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O54828

- RGS9_MOUSE

UniProt

O54828 - RGS9_MOUSE

Protein

Regulator of G-protein signaling 9

Gene

Rgs9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(t)-alpha. Involved in phototransduction; key element in the recovery phase of visual transduction.

    GO - Molecular functioni

    1. GTPase activator activity Source: RefGenome
    2. signal transducer activity Source: InterPro

    GO - Biological processi

    1. dopamine receptor signaling pathway Source: Ensembl
    2. G-protein coupled receptor signaling pathway Source: MGI
    3. intracellular signal transduction Source: InterPro
    4. nervous system development Source: Ensembl
    5. response to estrogen Source: Ensembl
    6. termination of G-protein coupled receptor signaling pathway Source: InterPro
    7. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Keywords - Biological processi

    Sensory transduction, Vision

    Enzyme and pathway databases

    ReactomeiREACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 9
    Short name:
    RGS9
    Gene namesi
    Name:Rgs9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1338824. Rgs9.

    Subcellular locationi

    Isoform 1 : Membrane; Peripheral membrane protein
    Note: Isoform 1 is targeted to the membrane via its interaction with RGS9BP.

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. heterotrimeric G-protein complex Source: InterPro
    3. nucleus Source: Ensembl
    4. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 675675Regulator of G-protein signaling 9PRO_0000204204Add
    BLAST

    Post-translational modificationi

    Retinal isoform 1 is light-dependent phosphorylated at 'Ser-475'. Phosphorylation is decreased by light exposition. Interaction with RGS9BP is decreased when isoform 1 is phosphorylated at 'Ser-475'.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO54828.
    PRIDEiO54828.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in photoreceptor outer segments. Isoform 2 is expressed in brain striatum.

    Gene expression databases

    ArrayExpressiO54828.
    BgeeiO54828.
    CleanExiMM_RGS9.
    GenevestigatoriO54828.

    Interactioni

    Subunit structurei

    Heterodimer with Gbeta5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5. Component of the RGS9-1-Gbeta5 complex composed of isoform 1 of RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP Probable.6 Publications

    Protein-protein interaction databases

    BioGridi202886. 1 interaction.
    DIPiDIP-46389N.
    IntActiO54828. 4 interactions.

    Structurei

    Secondary structure

    1
    675
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 2712
    Turni30 – 323
    Helixi52 – 6312
    Helixi67 – 7913
    Beta strandi82 – 887
    Beta strandi96 – 983
    Beta strandi100 – 1034
    Helixi106 – 1083
    Helixi118 – 13013
    Beta strandi132 – 1343
    Helixi138 – 15013
    Helixi152 – 1543
    Helixi155 – 16915
    Helixi174 – 19118
    Beta strandi207 – 2093
    Helixi219 – 23416
    Helixi240 – 25415
    Helixi255 – 2573
    Helixi259 – 2624
    Helixi269 – 2724
    Helixi276 – 2805
    Helixi290 – 2956
    Turni296 – 2983
    Helixi300 – 3056
    Helixi307 – 31913
    Helixi325 – 33713
    Beta strandi340 – 3423
    Helixi343 – 35412
    Helixi367 – 37610
    Turni382 – 3854
    Helixi386 – 39813
    Helixi400 – 4056
    Helixi408 – 4169

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PBIX-ray1.95A/C1-422[»]
    ProteinModelPortaliO54828.
    SMRiO54828. Positions 7-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO54828.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 10576DEPPROSITE-ProRule annotationAdd
    BLAST
    Domaini222 – 28362G protein gammaAdd
    BLAST
    Domaini299 – 414116RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 DEP domain.PROSITE-ProRule annotation
    Contains 1 G protein gamma domain.Curated
    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG327614.
    GeneTreeiENSGT00700000104259.
    HOGENOMiHOG000220864.
    HOVERGENiHBG007404.
    InParanoidiA1L352.
    KOiK13765.
    OMAiLVKDMQN.
    OrthoDBiEOG7BZVS5.
    TreeFamiTF351956.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.196.10. 1 hit.
    4.10.260.10. 1 hit.
    InterProiIPR000591. DEP_dom.
    IPR015898. G-protein_gamma-like_dom.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00610. DEP. 1 hit.
    PF00631. G-gamma. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view]
    PRINTSiPR01301. RGSPROTEIN.
    SMARTiSM00049. DEP. 1 hit.
    SM00224. GGL. 1 hit.
    SM00315. RGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    SSF48670. SSF48670. 1 hit.
    PROSITEiPS50186. DEP. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: O54828-1) [UniParc]FASTAAdd to Basket

