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RGS9_BOVIN
ID   RGS9_BOVIN              Reviewed;         484 AA.
AC   O46469;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 158.
DE   RecName: Full=Regulator of G-protein signaling 9;
DE            Short=RGS9;
GN   Name=RGS9;
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   INTERACTION WITH GNB5.
RX   PubMed=10051575; DOI=10.1073/pnas.96.5.1947;
RA   Makino E.R., Handy J.W., Li T., Arshavsky V.Y.;
RT   "The GTPase activating factor for transducin in rod photoreceptors is the
RT   complex between RGS9 and type 5 G protein beta subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1947-1952(1999).
RN   [3]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=12119397; DOI=10.1073/pnas.152094799;
RA   Hu G., Wensel T.G.;
RT   "R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein,
RT   RGS9-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9755-9760(2002).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 276-422 IN COMPLEX WITH PDE6G AND
RP   GNAT1.
RX   PubMed=11234020; DOI=10.1038/35059138;
RA   Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B.;
RT   "Structural determinants for regulation of phosphodiesterase by a G protein
RT   at 2.0 A.";
RL   Nature 409:1071-1077(2001).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into their
CC       inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction;
CC       key element in the recovery phase of visual transduction.
CC   -!- SUBUNIT: Heterodimer with GNB5. Interacts with RGS7BP, leading to
CC       regulate the subcellular location of the heterodimer formed with GNB5.
CC       Component of the RGS9-1-Gbeta5 complex composed of RGS9 (RGS9-1),
CC       Gbeta5 (GNB5) and RGS9BP (Probable). Interacts with PDE6G and GNAT1
CC       (PubMed:11234020). {ECO:0000269|PubMed:11234020,
CC       ECO:0000305|PubMed:10051575, ECO:0000305|PubMed:12119397}.
CC   -!- INTERACTION:
CC       O46469; A5PJS1: GNB5; NbExp=5; IntAct=EBI-6949890, EBI-6949917;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Note=Targeted to the membrane via its interaction with RGS9BP.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Photoreceptor outer segments.
CC   -!- PTM: Phosphorylation is decreased by light exposition.
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DR   EMBL; AF011357; AAC99480.1; -; mRNA.
DR   RefSeq; NP_776595.1; NM_174170.2.
DR   PDB; 1FQI; X-ray; 1.94 A; A=276-422.
DR   PDB; 1FQJ; X-ray; 2.02 A; B/E=276-422.
DR   PDB; 1FQK; X-ray; 2.30 A; B/D=276-422.
DR   PDBsum; 1FQI; -.
DR   PDBsum; 1FQJ; -.
DR   PDBsum; 1FQK; -.
DR   AlphaFoldDB; O46469; -.
DR   SMR; O46469; -.
DR   CORUM; O46469; -.
DR   IntAct; O46469; 2.
DR   MINT; O46469; -.
DR   STRING; 9913.ENSBTAP00000023605; -.
DR   iPTMnet; O46469; -.
DR   PaxDb; O46469; -.
DR   GeneID; 281453; -.
DR   KEGG; bta:281453; -.
DR   CTD; 8787; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   InParanoid; O46469; -.
DR   OrthoDB; 415625at2759; -.
DR   EvolutionaryTrace; O46469; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.167.10; -; 1.
DR   Gene3D; 4.10.260.10; -; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR040759; RGS_DHEX.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   Pfam; PF18148; RGS_DHEX; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48097; SSF48097; 1.
DR   SUPFAM; SSF48670; SSF48670; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Phosphoprotein; Reference proteome;
KW   Sensory transduction; Signal transduction inhibitor; Vision.
FT   CHAIN           1..484
FT                   /note="Regulator of G-protein signaling 9"
FT                   /id="PRO_0000204202"
FT   DOMAIN          30..105
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   DOMAIN          219..280
FT                   /note="G protein gamma"
FT   DOMAIN          299..414
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          460..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:1FQJ"
FT   HELIX           290..295
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   TURN            296..298
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           300..304
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           307..319
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           324..336
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           340..342
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           343..354
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           367..376
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   TURN            382..385
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           386..399
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           401..405
FT                   /evidence="ECO:0007829|PDB:1FQI"
FT   HELIX           408..416
FT                   /evidence="ECO:0007829|PDB:1FQI"
SQ   SEQUENCE   484 AA;  56680 MW;  3D8C61CEC1E22949 CRC64;
     MTIRHQGQQY RPRMAFLRKI EALVKDMQDP DTGVRVQNQK VKVVSIPHAM TGSDVLQWIS
     QRLWISGLEA QNLGNFIVKY GYIYPLQDPR NLTLKPDSSL YRFQTPYFWP TQQWPAEDVD
     YAIYLAKRNI KKKGILEEYE KENYNFLNKK INYKWDFVIM QAREQYRAGK ERNKVDRCAL
     DCQEKAYWLV HRCPPGANNV LDYGLDRVTN PNEDQKQTVV SVRKEIMYYR QALMRSTVKS
     SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVDIPTK MRVERWAFNF
     SELIRDPKGR QSFQHFLRKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR
     RWINIDGKTM DITVKGLKHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP
     QGTTRKSSSL PFMRRHLRSS PSPVILRQLE EEAKAREAAT TVDITQVMSK LDRRSQLRKE
     PPPK
 
 
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