O54828 (RGS9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 9
Short name=RGS9

Gene names

Name:

Rgs9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	675 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Isoform 1: Membrane; Peripheral membrane protein. Note: Isoform 1 is targeted to the membrane via its interaction with RGS9BP.
Tissue specificity	Isoform 1 is expressed in photoreceptor outer segments. Isoform 2 is expressed in brain striatum.
Post-translational modification	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'. Ref.6
Sequence similarities	Contains 1 DEP domain. Contains 1 G protein gamma domain. Contains 1 RGS domain.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Signal transduction inhibitor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Traceable author statement PubMed 11342430. Source: MGI dopamine receptor signaling pathway Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: InterPro nervous system development Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome heterotrimeric G-protein complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: O54828-1)

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.

Isoform 1 (identifier: O54828-2)

Also known as: RGS9-1;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 675

675

Regulator of G-protein signaling 9

PRO_0000204204

Regions

Domain

30 – 105

76

DEP

Domain

222 – 283

62

G protein gamma

Domain

299 – 414

116

RGS

Natural variations

Alternative sequence

467 – 484

18

PGQHL…YTGTC → VMSKLDRRSQLKKELPPK in isoform 1.

VSP_005678

Alternative sequence

485 – 675

191

Missing in isoform 1.

VSP_005679

Experimental info

Sequence conflict

76

1

F → L in AAC99481. Ref.1

Sequence conflict

76

1

F → L in AAD20014. Ref.2

Sequence conflict

161

1

Q → R in AAC99481. Ref.1

Sequence conflict

161

1

Q → R in AAD20014. Ref.2

Secondary structure

1

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675

Helix Strand Turn

Details...

Helix

16 – 27

12

Turn

30 – 32

3

Helix

52 – 63

12

Helix

67 – 79

13

Beta strand

82 – 88

7

Beta strand

96 – 98

3

Beta strand

100 – 103

4

Helix

106 – 108

3

Helix

118 – 130

13

Beta strand

132 – 134

3

Helix

138 – 150

13

Helix

152 – 154

3

Helix

155 – 169

15

Helix

174 – 191

18

Beta strand

207 – 209

3

Helix

219 – 234

16

Helix

240 – 254

15

Helix

255 – 257

3

Helix

259 – 262

4

Helix

269 – 272

4

Helix

276 – 280

5

Helix

290 – 295

6

Turn

296 – 298

3

Helix

300 – 305

6

Helix

307 – 319

13

Helix

325 – 337

13

Beta strand

340 – 342

3

Helix

343 – 354

12

Helix

367 – 376

10

Turn

382 – 385

4

Helix

386 – 398

13

Helix

400 – 405

6

Helix

408 – 416

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (RGS9-2) [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 72F1652D7D59EB05	FASTA	675	76,978
	10 20 30 40 50 60 MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM TGGDVLQWIT 70 80 90 100 110 120 QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL YRFQTPYFWP TQQWPAEDTD 130 140 150 160 170 180 YAIYLAKRNI KKKGILEEYE KENYDFLNKK INYKWDFVIM QAKEQYRTGK ERNKADRYAL 190 200 210 220 230 240 DCQEKAYWLV HRSPPGMNNV LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS 250 260 270 280 290 300 SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF 310 320 330 340 350 360 SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR 370 380 390 400 410 420 RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP 430 440 450 460 470 480 QETTKRSSTL PFMRRHLRSS PSPVILRQLE EEEKAREAAN TVDITQPGQH LAPSPHLAVY 490 500 510 520 530 540 TGTCVPPSPS SPFSPSCRSP RKPFASPSRF IRRPSIAICP SPSRVALEGS SGLEPKGEAS 550 560 570 580 590 600 WSGANSGPSV TENREPSADH SRPQPRAPPK ARAALSLGRF LRRGCLASPV FARLSPKCPS 610 620 630 640 650 660 VSHGKVQPLG DMGQQLPRLK PKKVANFFQI KMEMPTDSGT CLMDSDDPRA GESGDQTTEK 670 EVICPWESLA EGKAG
	Isoform 1 (RGS9-1) [UniParc]. Checksum: 60B37878EBB4CD3C	FASTA	484	56,940
	10 20 30 40 50 60 MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM TGGDVLQWIT 70 80 90 100 110 120 QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL YRFQTPYFWP TQQWPAEDTD 130 140 150 160 170 180 YAIYLAKRNI KKKGILEEYE KENYDFLNKK INYKWDFVIM QAKEQYRTGK ERNKADRYAL 190 200 210 220 230 240 DCQEKAYWLV HRSPPGMNNV LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS 250 260 270 280 290 300 SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF 310 320 330 340 350 360 SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR 370 380 390 400 410 420 RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP 430 440 450 460 470 480 QETTKRSSTL PFMRRHLRSS PSPVILRQLE EEEKAREAAN TVDITQVMSK LDRRSQLKKE LPPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"RGS expression rate-limits recovery of rod photoresponses." Krispel C.M., Chen D., Melling N., Chen Y.-J., Martemyanov K.A., Quillinan N., Arshavsky V.Y., Wensel T.G., Chen C.-K., Burns M.E. Neuron 51:409-416(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RGS9BP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00118767.
IPI00223466.

RefSeq

NP_035398.2. NM_011268.2.

UniGene

Mm.38548.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PBI	X-ray	1.95	A/C	1-422	[»]

ProteinModelPortal

O54828.

SMR

O54828. Positions 7-421.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46389N.

IntAct

O54828. 4 interactions.

Proteomic databases

PaxDb

O54828.

PRIDE

O54828.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020920; ENSMUSP00000020920; ENSMUSG00000020599.
ENSMUST00000106706; ENSMUSP00000102317; ENSMUSG00000020599.

GeneID

19739.

KEGG

mmu:19739.

Organism-specific databases

CTD

8787.

MGI

MGI:1338824. Rgs9.

Phylogenomic databases

eggNOG

NOG327614.

GeneTree

ENSGT00700000104259.

HOGENOM

HOG000220864.

HOVERGEN

HBG007404.

InParanoid

A1L352.

KO

K13765.

OMA

AKLVEIP.

OrthoDB

EOG44XJGT.

Gene expression databases

ArrayExpress

O54828.

Bgee

O54828.

CleanEx

MM_RGS9.

Genevestigator

O54828.

GermOnline

ENSMUSG00000020599. Mus musculus.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.

InterPro

IPR000591. DEP_dom.
IPR015898. G-protein_gamma-like_dom.
IPR000342. Regulat_G_prot_signal.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]

PRINTS

PR01301. RGSPROTEIN.

SMART

SM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]

SUPFAM

SSF48670. G-protein_gamma-like. 1 hit.
SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS50186. DEP. 1 hit.
PS50058. G_PROTEIN_GAMMA. False negative.
PS50132. RGS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RGS9. mouse.

EvolutionaryTrace

O54828.

NextBio

297184.

SOURCE

Search...

Entry information

Entry name

RGS9_MOUSE

Accession

Primary (citable) accession number: O54828
Secondary accession number(s): A1L352, Q9Z0S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program