ID   RGS16_RAT               Reviewed;         199 AA.
AC   P56700;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
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; Synonyms=Rgsr;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=8917514; DOI=10.1073/pnas.93.23.12885;
RA   Chen C.-K., Wieland T., Simon M.I.;
RT   "RGS-r, a retinal specific RGS protein, binds an intermediate conformation
RT   of transducin and enhances recycling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12885-12889(1996).
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   -!- TISSUE SPECIFICITY: Predominantly found in the retina. Some expression
CC       has been found in the liver. {ECO:0000269|PubMed:8917514}.
CC   -!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
CC       {ECO:0000250|UniProtKB:P97428}.
CC   -!- PTM: Phosphorylated. Phosphorylation at Tyr-167 by EGFR enhances GTPase
CC       accelerating (GAP) activity toward GNAI1.
CC       {ECO:0000250|UniProtKB:O15492}.
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DR   AlphaFoldDB; P56700; -.
DR   SMR; P56700; -.
DR   STRING; 10116.ENSRNOP00000029844; -.
DR   PaxDb; P56700; -.
DR   UCSC; RGD:1589741; rat.
DR   RGD; 1589741; Rgs16.
DR   eggNOG; KOG3589; Eukaryota.
DR   InParanoid; P56700; -.
DR   PhylomeDB; P56700; -.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-418597; G alpha (z) signalling events.
DR   PRO; PR:P56700; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:RGD.
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..199
FT                   /note="Regulator of G-protein signaling 16"
FT                   /id="PRO_0000204223"
FT   DOMAIN          64..180
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   MOD_RES         167
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O15492"
FT   MOD_RES         176
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   199 AA;  22400 MW;  3C5A51E83F3956CC CRC64;
     MCRTIATFPN TCLERAKEFK TRLGIFLHKS ELSSDTGGNG KFEWASKLSK ERSFSEDVLG
     WRESFQSLLN SKNGVAAFHA FLKTEFSEEN LEFWLACEEF KKIRSATKLA SRAHHIFDEY
     IRSEAPKEVN IDHETRELTK TNLQAATTSC FDVAQGKTRT LMEKDSYPRF LKSPAYRDLA
     AQASATSASG SSPAEPSHT