RGS9_MOUSE
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 03-AUG-2022, entry version 172.
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; 4.
DR DIP; DIP-46389N; -.
DR IntAct; O54828; 5.
DR STRING; 10090.ENSMUSP00000020920; -.
DR iPTMnet; O54828; -.
DR PhosphoSitePlus; O54828; -.
DR SwissPalm; O54828; -.
DR PaxDb; O54828; -.
DR PRIDE; O54828; -.
DR ProteomicsDB; 255196; -. [O54828-1]
DR ProteomicsDB; 255197; -. [O54828-2]
DR Antibodypedia; 9570; 170 antibodies from 29 providers.
DR DNASU; 19739; -.
DR Ensembl; ENSMUST00000020920; ENSMUSP00000020920; ENSMUSG00000020599. [O54828-1]
DR Ensembl; ENSMUST00000106706; ENSMUSP00000102317; ENSMUSG00000020599. [O54828-2]
DR GeneID; 19739; -.
DR KEGG; mmu:19739; -.
DR UCSC; uc007mbx.1; mouse. [O54828-1]
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; TNVDITQ; -.
DR OrthoDB; 415625at2759; -.
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 75 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 109 other tissues.
DR ExpressionAtlas; O54828; baseline and differential.
DR Genevisible; O54828; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density 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:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISO:MGI.
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; 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; 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
