ID   RGS9_MOUSE              Reviewed;         675 AA.
AC   O54828; A1L352; Q9Z0S0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Regulator of G-protein signaling 9;
DE            Short=RGS9;
GN   Name=Rgs9;
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] (ISOFORM 1).
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 [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Forebrain;
RX   PubMed=10066255; DOI=10.1523/jneurosci.19-06-02016.1999;
RA   Rahman Z., Gold S.J., Potenza M.N., Cowan C.W., Ni Y.G., He W.,
RA   Wensel T.G., Nestler E.J.;
RT   "Cloning and characterization of RGS9-2: a striatal-enriched alternatively
RT   spliced product of the RGS9 gene.";
RL   J. Neurosci. 19:2016-2026(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   PHOSPHORYLATION OF ISOFORM 1.
RX   PubMed=11292825; DOI=10.1074/jbc.m011539200;
RA   Hu G., Jang G.F., Cowan C.W., Wensel T.G., Palczewski K.;
RT   "Phosphorylation of RGS9-1 by an endogenous protein kinase in rod outer
RT   segments.";
RL   J. Biol. Chem. 276:22287-22295(2001).
RN   [7]
RP   INTERACTION WITH RGS9BP.
RC   STRAIN=C57BL/6 X 129; TISSUE=Retina;
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   [8]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=12499365; DOI=10.1074/jbc.m211782200;
RA   Sokal I., Hu G., Liang Y., Mao M., Wensel T.G., Palczewski K.;
RT   "Identification of protein kinase C isozymes responsible for the
RT   phosphorylation of photoreceptor-specific RGS9-1 at Ser475.";
RL   J. Biol. Chem. 278:8316-8325(2003).
RN   [9]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=14614075; DOI=10.1523/jneurosci.23-32-10175.2003;
RA   Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M.,
RA   Strissel K.J., Leskov I.B., Hopp J.A., Kolesnikov A.V., Chen C.-K., Lem J.,
RA   Heller S., Burns M.E., Arshavsky V.Y.;
RT   "The DEP domain determines subcellular targeting of the GTPase activating
RT   protein RGS9 in vivo.";
RL   J. Neurosci. 23:10175-10181(2003).
RN   [10]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15632198; DOI=10.1074/jbc.c400596200;
RA   Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT   "R7BP, a novel neuronal protein interacting with RGS proteins of the R7
RT   family.";
RL   J. Biol. Chem. 280:5133-5136(2005).
RN   [11]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15897264; DOI=10.1083/jcb.200502007;
RA   Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA   Linder M.E., Blumer K.J.;
RT   "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT   novel membrane anchor for the RGS7 family.";
RL   J. Cell Biol. 169:623-633(2005).
RN   [12]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=16908407; DOI=10.1016/j.neuron.2006.07.010;
RA   Krispel C.M., Chen D., Melling N., Chen Y.-J., Martemyanov K.A.,
RA   Quillinan N., Arshavsky V.Y., Wensel T.G., Chen C.-K., Burns M.E.;
RT   "RGS expression rate-limits recovery of rod photoresponses.";
RL   Neuron 51:409-416(2006).
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       (PubMed:15632198, PubMed:15897264). Component of the RGS9-1-Gbeta5
CC       complex composed of RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP
CC       (PubMed:12119397, PubMed:12499365, PubMed:14614075, PubMed:16908407).
CC       Interacts with PDE6G and GNAT1 (By similarity).
CC       {ECO:0000250|UniProtKB:O46469, ECO:0000305|PubMed:12119397,
CC       ECO:0000305|PubMed:12499365, ECO:0000305|PubMed:14614075,
CC       ECO:0000305|PubMed:15632198, ECO:0000305|PubMed:15897264,
CC       ECO:0000305|PubMed:16908407}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Peripheral membrane
CC       protein. Note=Isoform 1 is targeted to the membrane via its interaction
CC       with RGS9BP.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=RGS9-2;
CC         IsoId=O54828-1; Sequence=Displayed;
CC       Name=1; Synonyms=RGS9-1;
CC         IsoId=O54828-2; Sequence=VSP_005678, VSP_005679;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in photoreceptor outer
CC       segments. Isoform 2 is expressed in brain striatum.
CC   -!- PTM: Retinal isoform 1 is light-dependent phosphorylated at 'Ser-475'.
CC       Phosphorylation is decreased by light exposition. Interaction with
CC       RGS9BP is decreased when isoform 1 is phosphorylated at 'Ser-475'.
CC       {ECO:0000269|PubMed:11292825}.
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DR   EMBL; AF011358; AAC99481.1; -; mRNA.
DR   EMBL; AF125046; AAD20014.1; -; mRNA.
DR   EMBL; AL604043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466558; EDL34351.1; -; Genomic_DNA.
DR   EMBL; BC129899; AAI29900.1; -; mRNA.
DR   CCDS; CCDS25576.1; -. [O54828-1]
DR   CCDS; CCDS48969.1; -. [O54828-2]
DR   RefSeq; NP_035398.2; NM_011268.2. [O54828-1]
DR   PDB; 2PBI; X-ray; 1.95 A; A/C=1-422.
DR   PDBsum; 2PBI; -.
DR   AlphaFoldDB; O54828; -.