    Also known as: RGS9-2

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM    50
    TGGDVLQWIT QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL 100
    YRFQTPYFWP TQQWPAEDTD YAIYLAKRNI KKKGILEEYE KENYDFLNKK 150
    INYKWDFVIM QAKEQYRTGK ERNKADRYAL DCQEKAYWLV HRSPPGMNNV 200
    LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS SVSLGGIVKY 250
    SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF 300
    SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI 350
    YKLFLAPGAR RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS 400
    YARYLKSPIY KEMLAKAIEP QETTKRSSTL PFMRRHLRSS PSPVILRQLE 450
    EEEKAREAAN TVDITQPGQH LAPSPHLAVY TGTCVPPSPS SPFSPSCRSP 500
    RKPFASPSRF IRRPSIAICP SPSRVALEGS SGLEPKGEAS WSGANSGPSV 550
    TENREPSADH SRPQPRAPPK ARAALSLGRF LRRGCLASPV FARLSPKCPS 600
    VSHGKVQPLG DMGQQLPRLK PKKVANFFQI KMEMPTDSGT CLMDSDDPRA 650
    GESGDQTTEK EVICPWESLA EGKAG 675
    Length:675
    Mass (Da):76,978
    Last modified:July 27, 2011 - v3
    Checksum:i72F1652D7D59EB05
    GO
    Isoform 1 (identifier: O54828-2) [UniParc]FASTAAdd to Basket

    Also known as: RGS9-1

    The sequence of this isoform differs from the canonical sequence as follows:
         467-484: PGQHLAPSPHLAVYTGTC → VMSKLDRRSQLKKELPPK
         485-675: Missing.

    Show »
    Length:484
    Mass (Da):56,940
    Checksum:i60B37878EBB4CD3C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761F → L in AAC99481. (PubMed:9459445)Curated
    Sequence conflicti76 – 761F → L in AAD20014. (PubMed:10066255)Curated
    Sequence conflicti161 – 1611Q → R in AAC99481. (PubMed:9459445)Curated
    Sequence conflicti161 – 1611Q → R in AAD20014. (PubMed:10066255)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei467 – 48418PGQHL…YTGTC → VMSKLDRRSQLKKELPPK in isoform 1. 1 PublicationVSP_005678Add
    BLAST
    Alternative sequencei485 – 675191Missing in isoform 1. 1 PublicationVSP_005679Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011358 mRNA. Translation: AAC99481.1.
    AF125046 mRNA. Translation: AAD20014.1.
    AL604043 Genomic DNA. Translation: CAM22971.1.
    CH466558 Genomic DNA. Translation: EDL34351.1.
    BC129899 mRNA. Translation: AAI29900.1.
    CCDSiCCDS25576.1. [O54828-1]
    CCDS48969.1. [O54828-2]
    RefSeqiNP_035398.2. NM_011268.2. [O54828-1]
    UniGeneiMm.38548.

    Genome annotation databases

    EnsembliENSMUST00000020920; ENSMUSP00000020920; ENSMUSG00000020599. [O54828-1]
    ENSMUST00000106706; ENSMUSP00000102317; ENSMUSG00000020599. [O54828-2]
    GeneIDi19739.
    KEGGimmu:19739.
    UCSCiuc007mbx.1. mouse. [O54828-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011358 mRNA. Translation: AAC99481.1 .
    AF125046 mRNA. Translation: AAD20014.1 .
    AL604043 Genomic DNA. Translation: CAM22971.1 .
    CH466558 Genomic DNA. Translation: EDL34351.1 .
    BC129899 mRNA. Translation: AAI29900.1 .
    CCDSi CCDS25576.1. [O54828-1 ]
    CCDS48969.1. [O54828-2 ]
    RefSeqi NP_035398.2. NM_011268.2. [O54828-1 ]
    UniGenei Mm.38548.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PBI X-ray 1.95 A/C 1-422 [» ]
    ProteinModelPortali O54828.
    SMRi O54828. Positions 7-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202886. 1 interaction.
    DIPi DIP-46389N.
    IntActi O54828. 4 interactions.

