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Protein

Regulator of G-protein signaling 9

Gene

RGS9

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiR-BTA-2514859. 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Regulator of G-protein signaling 9PRO_0000204202Add
BLAST

Post-translational modificationi

Phosphorylation is decreased by light exposition.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO46469.
PRIDEiO46469.

PTM databases

iPTMnetiO46469.

Expressioni

Tissue specificityi

Photoreceptor outer segments.

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 RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP (Probable).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GNB5A5PJS15EBI-6949890,EBI-6949917

Protein-protein interaction databases

IntActiO46469. 2 interactions.
STRINGi9913.ENSBTAP00000023605.

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi282 – 2843Combined sources
Helixi290 – 2956Combined sources
Turni296 – 2983Combined sources
Helixi300 – 3045Combined sources
Helixi307 – 31913Combined sources
Helixi324 – 33613Combined sources
Helixi340 – 3423Combined sources
Helixi343 – 35412Combined sources
Helixi367 – 37610Combined sources
Turni382 – 3854Combined sources
Helixi386 – 39914Combined sources
Helixi401 – 4055Combined sources
Helixi408 – 4169Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQIX-ray1.94A276-422[»]
1FQJX-ray2.02B/E276-422[»]
1FQKX-ray2.30B/D276-422[»]
ProteinModelPortaliO46469.
SMRiO46469. Positions 7-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO46469.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10576DEPPROSITE-ProRule annotationAdd
BLAST
Domaini219 – 28062G 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

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
HOGENOMiHOG000220864.
HOVERGENiHBG007404.
InParanoidiO46469.
KOiK13765.

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.
IPR016137. RGS.
IPR024066. RGS_subdom1.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O46469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIRHQGQQY RPRMAFLRKI EALVKDMQDP DTGVRVQNQK VKVVSIPHAM
60 70 80 90 100
TGSDVLQWIS QRLWISGLEA QNLGNFIVKY GYIYPLQDPR NLTLKPDSSL
110 120 130 140 150
YRFQTPYFWP TQQWPAEDVD YAIYLAKRNI KKKGILEEYE KENYNFLNKK
160 170 180 190 200
INYKWDFVIM QAREQYRAGK ERNKVDRCAL DCQEKAYWLV HRCPPGANNV
210 220 230 240 250
LDYGLDRVTN PNEDQKQTVV SVRKEIMYYR QALMRSTVKS SVSLGGIVKY
260 270 280 290 300
SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVDIPTK MRVERWAFNF
310 320 330 340 350
SELIRDPKGR QSFQHFLRKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI
360 370 380 390 400
YKLFLAPGAR RWINIDGKTM DITVKGLKHP HRYVLDAAQT HIYMLMKKDS
410 420 430 440 450
YARYLKSPIY KEMLAKAIEP QGTTRKSSSL PFMRRHLRSS PSPVILRQLE
460 470 480
EEAKAREAAT TVDITQVMSK LDRRSQLRKE PPPK
Length:484
Mass (Da):56,680
Last modified:June 1, 1998 - v1
Checksum:i3D8C61CEC1E22949
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011357 mRNA. Translation: AAC99480.1.
RefSeqiNP_776595.1. NM_174170.2.
UniGeneiBt.97062.

Genome annotation databases

GeneIDi281453.
KEGGibta:281453.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011357 mRNA. Translation: AAC99480.1.
RefSeqiNP_776595.1. NM_174170.2.
UniGeneiBt.97062.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQIX-ray1.94A276-422[»]
1FQJX-ray2.02B/E276-422[»]
1FQKX-ray2.30B/D276-422[»]
ProteinModelPortaliO46469.
SMRiO46469. Positions 7-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO46469. 2 interactions.
STRINGi9913.ENSBTAP00000023605.

PTM databases

iPTMnetiO46469.

Proteomic databases

PaxDbiO46469.
PRIDEiO46469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281453.
KEGGibta:281453.

Organism-specific databases

CTDi8787.

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
HOGENOMiHOG000220864.
HOVERGENiHBG007404.
InParanoidiO46469.
KOiK13765.

Enzyme and pathway databases

ReactomeiR-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

EvolutionaryTraceiO46469.

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.
IPR016137. RGS.
IPR024066. RGS_subdom1.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
  2. "The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit."
    Makino E.R., Handy J.W., Li T., Arshavsky V.Y.
    Proc. Natl. Acad. Sci. U.S.A. 96:1947-1952(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GBB5.
  3. "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.
  4. "Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A."
    Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B.
    Nature 409:1071-1077(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 276-422 IN COMPLEX WITH PDE6G AND GNAT1.

Entry informationi

Entry nameiRGS9_BOVIN
AccessioniPrimary (citable) accession number: O46469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 130 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.