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Protein

Rhodopsin kinase

Gene

Grk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191ATPPROSITE-ProRule annotation
Active sitei317 – 3171Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2049ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • negative regulation of apoptotic process Source: MGI
  • photoreceptor cell morphogenesis Source: MGI
  • positive regulation of phosphorylation Source: MGI
  • post-embryonic retina morphogenesis in camera-type eye Source: MGI
  • protein autophosphorylation Source: UniProtKB
  • regulation of rhodopsin mediated signaling pathway Source: UniProtKB
  • response to light stimulus Source: MGI
  • signal transduction Source: InterPro
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin kinase (EC:2.7.11.141 Publication)
Short name:
RK
Alternative name(s):
G protein-coupled receptor kinase 1
Gene namesi
Name:Grk1
Synonyms:Rhok
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1345146. Grk1.

Subcellular locationi

  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  • membrane Source: UniProtKB-SubCell
  • photoreceptor outer segment Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

In rod photoreceptor cells, the light-induced ion currents do not decay rapidly, but are greatly prolonged, contrary to what is observed with wild-type mice. The retina photoreceptor layer appears normal when mutant mice are kept in constant darkness, but exposure to light causes apoptosis in retina photoreceptor cells.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Rhodopsin kinasePRO_0000024377Add
BLAST
Propeptidei562 – 5643Removed in mature formBy similarityPRO_0000024378

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei21 – 211Phosphoserine; by PKA and autocatalysis1 Publication
Modified residuei491 – 4911Phosphoserine; by autocatalysisBy similarity
Modified residuei492 – 4921Phosphothreonine; by autocatalysisBy similarity
Modified residuei561 – 5611Cysteine methyl esterBy similarity
Lipidationi561 – 5611S-farnesyl cysteineBy similarity

Post-translational modificationi

Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492. Phosphorylation at Ser-21 is regulated by light and activated by cAMP.By similarity
Farnesylation is required for full activity.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ9WVL4.
PaxDbiQ9WVL4.
PRIDEiQ9WVL4.

PTM databases

iPTMnetiQ9WVL4.
PhosphoSiteiQ9WVL4.

Expressioni

Tissue specificityi

Primarily located in rod outer segments of retina photoreceptor cells. Also detected in cone photoreceptor cells (at protein level) (PubMed:10704496). Detected in retina (PubMed:10097103, PubMed:10704496).4 Publications

Gene expression databases

CleanExiMM_GRK1.

Interactioni

Subunit structurei

Interacts (when prenylated) with PDE6D; this promotes release from membranes.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033827.

Structurei

3D structure databases

ProteinModelPortaliQ9WVL4.
SMRiQ9WVL4. Positions 30-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 175118RGSPROSITE-ProRule annotationAdd
BLAST
Domaini190 – 455266Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini456 – 52166AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189N-terminalAdd
BLAST
Regioni456 – 564109C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0986. Eukaryota.
ENOG410YRQZ. LUCA.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ9WVL4.
PhylomeDBiQ9WVL4.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR032965. GRK1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24355:SF11. PTHR24355:SF11. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFGSLETVV ANSAFIAARG SFDGSSTPSS RDKKYLAKLR LPPLSKCEGL
60 70 80 90 100
RDNLSLEFES LCSEQPIGKR LFQQFLKTDE RHVPALELWK DIEDYDTADD
110 120 130 140 150
DLRPQKAQAI LAEYLDPQGT LFCNFLDQGM VTRVKEGPTG SQDGLFQPLL
160 170 180 190 200
QATMEHLSQA PFQEYLESLY FLRFLQWKWL EAQPIGEDWF LDFRVLGKGG
210 220 230 240 250
FGEVSACQMK ATGKMYACKK LNKKRLKKKK GYQGAIVEKR ILTKVHSRFI
260 270 280 290 300
VSLAYAFETK TDLCLVMTIM NGGDVRYHIY NVDEDNPGFS EPRAIYYTAQ
310 320 330 340 350
IISGLEHLHQ RRIVYRDLKP ENVLLDNDGN IRISDLGLAV ELKEGQNKTK
360 370 380 390 400
GYAGTPGFMA PELLRGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE
410 420 430 440 450
NKELKQRIIS EPVKYPEKFS QASKDFCEQL LEKDPEKRLG FRDGTCDALR
460 470 480 490 500
ANVLFKDISW RQLEAGMLIP PFIPDSRTVY AKNIQDVGAF STVKGVVFDK
510 520 530 540 550
ADTEFFQEFA SGNCSIPWQE EMIETGLFGD LNVWRADGQM PDDMKGITTE
560
EAAPTAKSGM CLIS
Length:564
Mass (Da):63,837
Last modified:November 1, 1999 - v1
Checksum:iEF0795FAE42BA5DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085240 mRNA. Translation: AAD40189.1.
CCDSiCCDS22112.1.
UniGeneiMm.257501.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085240 mRNA. Translation: AAD40189.1.
CCDSiCCDS22112.1.
UniGeneiMm.257501.

3D structure databases

ProteinModelPortaliQ9WVL4.
SMRiQ9WVL4. Positions 30-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033827.

PTM databases

iPTMnetiQ9WVL4.
PhosphoSiteiQ9WVL4.

Proteomic databases

MaxQBiQ9WVL4.
PaxDbiQ9WVL4.
PRIDEiQ9WVL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1345146. Grk1.

Phylogenomic databases

eggNOGiKOG0986. Eukaryota.
ENOG410YRQZ. LUCA.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ9WVL4.
PhylomeDBiQ9WVL4.

Miscellaneous databases

ChiTaRSiGrk1. mouse.
PROiQ9WVL4.
SOURCEiSearch...

Gene expression databases

CleanExiMM_GRK1.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR032965. GRK1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24355:SF11. PTHR24355:SF11. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  2. "Mice lacking G-protein receptor kinase 1 have profoundly slowed recovery of cone-driven retinal responses."
    Lyubarsky A.L., Chen C., Simon M.I., Pugh E.N. Jr.
    J. Neurosci. 20:2209-2217(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  3. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-21.

Entry informationi

Entry nameiRK_MOUSE
AccessioniPrimary (citable) accession number: Q9WVL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 126 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.