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Protein

Rhodopsin kinase 2

Gene

grk7-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei218ATPPROSITE-ProRule annotation1
Active sitei314Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi195 – 203ATPPROSITE-ProRule annotation9

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

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin kinase 2 (EC:2.7.11.14By similarity)
Alternative name(s):
G protein-coupled receptor kinase 7B
Gene namesi
Name:grk7-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6252064. grk7.

Subcellular locationi

  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004128181 – 547Rhodopsin kinase 2Add BLAST547
PropeptideiPRO_0000412819548 – 550Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36Phosphoserine1 Publication1
Modified residuei487PhosphoserineBy similarity1
Modified residuei547Cysteine methyl esterSequence analysis1
Lipidationi547S-geranylgeranyl cysteineSequence analysis1

Post-translational modificationi

Autophosphorylated in vitro at Ser-487 (By similarity). Phosphorylation at Ser-36 is regulated by light and activated by cAMP.By similarity1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

PTM databases

iPTMnetiB6CZ18.

Expressioni

Tissue specificityi

Retina, cones.1 Publication

Structurei

3D structure databases

ProteinModelPortaliB6CZ18.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 174RGSPROSITE-ProRule annotationAdd BLAST118
Domaini189 – 451Protein kinasePROSITE-ProRule annotationAdd BLAST263
Domaini452 – 517AGC-kinase C-terminalAdd BLAST66

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

HOVERGENiHBG004532.
KOiK00909.

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.
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.

B6CZ18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDMGGLDNL IANTAYLQAR KSSEGDAKEL QKRRKSLSLP PPDVSRNEVK
60 70 80 90 100
ETITLDYQSI CVEQPIGQRL FKDFLATVPE YKLAEDFLEE VKEWELEEGS
110 120 130 140 150
AKEQLMEKLV SRRFKEPAEG SLNFLGKDLS SRIQQAQSKD MPELILLAKD
160 170 180 190 200
SGNAFLMDAP FQDFQNSPFY DRFLQWKAFE RQPINQKYFY EFRILGKGGF
210 220 230 240 250
GEVCAIQVKN TGQMYACKKL DKKRLKKKNG EKMALLEKEI LEKVHSPFIV
260 270 280 290 300
SLAYAYETKT HLCLVMSLMN GGDLKFHIYN VGDKGVEIKR VIFYSAQICC
310 320 330 340 350
GILHLHSLKI VYRDMKPENV LLDDHGNCRL SDLGLAVKVK EGKAITQRAG
360 370 380 390 400
TNGYMAPEIL TDEDYSYPVD WFAMGCSIFE MIAAYTPFRD PKEKTSKEEL
410 420 430 440 450
KRKTLEDEVV FPLPTFTEEA KDICRLFLAK KPQNRLGSRT NDDDPRKHAF
460 470 480 490 500
FKSINFQRLE AGMVDPPFVP DPSVVYAKDI SDIADFSEVK GIEFDDKDAK
510 520 530 540 550
LFKRFSTGAV PISWQKEIID TGLFDELNDP SREVTGGGNS GEKSGVCSIL
Length:550
Mass (Da):62,493
Last modified:November 25, 2008 - v1
Checksum:i86F610D8275855CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU621674 mRNA. Translation: ACF28431.1.
RefSeqiNP_001131052.1. NM_001137580.1.
UniGeneiXl.85104.

Genome annotation databases

GeneIDi100192359.
KEGGixla:100192359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU621674 mRNA. Translation: ACF28431.1.
RefSeqiNP_001131052.1. NM_001137580.1.
UniGeneiXl.85104.

3D structure databases

ProteinModelPortaliB6CZ18.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiB6CZ18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100192359.
KEGGixla:100192359.

Organism-specific databases

CTDi100192359.
XenbaseiXB-GENE-6252064. grk7.

Phylogenomic databases

HOVERGENiHBG004532.
KOiK00909.

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.
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...

Entry informationi

Entry nameiGRK7B_XENLA
AccessioniPrimary (citable) accession number: B6CZ18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 25, 2008
Last modified: May 11, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Although the protein is present in a diversity of vertebrates ranging from bony fish to mammals, the mouse and rat orthologous proteins do not exist.

Documents

  1. 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.