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Protein

Rhodopsin kinase

Gene

Grk1

Organism
Rattus norvegicus (Rat)
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.By similarity

Catalytic activityi

ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.By similarity

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

  1. ATP binding Source: UniProtKB-KW
  2. G-protein coupled receptor kinase activity Source: InterPro
  3. rhodopsin kinase activity Source: RGD

GO - Biological processi

  1. protein autophosphorylation Source: RGD
  2. regulation of rhodopsin mediated signaling pathway Source: UniProtKB
  3. response to drug Source: RGD
  4. response to light stimulus Source: RGD
  5. rhodopsin mediated signaling pathway Source: RGD
  6. termination of G-protein coupled receptor signaling pathway Source: InterPro
  7. 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

Enzyme and pathway databases

BRENDAi2.7.11.14. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin kinase (EC:2.7.11.14By similarity)
Short name:
RK
Alternative name(s):
G protein-coupled receptor kinase 1
Gene namesi
Name:Grk1
Synonyms:Rhok
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619712. Grk1.

Subcellular locationi

Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Rhodopsin kinasePRO_0000024379Add
BLAST
Propeptidei562 – 5643Removed in mature formBy similarityPRO_0000024380

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 (By similarity). Phosphorylation at Ser-21 is regulated by light and activated by cAMP.By similarity1 Publication
Farnesylation is required for full activity.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiQ63651.
PRIDEiQ63651.

PTM databases

PhosphoSiteiQ63651.

Expressioni

Tissue specificityi

Detected in retina (at protein level) (PubMed:21504899). Retina-specific. Expressed in rod and cone photoreceptor cells.2 Publications

Gene expression databases

GenevestigatoriQ63651.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024999.

Structurei

3D structure databases

ProteinModelPortaliQ63651.
SMRiQ63651. Positions 30-536.
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

eggNOGiCOG0515.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ63651.
KOiK00909.
PhylomeDBiQ63651.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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.

Q63651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFGSLETVV ANSAFIAARG SFDGSSTPSS RDKKYLAKLR LPPLSKCEGL
60 70 80 90 100
RDSISLEFDN LCSEQPIGKR LFQQFLKTDE RHVPALELWK DIEDYDTADD
110 120 130 140 150
DLRPQKAQAI LAEYLDPQGT LFCNFLDQGM VARVKEGPTG SQDGLFQPLL
160 170 180 190 200
QATLEHLSQG PFQEYLGSLY FLRFLQWKWL EAQPIGEDWF LDFRVLGKGG
210 220 230 240 250
FGEVSACQMK ATGKMYACKK LNKKRLKKRK GYQGAIVEKR ILAKVHSRFI
260 270 280 290 300
VSLAYAFETK TDLCLVMTIM NGGDVRYHIY NVDEENPGFP 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 EMIETGFFGD LNVWRPDGQM PDDMKGITVE
560
EAAPTAKSGM CLIS
Length:564
Mass (Da):63,769
Last modified:November 1, 1997 - v1
Checksum:i17E05784E6D1ED00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63971 mRNA. Translation: AAB05930.1.
RefSeqiNP_112358.1. NM_031096.1.
UniGeneiRn.10548.

Genome annotation databases

GeneIDi81760.
KEGGirno:81760.
UCSCiRGD:619712. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63971 mRNA. Translation: AAB05930.1.
RefSeqiNP_112358.1. NM_031096.1.
UniGeneiRn.10548.

3D structure databases

ProteinModelPortaliQ63651.
SMRiQ63651. Positions 30-536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024999.

PTM databases

PhosphoSiteiQ63651.

Proteomic databases

PaxDbiQ63651.
PRIDEiQ63651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81760.
KEGGirno:81760.
UCSCiRGD:619712. rat.

Organism-specific databases

CTDi6011.
RGDi619712. Grk1.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ63651.
KOiK00909.
PhylomeDBiQ63651.

Enzyme and pathway databases

BRENDAi2.7.11.14. 5301.

Miscellaneous databases

NextBioi615542.

Gene expression databases

GenevestigatoriQ63651.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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. "Molecular cloning and localization of rhodopsin kinase in the mammalian pineal."
    Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H., Palczewski K.
    Vis. Neurosci. 14:225-232(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Retina.
  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(2000) [PubMed] [Europe PMC] [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-31, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-21, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRK_RAT
AccessioniPrimary (citable) accession number: Q63651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 123 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.