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   27-MAR-2024, entry version 155.
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; 10090-ENSMUSP00000033133; -.
DR   ProteomicsDB; 254949; -.
DR   Pumba; Q9CQE5; -.
DR   Antibodypedia; 3878; 264 antibodies from 31 providers.
DR   DNASU; 67865; -.
DR   Ensembl; ENSMUST00000033133.12; ENSMUSP00000033133.6; ENSMUSG00000030844.12.
DR   GeneID; 67865; -.
DR   KEGG; mmu:67865; -.
DR   UCSC; uc009jyw.1; mouse.
DR   AGR; MGI:1915115; -.
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; ANEIYMT; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; Q9CQE5; -.
DR   TreeFam; TF315837; -.
DR   BioGRID-ORCS; 67865; 1 hit in 76 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 249 other cell types or tissues.
DR   ExpressionAtlas; Q9CQE5; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
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:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IEA:InterPro.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   CDD; cd08741; RGS_RGS10; 1.
DR   Gene3D; 1.10.196.10; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR046995; RGS10/12/14-like.
DR   InterPro; IPR037879; RGS10_RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR45945; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR   PANTHER; PTHR45945:SF3; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; Q9CQE5; MM.
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
//