Rhodopsin kinase precursor - Mus musculus (Mouse)

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Q9WVL4 (RK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Rhodopsin kinase
Short name=RK
EC=2.7.11.14

Alternative name(s):
G protein-coupled receptor kinase 1

Gene names

Name:	Grk1
Synonyms:	Rhok

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination.
Catalytic activity	ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.
Subcellular location	Membrane; Lipid-anchor.
Tissue specificity	Retinal-specific. Primarily located in rod outer segments. Expressed also in cones cells. Ref.2 Ref.3
Post-translational modification	Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492 By similarity. Phosphorylation at Ser-21 is regulated by light and activated by cAMP By similarity. Ref.3 Farnesylation is required for full activity By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain. Contains 1 RGS domain.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of rhodopsin mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activity Inferred from electronic annotation. Source: InterPro rhodopsin kinase activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 561

561

Rhodopsin kinase

PRO_0000024377

Propeptide

562 – 564

Removed in mature form By similarity

PRO_0000024378

Regions

Domain

58 – 175

118

RGS

Domain

190 – 455

266

Protein kinase

Domain

456 – 521

AGC-kinase C-terminal

Nucleotide binding

196 – 204

ATP By similarity

Region

1 – 189

189

N-terminal

Region

456 – 564

109

C-terminal

Sites

Active site

317

Proton acceptor By similarity

Binding site

219

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine; by PKA and autocatalysis Probable

Modified residue

491

Phosphoserine; by autocatalysis By similarity

Modified residue

492

Phosphothreonine; by autocatalysis By similarity

Modified residue

561

Cysteine methyl ester By similarity

Lipidation

561

S-farnesyl cysteine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WVL4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: EF0795FAE42BA5DB
Show »

FASTA

564

63,837

        10         20         30         40         50         60 
MDFGSLETVV ANSAFIAARG SFDGSSTPSS RDKKYLAKLR LPPLSKCEGL RDNLSLEFES 

        70         80         90        100        110        120 
LCSEQPIGKR LFQQFLKTDE RHVPALELWK DIEDYDTADD DLRPQKAQAI LAEYLDPQGT 

       130        140        150        160        170        180 
LFCNFLDQGM VTRVKEGPTG SQDGLFQPLL QATMEHLSQA PFQEYLESLY FLRFLQWKWL 

       190        200        210        220        230        240 
EAQPIGEDWF LDFRVLGKGG FGEVSACQMK ATGKMYACKK LNKKRLKKKK GYQGAIVEKR 

       250        260        270        280        290        300 
ILTKVHSRFI VSLAYAFETK TDLCLVMTIM NGGDVRYHIY NVDEDNPGFS EPRAIYYTAQ 

       310        320        330        340        350        360 
IISGLEHLHQ RRIVYRDLKP ENVLLDNDGN IRISDLGLAV ELKEGQNKTK GYAGTPGFMA 

       370        380        390        400        410        420 
PELLRGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE NKELKQRIIS EPVKYPEKFS 

       430        440        450        460        470        480 
QASKDFCEQL LEKDPEKRLG FRDGTCDALR ANVLFKDISW RQLEAGMLIP PFIPDSRTVY 

       490        500        510        520        530        540 
AKNIQDVGAF STVKGVVFDK ADTEFFQEFA SGNCSIPWQE EMIETGLFGD LNVWRADGQM 

       550        560 
PDDMKGITTE EAAPTAKSGM CLIS

« Hide

References

[1]	"Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase." Chen C.K., Burns M.E., Spencer M., Niemi G.A., Chen J., Hurley J.B., Baylor D.A., Simon M.I. Proc. Natl. Acad. Sci. U.S.A. 96:3718-3722(1999) [PubMed: 10097103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Species-specific differences in expression of G-protein-coupled receptor kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor cells: implications for cone cell phototransduction." Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S. J. Neurosci. 21:9175-9184(2001) [PubMed: 11717351] [Abstract] Cited for: TISSUE SPECIFICITY.
[3]	"Phosphorylation of G protein-coupled receptor kinase 1 (GRK1) is regulated by light but independent of phototransduction in rod photoreceptors." Osawa S., Jo R., Xiong Y., Reidel B., Tserentsoodol N., Arshavsky V.Y., Iuvone P.M., Weiss E.R. J. Biol. Chem. 286:20923-20929(2011) [PubMed: 21504899] [Abstract] Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-21.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF085240 mRNA. Translation: AAD40189.1.
IPI	IPI00126128.
UniGene	Mm.257501.
3D structure databases
ProteinModelPortal	Q9WVL4.
SMR	Q9WVL4. Positions 30-535.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WVL4.
PTM databases
PhosphoSite	Q9WVL4.
Proteomic databases
PRIDE	Q9WVL4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:1345146. Grk1.
Phylogenomic databases
GeneTree	ENSGT00550000074318.
HOGENOM	HBG716704.
HOVERGEN	HBG004532.
InParanoid	Q9WVL4.
OrthoDB	EOG4Q84X5.
Gene expression databases
ArrayExpress	Q9WVL4.
Bgee	Q9WVL4.
CleanEx	MM_GRK1.
Genevestigator	Q9WVL4.
GermOnline	ENSMUSG00000031450. Mus musculus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000239. GPCR_kinase. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000342. Regulat_G_prot_signal. IPR016137. Regulat_G_prot_signal_superfam. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00615. RGS. 1 hit. [Graphical view]
PRINTS	PR00717. GPCRKINASE.
SMART	SM00315. RGS. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF48097. Regulat_G_prot_signal_superfam. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50132. RGS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

RK_MOUSE

Accession

Primary (citable) accession number: Q9WVL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	October 19, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents