ID   RGS10_BOVIN             Reviewed;         181 AA.
AC   Q2KHW7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Regulator of G-protein signaling 10;
DE            Short=RGS10;
GN   Name=RGS10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC112856; AAI12857.1; -; mRNA.
DR   RefSeq; NP_001040005.1; NM_001046540.2.
DR   AlphaFoldDB; Q2KHW7; -.
DR   SMR; Q2KHW7; -.
DR   STRING; 9913.ENSBTAP00000061827; -.
DR   PaxDb; 9913-ENSBTAP00000003425; -.
DR   Ensembl; ENSBTAT00000003425.4; ENSBTAP00000003425.3; ENSBTAG00000002647.4.
DR   GeneID; 614550; -.
DR   KEGG; bta:614550; -.
DR   CTD; 6001; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002647; -.
DR   VGNC; VGNC:33911; RGS10.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000161426; -.
DR   HOGENOM; CLU_059863_1_4_1; -.
DR   InParanoid; Q2KHW7; -.
DR   OMA; ANEIYMT; -.
DR   TreeFam; TF315837; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000002647; Expressed in oocyte and 100 other cell types or tissues.
DR   ExpressionAtlas; Q2KHW7; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:InterPro.
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   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   2: Evidence at transcript 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_0000244459"
FT   DOMAIN          41..156
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          1..40
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..40
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;  21195 MW;  F722EFB8EFFE9801 CRC64;
     MFNRAVSRLS RKRPPSDIHD SDGSSSSSHQ TPKSTAKWAS SLENLLEDPE GVKRFREFLK
     KEFSEENVLF WLACEDFKKT QDKKQMQEKA KEIYMTFLSS KASSQVNVEG QSRLNEKILE
     EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKHKRTEE EDEESPDAQT AAKRASRIYN
     T
//