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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)DescriptionActionsGraphical viewLength
Binding sitei216ATPPROSITE-ProRule annotation1
Active sitei314Proton acceptorPROSITE-ProRule annotation1
Binding sitei332ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi193 – 201ATPPROSITE-ProRule annotation1 Publication9
Nucleotide bindingi265 – 267ATP1 Publication3

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)DescriptionActionsGraphical viewLength
Mutagenesisi558C → S: 75% decrease in enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000243731 – 558Rhodopsin kinaseAdd BLAST558
PropeptideiPRO_0000024374559 – 561Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5Phosphoserine1 Publication1
Modified residuei8Phosphothreonine1 Publication1
Modified residuei21Phosphoserine; by PKA and autocatalysis2 Publications1
Modified residuei488Phosphoserine; by autocatalysis2 Publications1
Modified residuei489Phosphothreonine; by autocatalysis2 Publications1
Modified residuei558Cysteine methyl ester1 Publication1
Lipidationi558S-farnesyl cysteine1 Publication1

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 interactors.
MINTiMINT-1507451.
STRINGi9913.ENSBTAP00000042484.

Structurei

Secondary structure

1561
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 17Combined sources5
Helixi20 – 23Combined sources4
Beta strandi25 – 27Combined sources3
Helixi33 – 36Combined sources4
Helixi44 – 47Combined sources4
Helixi48 – 53Combined sources6
Helixi58 – 62Combined sources5
Helixi66 – 78Combined sources13
Helixi80 – 82Combined sources3
Helixi83 – 96Combined sources14
Turni100 – 102Combined sources3
Helixi103 – 114Combined sources12
Beta strandi116 – 119Combined sources4
Helixi128 – 135Combined sources8
Turni140 – 143Combined sources4
Helixi144 – 154Combined sources11
Helixi157 – 163Combined sources7
Helixi166 – 178Combined sources13
Helixi184 – 186Combined sources3
Beta strandi187 – 195Combined sources9
Beta strandi197 – 206Combined sources10
Turni207 – 209Combined sources3
Beta strandi212 – 219Combined sources8
Helixi220 – 225Combined sources6
Helixi229 – 241Combined sources13
Beta strandi250 – 255Combined sources6
Beta strandi257 – 264Combined sources8
Beta strandi269 – 271Combined sources3
Helixi272 – 277Combined sources6
Beta strandi278 – 283Combined sources6
Helixi288 – 307Combined sources20
Helixi317 – 319Combined sources3
Beta strandi320 – 322Combined sources3
Beta strandi328 – 330Combined sources3
Helixi333 – 335Combined sources3
Turni353 – 355Combined sources3
Helixi358 – 361Combined sources4
Helixi369 – 384Combined sources16
Beta strandi385 – 387Combined sources3
Beta strandi388 – 390Combined sources3
Helixi398 – 407Combined sources10
Helixi418 – 427Combined sources10
Helixi432 – 434Combined sources3
Helixi444 – 447Combined sources4
Helixi450 – 452Combined sources3
Helixi457 – 461Combined sources5
Beta strandi473 – 475Combined sources3
Helixi481 – 483Combined sources3
Helixi497 – 506Combined sources10
Helixi512 – 521Combined sources10
Helixi524 – 528Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 172RGSPROSITE-ProRule annotationAdd BLAST115
Domaini187 – 452Protein kinasePROSITE-ProRule annotation1 PublicationAdd BLAST266
Domaini453 – 518AGC-kinase C-terminalAdd BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 186N-terminalAdd BLAST186
Regioni453 – 561C-terminalAdd BLAST109

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.
GeneTreeiENSGT00860000133699.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiP28327.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG091G062G.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28327. 3 interactors.
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.
GeneTreeiENSGT00860000133699.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiP28327.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG091G062G.
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...

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: November 30, 2016
This is version 147 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.