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O54828

- RGS9_MOUSE

UniProt

O54828 - RGS9_MOUSE

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO54828.
CleanExiMM_RGS9.
ExpressionAtlasiO54828. baseline and differential.
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.
GeneTreeiENSGT00760000119142.
HOGENOMiHOG000220864.
HOVERGENiHBG007404.
InParanoidiO54828.
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

        10         20         30         40         50
MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM
60 70 80 90 100
TGGDVLQWIT QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL
110 120 130 140 150
YRFQTPYFWP TQQWPAEDTD YAIYLAKRNI KKKGILEEYE KENYDFLNKK
160 170 180 190 200
INYKWDFVIM QAKEQYRTGK ERNKADRYAL DCQEKAYWLV HRSPPGMNNV
210 220 230 240 250
LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS SVSLGGIVKY
260 270 280 290 300
SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF
310 320 330 340 350
SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI
360 370 380 390 400
YKLFLAPGAR RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS
410 420 430 440 450
YARYLKSPIY KEMLAKAIEP QETTKRSSTL PFMRRHLRSS PSPVILRQLE
460 470 480 490 500
EEEKAREAAN TVDITQPGQH LAPSPHLAVY TGTCVPPSPS SPFSPSCRSP
510 520 530 540 550
RKPFASPSRF IRRPSIAICP SPSRVALEGS SGLEPKGEAS WSGANSGPSV
560 570 580 590 600
TENREPSADH SRPQPRAPPK ARAALSLGRF LRRGCLASPV FARLSPKCPS
610 620 630 640 650
VSHGKVQPLG DMGQQLPRLK PKKVANFFQI KMEMPTDSGT CLMDSDDPRA
660 670
GESGDQTTEK EVICPWESLA EGKAG
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 ENSGT00760000119142.
HOGENOMi HOG000220864.
HOVERGENi HBG007404.
InParanoidi O54828.
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

Bgeei O54828.
CleanExi MM_RGS9.
ExpressionAtlasi O54828. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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