    Proteomic databases

    PaxDbi O54828.
    PRIDEi O54828.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020920 ; ENSMUSP00000020920 ; ENSMUSG00000020599 . [O54828-1 ]
    ENSMUST00000106706 ; ENSMUSP00000102317 ; ENSMUSG00000020599 . [O54828-2 ]
    GeneIDi 19739.
    KEGGi mmu:19739.
    UCSCi uc007mbx.1. mouse. [O54828-1 ]

    Organism-specific databases

    CTDi 8787.
    MGIi MGI:1338824. Rgs9.

    Phylogenomic databases

    eggNOGi NOG327614.
    GeneTreei ENSGT00700000104259.
    HOGENOMi HOG000220864.
    HOVERGENi HBG007404.
    InParanoidi A1L352.
    KOi K13765.
    OMAi LVKDMQN.
    OrthoDBi EOG7BZVS5.
    TreeFami TF351956.

    Enzyme and pathway databases

    Reactomei REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    ChiTaRSi RGS9. mouse.
    EvolutionaryTracei O54828.
    NextBioi 297184.
    PROi O54828.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54828.
    Bgeei O54828.
    CleanExi MM_RGS9.
    Genevestigatori O54828.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.196.10. 1 hit.
    4.10.260.10. 1 hit.
    InterProi IPR000591. DEP_dom.
    IPR015898. G-protein_gamma-like_dom.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00610. DEP. 1 hit.
    PF00631. G-gamma. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00049. DEP. 1 hit.
    SM00224. GGL. 1 hit.
    SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF48670. SSF48670. 1 hit.
    PROSITEi PS50186. DEP. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RGS9, a GTPase accelerator for phototransduction."
      He W., Cowan C.W., Wensel T.G.
      Neuron 20:95-102(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and characterization of RGS9-2: a striatal-enriched alternatively spliced product of the RGS9 gene."
      Rahman Z., Gold S.J., Potenza M.N., Cowan C.W., Ni Y.G., He W., Wensel T.G., Nestler E.J.
      J. Neurosci. 19:2016-2026(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Forebrain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Phosphorylation of RGS9-1 by an endogenous protein kinase in rod outer segments."
      Hu G., Jang G.F., Cowan C.W., Wensel T.G., Palczewski K.
      J. Biol. Chem. 276:22287-22295(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION OF ISOFORM 1.
    7. "R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1."
      Hu G., Wensel T.G.
      Proc. Natl. Acad. Sci. U.S.A. 99:9755-9760(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS9BP.
      Strain: C57BL/6 X 129.
      Tissue: Retina.
    8. "Identification of protein kinase C isozymes responsible for the phosphorylation of photoreceptor-specific RGS9-1 at Ser475."
      Sokal I., Hu G., Liang Y., Mao M., Wensel T.G., Palczewski K.
      J. Biol. Chem. 278:8316-8325(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS9BP.
    9. "The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo."
      Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M., Strissel K.J., Leskov I.B., Hopp J.A., Kolesnikov A.V., Chen C.-K., Lem J., Heller S., Burns M.E., Arshavsky V.Y.
      J. Neurosci. 23:10175-10181(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS9BP.
    10. "R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family."
      Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.
      J. Biol. Chem. 280:5133-5136(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS7BP.
    11. "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family."
      Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E., Linder M.E., Blumer K.J.
      J. Cell Biol. 169:623-633(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS7BP.
    12. Cited for: INTERACTION WITH RGS9BP.

    Entry informationi

    Entry nameiRGS9_MOUSE
    AccessioniPrimary (citable) accession number: O54828
    Secondary accession number(s): A1L352, Q9Z0S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3