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Database: UniProt
Entry: P97428
LinkDB: P97428
Original site: P97428 
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   07-APR-2021, entry version 164.
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}.
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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   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; 334 antibodies.
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   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000154304; -.
DR   HOGENOM; CLU_059863_3_0_1; -.
DR   InParanoid; P97428; -.
DR   OMA; MCRTLAT; -.
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; 0 hits in 52 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 276 other tissues.
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; 1.10.196.10; -; 2.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
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   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:0007744|PDB:3C7L"
FT   HELIX           65..68
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           72..83
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   TURN            84..86
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           88..100
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           106..120
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           133..144
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   TURN            148..151
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           152..163
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           166..171
FT                   /evidence="ECO:0007744|PDB:3C7L"
FT   HELIX           174..177
FT                   /evidence="ECO:0007744|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
//
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