DR   SMR; O54828; -.
DR   BioGRID; 202886; 5.
DR   DIP; DIP-46389N; -.
DR   IntAct; O54828; 5.
DR   STRING; 10090.ENSMUSP00000020920; -.
DR   GlyGen; O54828; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O54828; -.
DR   PhosphoSitePlus; O54828; -.
DR   SwissPalm; O54828; -.
DR   PaxDb; 10090-ENSMUSP00000020920; -.
DR   ProteomicsDB; 255196; -. [O54828-1]
DR   ProteomicsDB; 255197; -. [O54828-2]
DR   Antibodypedia; 9570; 183 antibodies from 29 providers.
DR   DNASU; 19739; -.
DR   Ensembl; ENSMUST00000020920.10; ENSMUSP00000020920.4; ENSMUSG00000020599.14. [O54828-1]
DR   Ensembl; ENSMUST00000106706.8; ENSMUSP00000102317.2; ENSMUSG00000020599.14. [O54828-2]
DR   GeneID; 19739; -.
DR   KEGG; mmu:19739; -.
DR   UCSC; uc007mbx.1; mouse. [O54828-1]
DR   AGR; MGI:1338824; -.
DR   CTD; 8787; -.
DR   MGI; MGI:1338824; Rgs9.
DR   VEuPathDB; HostDB:ENSMUSG00000020599; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000156505; -.
DR   HOGENOM; CLU_025092_5_0_1; -.
DR   InParanoid; O54828; -.
DR   OMA; PRMACLR; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; O54828; -.
DR   TreeFam; TF351956; -.
DR   Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 19739; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; Rgs9; mouse.
DR   EvolutionaryTrace; O54828; -.
DR   PRO; PR:O54828; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O54828; Protein.
DR   Bgee; ENSMUSG00000020599; Expressed in retinal neural layer and 111 other cell types or tissues.
DR   ExpressionAtlas; O54828; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR   GO; GO:1990603; P:dark adaptation; IDA:MGI.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0036367; P:light adaption; IDA:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:1905912; P:regulation of calcium ion export across plasma membrane; ISO:MGI.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd04450; DEP_RGS7-like; 1.
DR   CDD; cd00068; GGL; 1.
DR   CDD; cd08739; RGS_RGS9; 1.
DR   Gene3D; 1.10.1240.60; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR047016; RGS6/7/9/11.
DR   InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR   InterPro; IPR047077; RGS9_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   PANTHER; PTHR45746; LP21163P; 1.
DR   PANTHER; PTHR45746:SF1; REGULATOR OF G-PROTEIN SIGNALING 9; 1.
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; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; O54828; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Membrane; Phosphoprotein;
KW   Reference proteome; Sensory transduction; Signal transduction inhibitor;
KW   Vision.
FT   CHAIN           1..675
FT                   /note="Regulator of G-protein signaling 9"
FT                   /id="PRO_0000204204"
FT   DOMAIN          30..105
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   DOMAIN          222..283
FT                   /note="G protein gamma"
FT   DOMAIN          299..414
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          524..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         467..484
FT                   /note="PGQHLAPSPHLAVYTGTC -> VMSKLDRRSQLKKELPPK (in isoform
FT                   1)"
FT                   /evidence="ECO:0000303|PubMed:9459445"
FT                   /id="VSP_005678"
FT   VAR_SEQ         485..675
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:9459445"
FT                   /id="VSP_005679"
FT   CONFLICT        76
FT                   /note="F -> L (in Ref. 1; AAC99481 and 2; AAD20014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="Q -> R (in Ref. 1; AAC99481 and 2; AAD20014)"
FT                   /evidence="ECO:0000305"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           52..63
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           118..130
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           138..150
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           155..169
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           174..191
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           219..234
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           240..254
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           259..262
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           276..280
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           290..295
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   TURN            296..298
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           300..305
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           307..319
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           325..337
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   STRAND          340..342
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           343..354
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           367..376
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   TURN            382..385
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           386..398
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           400..405
FT                   /evidence="ECO:0007829|PDB:2PBI"
FT   HELIX           408..416
FT                   /evidence="ECO:0007829|PDB:2PBI"
SQ   SEQUENCE   675 AA;  76978 MW;  72F1652D7D59EB05 CRC64;
     MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM TGGDVLQWIT
     QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL YRFQTPYFWP TQQWPAEDTD
     YAIYLAKRNI KKKGILEEYE KENYDFLNKK INYKWDFVIM QAKEQYRTGK ERNKADRYAL
     DCQEKAYWLV HRSPPGMNNV LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS
     SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF
     SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR
     RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP
     QETTKRSSTL PFMRRHLRSS PSPVILRQLE EEEKAREAAN TVDITQPGQH LAPSPHLAVY
     TGTCVPPSPS SPFSPSCRSP RKPFASPSRF IRRPSIAICP SPSRVALEGS SGLEPKGEAS
     WSGANSGPSV TENREPSADH SRPQPRAPPK ARAALSLGRF LRRGCLASPV FARLSPKCPS
     VSHGKVQPLG DMGQQLPRLK PKKVANFFQI KMEMPTDSGT CLMDSDDPRA GESGDQTTEK
     EVICPWESLA EGKAG
//