RGS16_MOUSE
ID RGS16_MOUSE Reviewed; 201 AA.
AC P97428; O09091; P97420; Q80V16;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Regulator of G-protein signaling 16;
DE Short=RGS16;
DE AltName: Full=A28-RGS14P;
DE AltName: Full=Retinal-specific RGS;
DE Short=RGS-r {ECO:0000303|PubMed:8917514};
DE AltName: Full=Retinally abundant regulator of G-protein signaling;
GN Name=Rgs16; Synonyms=Rgsr;
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 [MRNA], AND FUNCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH GNAI3; GNAO1 AND
RP GNAI2.
RC TISSUE=Pituitary;
RX PubMed=9079700; DOI=10.1074/jbc.272.13.8679;
RA Chen C., Zheng B., Han J., Lin S.-C.;
RT "Characterization of a novel mammalian RGS protein that binds to Galpha
RT proteins and inhibits pheromone signaling in yeast.";
RL J. Biol. Chem. 272:8679-8685(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9223279; DOI=10.1073/pnas.94.15.7868;
RA Buckbinder L., Velasco-Miguel S., Chen Y., Xu N., Talbott R., Gelbert L.,
RA Gao J., Seizinger B.R., Gutkind J.S., Kley N.;
RT "The p53 tumor suppressor targets a novel regulator of G protein
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7868-7872(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=9469939; DOI=10.1016/s0378-1119(97)00593-3;
RA Snow B.E., Antonio L., Suggs S., Siderovski D.P.;
RT "Cloning of a retinally abundant regulator of G-protein signaling (RGS-
RT r/RGS16): genomic structure and chromosomal localization of the human
RT gene.";
RL Gene 206:247-253(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PALMITOYLATION AT CYS-2 AND CYS-12, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10373502; DOI=10.1074/jbc.274.26.18836;
RA Druey K.M., Ugur O., Caron J.M., Chen C.-K., Backlund P.S., Jones T.L.Z.;
RT "Amino-terminal cysteine residues of RGS16 are required for palmitoylation
RT and modulation of Gi- and Gq-mediated signaling.";
RL J. Biol. Chem. 274:18836-18842(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 53-180 IN COMPLEX WITH GNAO1, AND
RP INTERACTION WITH GNAO1.
RX PubMed=18434540; DOI=10.1073/pnas.0801569105;
RA Slep K.C., Kercher M.A., Wieland T., Chen C.K., Simon M.I., Sigler P.B.;
RT "Molecular architecture of Galphao and the structural basis for RGS16-
RT mediated deactivation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6243-6248(2008).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades
CC (PubMed:9079700). Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits, thereby driving them into their
CC inactive GDP-bound form (PubMed:10373502). Plays an important role in
CC the phototransduction cascade by regulating the lifetime and effective
CC concentration of activated transducin alpha (PubMed:8917514). May
CC regulate extra and intracellular mitogenic signals.
CC {ECO:0000269|PubMed:10373502, ECO:0000269|PubMed:8917514, ECO:0000305}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with
CC GNAI3, GNAI3 and GNAO1 (PubMed:9079700, PubMed:18434540).
CC {ECO:0000250|UniProtKB:O15492, ECO:0000269|PubMed:18434540,
CC ECO:0000269|PubMed:9079700}.
CC -!- INTERACTION:
CC P97428; P18872-1: Gnao1; NbExp=2; IntAct=EBI-643424, EBI-1018790;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10373502}; Lipid-
CC anchor {ECO:0000269|PubMed:10373502}.
CC -!- TISSUE SPECIFICITY: Retinal; also predominantly expressed in the liver
CC and pituitary.
CC -!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
CC {ECO:0000269|PubMed:10373502}.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-167 by EGFR enhances GTPase
CC accelerating (GAP) activity toward GNAI1.
CC {ECO:0000250|UniProtKB:O15492}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U72881; AAC52927.1; -; mRNA.
DR EMBL; U67189; AAB50619.1; -; mRNA.
DR EMBL; U70427; AAC16913.1; -; Genomic_DNA.
DR EMBL; U94828; AAC53549.1; -; mRNA.
DR EMBL; BC010980; AAH10980.1; -; mRNA.
DR EMBL; BC049968; AAH49968.2; -; mRNA.
DR CCDS; CCDS15376.1; -.
DR RefSeq; NP_035397.2; NM_011267.3.
DR PDB; 3C7K; X-ray; 2.90 A; B/D=53-180.
DR PDB; 3C7L; X-ray; 1.89 A; A/B=53-180.
DR PDBsum; 3C7K; -.
DR PDBsum; 3C7L; -.
DR AlphaFoldDB; P97428; -.
DR SMR; P97428; -.
DR DIP; DIP-29922N; -.
DR ELM; P97428; -.
DR IntAct; P97428; 2.
DR STRING; 10090.ENSMUSP00000027748; -.
DR iPTMnet; P97428; -.
DR PhosphoSitePlus; P97428; -.
DR SwissPalm; P97428; -.
DR PaxDb; P97428; -.
DR PRIDE; P97428; -.
DR ProteomicsDB; 254952; -.
DR Antibodypedia; 34439; 360 antibodies from 25 providers.
DR DNASU; 19734; -.
DR Ensembl; ENSMUST00000027748; ENSMUSP00000027748; ENSMUSG00000026475.
DR GeneID; 19734; -.
DR KEGG; mmu:19734; -.
DR UCSC; uc007dae.2; mouse.
DR CTD; 6004; -.
DR MGI; MGI:108407; Rgs16.
DR VEuPathDB; HostDB:ENSMUSG00000026475; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154304; -.
DR HOGENOM; CLU_059863_3_0_1; -.
DR InParanoid; P97428; -.
DR OMA; KSPAYQD; -.
DR OrthoDB; 1296189at2759; -.
DR PhylomeDB; P97428; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR BioGRID-ORCS; 19734; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rgs16; mouse.
DR EvolutionaryTrace; P97428; -.
DR PRO; PR:P97428; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97428; protein.
DR Bgee; ENSMUSG00000026475; Expressed in medial geniculate body and 216 other tissues.
DR ExpressionAtlas; P97428; baseline and differential.
DR Genevisible; P97428; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA: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 1: Evidence at protein level;
KW 3D-structure; GTPase activation; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..201
FT /note="Regulator of G-protein signaling 16"
FT /id="PRO_0000204222"
FT DOMAIN 64..180
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 181..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphotyrosine; by EGFR"
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:0000305|PubMed:10373502"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10373502"
FT CONFLICT 51
FT /note="E -> EN (in Ref. 3; AAC16913)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="H -> Q (in Ref. 3; AAC16913)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="D -> E (in Ref. 3; AAC16913)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> V (in Ref. 3; AAC16913)"
FT /evidence="ECO:0000305"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3C7L"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:3C7L"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3C7L"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:3C7L"
SQ SEQUENCE 201 AA; 22691 MW; AE3D798F15787392 CRC64;
MCRTLATFPN TCLERAKEFK TRLGIFLHKS ELSSDTGGIS KFEWASKHNK ERSFSEDVLG
WRESFDLLLN SKNGVAAFHA FLKTEFSEEN LEFWLACEEF KKIRSATKLA SRAHHIFDEY
IRSEAPKEVN IDHETRELTK TNLQAATTSC FDVAQGKTRT LMEKDSYPRF LKSPAYRDLA
AQASATSTSA PSGSPAEPSH T
