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Protein

Rhodopsin kinase

Gene

GRK1

Organism
Bos taurus (Bovine)
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.2 Publications

Enzyme regulationi

Inhibited by phosphorylation of Ser-21.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei216 – 2161ATPPROSITE-ProRule annotation
Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation
Binding sitei332 – 3321ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 2019ATPPROSITE-ProRule annotation1 Publication
Nucleotide bindingi265 – 2673ATP1 Publication

GO - Molecular functioni

GO - Biological processi

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

BioCyciMetaCyc:MONOMER-4461.
BRENDAi2.7.11.14. 908.
ReactomeiR-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKP28327.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin kinase (EC:2.7.11.142 Publications)
Short name:
RK
Alternative name(s):
G protein-coupled receptor kinase 1
Gene namesi
Name:GRK1
Synonyms:RHOK
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 12

Subcellular locationi

  • Membrane 1 Publication2 Publications; Lipid-anchor 1 Publication1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi558 – 5581C → S: 75% decrease in enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Rhodopsin kinasePRO_0000024373Add
BLAST
Propeptidei559 – 5613Removed in mature formPRO_0000024374

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei8 – 81Phosphothreonine1 Publication
Modified residuei21 – 211Phosphoserine; by PKA and autocatalysis2 Publications
Modified residuei488 – 4881Phosphoserine; by autocatalysis2 Publications
Modified residuei489 – 4891Phosphothreonine; by autocatalysis2 Publications
Modified residuei558 – 5581Cysteine methyl ester1 Publication
Lipidationi558 – 5581S-farnesyl cysteine1 Publication

Post-translational modificationi

Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-488 and Thr-489. Phosphorylation at Ser-21 is regulated by light and activated by cAMP (Probable).2 Publications
Farnesylation is required for full activity.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP28327.
PRIDEiP28327.

PTM databases

iPTMnetiP28327.

Expressioni

Tissue specificityi

Rod outer segments of retina photoreceptor cells (at protein level) (PubMed:1656454, PubMed:1730692, PubMed:1527025). Retina (PubMed:1656454).3 Publications

Interactioni

Subunit structurei

Interacts (when prenylated) with PDE6D; this promotes release from membranes.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RCVRNP214572EBI-7865560,EBI-8592784

Protein-protein interaction databases

IntActiP28327. 3 interactions.
MINTiMINT-1507451.
STRINGi9913.ENSBTAP00000042484.

Structurei

Secondary structure

1
561
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 175Combined sources
Helixi20 – 234Combined sources
Beta strandi25 – 273Combined sources
Helixi33 – 364Combined sources
Helixi44 – 474Combined sources
Helixi48 – 536Combined sources
Helixi58 – 625Combined sources
Helixi66 – 7813Combined sources
Helixi80 – 823Combined sources
Helixi83 – 9614Combined sources
Turni100 – 1023Combined sources
Helixi103 – 11412Combined sources
Beta strandi116 – 1194Combined sources
Helixi128 – 1358Combined sources
Turni140 – 1434Combined sources
Helixi144 – 15411Combined sources
Helixi157 – 1637Combined sources
Helixi166 – 17813Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1959Combined sources
Beta strandi197 – 20610Combined sources
Turni207 – 2093Combined sources
Beta strandi212 – 2198Combined sources
Helixi220 – 2256Combined sources
Helixi229 – 24113Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi257 – 2648Combined sources
Beta strandi269 – 2713Combined sources
Helixi272 – 2776Combined sources
Beta strandi278 – 2836Combined sources
Helixi288 – 30720Combined sources
Helixi317 – 3193Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi328 – 3303Combined sources
Helixi333 – 3353Combined sources
Turni353 – 3553Combined sources
Helixi358 – 3614Combined sources
Helixi369 – 38416Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi388 – 3903Combined sources
Helixi398 – 40710Combined sources
Helixi418 – 42710Combined sources
Helixi432 – 4343Combined sources
Helixi444 – 4474Combined sources
Helixi450 – 4523Combined sources
Helixi457 – 4615Combined sources
Beta strandi473 – 4753Combined sources
Helixi481 – 4833Combined sources
Helixi497 – 50610Combined sources
Helixi512 – 52110Combined sources
Helixi524 – 5285Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I94NMR-B1-25[»]
3C4WX-ray2.70A/B1-535[»]
3C4XX-ray2.90A/B1-535[»]
3C4YX-ray7.51A/B1-535[»]
3C4ZX-ray1.84A1-535[»]
3C50X-ray2.60A/B1-535[»]
3C51X-ray3.55A/B1-535[»]
3QC9X-ray2.70A/B/C/D1-535[»]
3T8OX-ray2.50A1-535[»]
4L9IX-ray2.32A/B30-533[»]
4PNIX-ray1.85A1-561[»]
4WBOX-ray2.81A/B/C/D1-535[»]
ProteinModelPortaliP28327.
SMRiP28327. Positions 30-533.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 172115RGSPROSITE-ProRule annotationAdd
BLAST
Domaini187 – 452266Protein kinasePROSITE-ProRule annotation1 PublicationAdd
BLAST
Domaini453 – 51866AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 186186N-terminalAdd
BLAST
Regioni453 – 561109C-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.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiP28327.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG7TF78J.
TreeFamiTF313940.

