ID   RGS10_RAT               Reviewed;         181 AA.
AC   P49806; G3V8Q0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Regulator of G-protein signaling 10;
DE            Short=RGS10;
GN   Name=Rgs10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 72-137.
RC   TISSUE=Brain;
RX   PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA   Koelle M.R., Horvitz H.R.;
RT   "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT   shares a conserved domain with many mammalian proteins.";
RL   Cell 84:115-125(1996).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; AABR07005782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07005783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07071989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473956; EDM17179.1; -; Genomic_DNA.
DR   EMBL; U32437; AAC52374.1; -; mRNA.
DR   AlphaFoldDB; P49806; -.
DR   SMR; P49806; -.
DR   STRING; 10116.ENSRNOP00000027375; -.
DR   PhosphoSitePlus; P49806; -.
DR   PaxDb; 10116-ENSRNOP00000027375; -.
DR   Ensembl; ENSRNOT00000027375.6; ENSRNOP00000027375.4; ENSRNOG00000042592.3.
DR   Ensembl; ENSRNOT00055047219; ENSRNOP00055038829; ENSRNOG00055027267.
DR   Ensembl; ENSRNOT00060046538; ENSRNOP00060038692; ENSRNOG00060026852.
DR   Ensembl; ENSRNOT00065026516; ENSRNOP00065020798; ENSRNOG00065015957.
DR   UCSC; RGD:3562; rat.
DR   AGR; RGD:3562; -.
DR   RGD; 3562; Rgs10.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000161426; -.
DR   InParanoid; P49806; -.
DR   OMA; ANEIYMT; -.
DR   TreeFam; TF315837; -.
DR   PRO; PR:P49806; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Proteomes; UP000234681; Chromosome 1.
DR   Bgee; ENSRNOG00000042592; Expressed in thymus and 20 other cell types or tissues.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:RGD.
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; TAS:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
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.
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_0000204209"
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          157..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   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43665"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQE5"
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"
SQ   SEQUENCE   181 AA;  21176 MW;  E07F38C75B3A5DAE CRC64;
     MFTRAVSRLS RKRPPSDIHD GDGSSSSGHQ SLKSTAKWAS SLENLLEDPE GVKRFREFLK
     KEFSEENVLF WLACEDFKKT EDKKQMQEKA KKIYMTFLSN KASSQVNVEG QSRLTEKILE
     EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKHRRTEE EEEDPPDAQT AAKRASRIYN
     T
//