.
DR GeneID; 19737; -.
DR KEGG; mmu:19737; -.
DR UCSC; uc007dlm.1; mouse.
DR CTD; 8490; -.
DR MGI; MGI:1098434; Rgs5.
DR VEuPathDB; HostDB:ENSMUSG00000026678; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157380; -.
DR HOGENOM; CLU_059863_3_0_1; -.
DR InParanoid; O08850; -.
DR OMA; MAQKRIF; -.
DR OrthoDB; 1416350at2759; -.
DR PhylomeDB; O08850; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 19737; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rgs5; mouse.
DR PRO; PR:O08850; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O08850; protein.
DR Bgee; ENSMUSG00000026678; Expressed in aorta tunica media and 261 other tissues.
DR ExpressionAtlas; O08850; baseline and differential.
DR Genevisible; O08850; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
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:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR CDD; cd08717; RGS_RGS5; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034955; RGS5.
DR InterPro; IPR034956; RGS_RGS5.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF42; PTHR10845:SF42; 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 Cytoplasm; Membrane; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..181
FT /note="Regulator of G-protein signaling 5"
FT /id="PRO_0000204189"
FT DOMAIN 64..180
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT CONFLICT 49..50
FT /note="KA -> NG (in Ref. 1; AAB50618)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> T (in Ref. 1; AAB50618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 21086 MW; B4B561CFE3DA9630 CRC64;
MCKGLAALPH SCLERAKEIK IKLGILLQKP DSAVDLVIPY NEKPEKPAKA HKPSLEEVLQ
WRQSLDKLLQ NSYGFASFKS FLKSEFSEEN LEFWVACENY KKIKSPIKMA EKAKQIYEEF
IQTEAPKEVN IDHFTKDITM KNLVEPSPRS FDLAQKRIYA LMEKDSLPRF VRSEFYKELI
K
