RGS10_MOUSE
ID RGS10_MOUSE Reviewed; 181 AA.
AC Q9CQE5; Q9D3L2;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Regulator of G-protein signaling 10;
DE Short=RGS10;
GN Name=Rgs10;
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=Head, Thymus, and Tongue;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Spleen, and Testis;
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 downstream of the muscarinic acetylcholine receptor
CC CHRM2. Inhibits signal transduction by increasing the GTPase activity
CC of G protein alpha subunits, thereby driving them into their inactive
CC GDP-bound form. Modulates the activity of potassium channels that are
CC activated in response to CHRM2 signaling. Activity on GNAZ is inhibited
CC by palmitoylation of the G-protein. {ECO:0000250|UniProtKB:O43665}.
CC -!- SUBUNIT: Interacts with GNAZ, GNAI1 and GNAI3. Associates specifically
CC with the activated, GTP-bound forms of GNAZ and GNAI3.
CC {ECO:0000250|UniProtKB:O43665}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O43665}. Nucleus {ECO:0000250|UniProtKB:O43665}.
CC Note=Forskolin treatment promotes phosphorylation and translocation to
CC the nucleus. {ECO:0000250|UniProtKB:O43665}.
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DR EMBL; AK009686; BAB26440.1; -; mRNA.
DR EMBL; AK009283; BAB26193.1; -; mRNA.
DR EMBL; AK017314; BAB30688.1; -; mRNA.
DR EMBL; AK088009; BAC40091.1; -; mRNA.
DR CCDS; CCDS21896.1; -.
DR RefSeq; NP_080694.1; NM_026418.2.
DR AlphaFoldDB; Q9CQE5; -.
DR SMR; Q9CQE5; -.
DR BioGRID; 212492; 5.
DR STRING; 10090.ENSMUSP00000033133; -.
DR iPTMnet; Q9CQE5; -.
DR PhosphoSitePlus; Q9CQE5; -.
DR EPD; Q9CQE5; -.
DR MaxQB; Q9CQE5; -.
DR PaxDb; Q9CQE5; -.
DR PRIDE; Q9CQE5; -.
DR ProteomicsDB; 254949; -.
DR Antibodypedia; 3878; 225 antibodies from 31 providers.
DR DNASU; 67865; -.
DR Ensembl; ENSMUST00000033133; ENSMUSP00000033133; ENSMUSG00000030844.
DR GeneID; 67865; -.
DR KEGG; mmu:67865; -.
DR UCSC; uc009jyw.1; mouse.
DR CTD; 6001; -.
DR MGI; MGI:1915115; Rgs10.
DR VEuPathDB; HostDB:ENSMUSG00000030844; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161426; -.
DR HOGENOM; CLU_059863_1_4_1; -.
DR InParanoid; Q9CQE5; -.
DR OMA; HKKCEEQ; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; Q9CQE5; -.
DR TreeFam; TF315837; -.
DR BioGRID-ORCS; 67865; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Rgs10; mouse.
DR PRO; PR:Q9CQE5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CQE5; protein.
DR Bgee; ENSMUSG00000030844; Expressed in blood and 246 other tissues.
DR ExpressionAtlas; Q9CQE5; baseline and differential.
DR Genevisible; Q9CQE5; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR CDD; cd08741; RGS_RGS10; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR037879; RGS10_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
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; GTPase activation; Lipoprotein; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..181
FT /note="Regulator of G-protein signaling 10"
FT /id="PRO_0000204208"
FT DOMAIN 41..156
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43665"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43665"
FT LIPID 74
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O43665"
FT CONFLICT 73
FT /note="A -> E (in Ref. 1; BAB30688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 21151 MW; 9897860505962286 CRC64;
MFTRAVSRLS RKRPPSDIHD GDGSSSSGHQ SLKSTAKWAS SLENLLEDPE GVQRFREFLK
KEFSEENVLF WLACEDFKKT EDRKQMQEKA KEIYMTFLSN KASSQVNVEG QSRLTEKILE
EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKPKRTEE EEEEPPDAQT AAKRASRIYN
T
