ID   RGS16_BOVIN             Reviewed;         202 AA.
AC   O46471; Q08E37;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Regulator of G-protein signaling 16;
DE            Short=RGS16;
DE   AltName: Full=Retinal-specific RGS;
DE            Short=RGS-r;
DE   AltName: Full=Retinally abundant regulator of G-protein signaling;
GN   Name=RGS16;
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 [MRNA].
RX   PubMed=9459445; DOI=10.1016/s0896-6273(00)80437-7;
RA   He W., Cowan C.W., Wensel T.G.;
RT   "RGS9, a GTPase accelerator for phototransduction.";
RL   Neuron 20:95-102(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC       Inhibits signal transduction by increasing the GTPase activity of G
CC       protein alpha subunits, thereby driving them into their inactive GDP-
CC       bound form. Plays an important role in the phototransduction cascade by
CC       regulating the lifetime and effective concentration of activated
CC       transducin alpha. May regulate extra and intracellular mitogenic
CC       signals. {ECO:0000250|UniProtKB:P97428}.
CC   -!- SUBUNIT: Interacts with GNAI1 and GNAQ. Interacts with GNAI3, GNAI3 and
CC       GNAO1. {ECO:0000250|UniProtKB:O15492, ECO:0000250|UniProtKB:P97428}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P97428}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P97428}.
CC   -!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
CC       {ECO:0000250|UniProtKB:P97428}.
CC   -!- PTM: Phosphorylated. Phosphorylation at Tyr-168 by EGFR enhances GTPase
CC       accelerating (GAP) activity toward GNAI1.
CC       {ECO:0000250|UniProtKB:O15492}.
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DR   EMBL; AF011361; AAC99484.1; -; mRNA.
DR   EMBL; BC123439; AAI23440.1; -; mRNA.
DR   RefSeq; NP_776875.1; NM_174450.3.
DR   AlphaFoldDB; O46471; -.
DR   SMR; O46471; -.
DR   STRING; 9913.ENSBTAP00000005642; -.
DR   PaxDb; O46471; -.
DR   PRIDE; O46471; -.
DR   Ensembl; ENSBTAT00000005642; ENSBTAP00000005642; ENSBTAG00000004305.
DR   GeneID; 282035; -.
DR   KEGG; bta:282035; -.
DR   CTD; 6004; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004305; -.
DR   VGNC; VGNC:33915; RGS16.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000154304; -.
DR   HOGENOM; CLU_059863_3_0_1; -.
DR   InParanoid; O46471; -.
DR   OMA; KSPAYQD; -.
DR   OrthoDB; 1296189at2759; -.
DR   TreeFam; TF315837; -.
DR   Reactome; R-BTA-416476; G alpha (q) signalling events.
DR   Reactome; R-BTA-418594; G alpha (i) signalling events.
DR   Reactome; R-BTA-418597; G alpha (z) signalling events.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000004305; Expressed in ureter and 98 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled 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   Gene3D; 1.10.167.10; -; 1.
DR   Gene3D; 1.10.196.10; -; 1.
DR   InterPro; IPR016137; 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   2: Evidence at transcript level;
KW   GTPase activation; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..202
FT                   /note="Regulator of G-protein signaling 16"
FT                   /id="PRO_0000204220"
FT   DOMAIN          65..181
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          183..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         168
FT                   /note="Phosphotyrosine; by EGFR"
FT                   /evidence="ECO:0000250|UniProtKB:O15492"
FT   MOD_RES         177
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O15492"
FT   LIPID           2
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P97428"
FT   LIPID           12
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P97428"
SQ   SEQUENCE   202 AA;  22636 MW;  F8DC44F49DD1C6B6 CRC64;
     MCRTLAAFPT SCLERAKEFK TRLGIFLHKS ELGSDTGSVG KFEWGSKHSK EGKNFSEDVL
     GWKESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKLRSATKL GSRAHRIFEE
     FICSEAPKEV NIDHETRELT RTNLQAATAV CFDAAQWKVR ALMEKDSYPR FLKSPAYRDL
     ATQATAASAS PSSSSPAEPL HT