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.

P28327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFGSLETVV ANSAFIAARG SFDASSGPAS RDRKYLARLK LPPLSKCEAL
60 70 80 90 100
RESLDLGFEG MCLEQPIGKR LFQQFLRTHE QHGPALQLWK DIEDYDTADD
110 120 130 140 150
ALRPQKAQAL RAAYLEPQAQ LFCSFLDAET VARARAGAGD GLFQPLLRAV
160 170 180 190 200
LAHLGQAPFQ EFLDSLYFLR FLQWKWLEAQ PMGEDWFLDF RVLGRGGFGE
210 220 230 240 250
VFACQMKATG KLYACKKLNK KRLKKRKGYQ GAMVEKKILA KVHSRFIVSL
260 270 280 290 300
AYAFETKTDL CLVMTIMNGG DIRYHIYNVD EDNPGFQEPR AIFYTAQIVS
310 320 330 340 350
GLEHLHQRNI IYRDLKPENV LLDDDGNVRI SDLGLAVELK AGQTKTKGYA
360 370 380 390 400
GTPGFMAPEL LLGEEYDFSV DYFALGVTLY EMIAARGPFR ARGEKVENKE
410 420 430 440 450
LKQRVLEQAV TYPDKFSPAS KDFCEALLQK DPEKRLGFRD GSCDGLRTHP
460 470 480 490 500
LFRDISWRQL EAGMLTPPFV PDSRTVYAKN IQDVGAFSTV KGVAFEKADT
510 520 530 540 550
EFFQEFASGT CPIPWQEEMI ETGVFGDLNV WRPDGQMPDD MKGVSGQEAA
560
PSSKSGMCVL S
Length:561
Mass (Da):62,934
Last modified:December 1, 1992 - v1
Checksum:i1AC6FEC1B277DDD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73836 mRNA. Translation: AAA30752.1.
PIRiA41365.
RefSeqiNP_776598.1. NM_174173.2.
UniGeneiBt.459.

Genome annotation databases

EnsembliENSBTAT00000045068; ENSBTAP00000042484; ENSBTAG00000019963.
GeneIDi281457.
KEGGibta:281457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73836 mRNA. Translation: AAA30752.1.
PIRiA41365.
RefSeqiNP_776598.1. NM_174173.2.
UniGeneiBt.459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I94NMR-B1-25[»]
3C4WX-ray2.70A/B1-535[»]
3C4XX-ray2.90A/B1-535[»]
3C4YX-ray7.51A/B1-535[»]
3C4ZX-ray1.84A1-535[»]
3C50X-ray2.60A/B1-535[»]
3C51X-ray3.55A/B1-535[»]
3QC9X-ray2.70A/B/C/D1-535[»]
3T8OX-ray2.50A1-535[»]
4L9IX-ray2.32A/B30-533[»]
4PNIX-ray1.85A1-561[»]
4WBOX-ray2.81A/B/C/D1-535[»]
ProteinModelPortaliP28327.
SMRiP28327. Positions 30-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28327. 3 interactions.
MINTiMINT-1507451.
STRINGi9913.ENSBTAP00000042484.

PTM databases

iPTMnetiP28327.

Proteomic databases

PaxDbiP28327.
PRIDEiP28327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000045068; ENSBTAP00000042484; ENSBTAG00000019963.
GeneIDi281457.
KEGGibta:281457.

Organism-specific databases

CTDi6011.

Phylogenomic databases

eggNOGiKOG0986. Eukaryota.
ENOG410YRQZ. LUCA.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiP28327.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG7TF78J.
TreeFamiTF313940.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4461.
BRENDAi2.7.11.14. 908.
ReactomeiR-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKP28327.

Miscellaneous databases

EvolutionaryTraceiP28327.

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. "The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase."
    Lorenz W., Inglese J., Palczewski K., Onorato J.J., Caron M.G., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:8715-8719(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 268-297, TISSUE SPECIFICITY.
    Tissue: Retina.
  2. "Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase."
    Inglese J., Glickman J.F., Lorenz W., Caron M.G., Lefkowitz R.J.
    J. Biol. Chem. 267:1422-1425(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-558, METHYLATION AT CYS-558, MUTAGENESIS OF CYS-558, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Identification of the autophosphorylation sites in rhodopsin kinase."
    Palczewski K., Buczylko J., van Hooser P., Carr S.A., Huddleston M.J., Crabb J.W.
    J. Biol. Chem. 267:18991-18998(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-21; SER-488 AND THR-489, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein."
    Zhang H., Liu X.H., Zhang K., Chen C.K., Frederick J.M., Prestwich G.D., Baehr W.
    J. Biol. Chem. 279:407-413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE6D, SUBCELLULAR LOCATION.
  5. "Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation."
    Singh P., Wang B., Maeda T., Palczewski K., Tesmer J.J.
    J. Biol. Chem. 283:14053-14062(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 1-535 IN COMPLEX WITH ATP, PHOSPHORYLATION AT SER-5; THR-8; SER-21; SER-488 AND THR-489.

Entry informationi

Entry nameiRK_BOVIN
AccessioniPrimary (citable) accession number: P28327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 8, 2016
This is version 143 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, Direct protein sequencing, 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.