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Q49HM9 (GRK7A_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein-coupled receptor kinase 7A

EC=2.7.11.14
EC=2.7.11.16
Alternative name(s):
G protein-coupled receptor kinase 7-1
Gene names
Name:grk7a
Synonyms:grk7-1
ORF Names:dkeyp-13a3.1
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO). Ref.1

Catalytic activity

ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate. Ref.2

ATP + [rhodopsin] = ADP + [rhodopsin] phosphate. Ref.2

Subcellular location

Membrane; Lipid-anchor By similarity.

Post-translational modification

Phosphorylation at Ser-33 is regulated by light and activated by cAMP By similarity.

Disruption phenotype

Impaired cone response recovery and delayed dark adaptation. Ref.1

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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Contains 1 RGS domain.

Biophysicochemical properties

Kinetic parameters:

KM=4.4 µM for rhodopsin Ref.2

Vmax=773 nmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546G-protein-coupled receptor kinase 7A
PRO_0000412812
Propeptide547 – 5493Removed in mature form By similarity
PRO_0000412813

Regions

Domain53 – 171119RGS
Domain186 – 449264Protein kinase
Domain450 – 51566AGC-kinase C-terminal
Nucleotide binding192 – 2009ATP By similarity

Sites

Active site3111Proton acceptor By similarity
Binding site2151ATP By similarity

Amino acid modifications

Modified residue331Phosphoserine By similarity
Modified residue5461Cysteine methyl ester Potential
Lipidation5461S-geranylgeranyl cysteine Potential

Experimental info

Sequence conflict801T → I in AAX69081. Ref.1
Sequence conflict3851F → I in AAX69081. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q49HM9 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 3F76C291F8BC9716

FASTA54962,232
        10         20         30         40         50         60 
MCDMGGLDNL VANTAYLKAQ GGDDKEMKKR RRSLSLPKPE QCASLRTSLD KDFESLCEKQ 

        70         80         90        100        110        120 
PIGKKLFRQY LSQGGPECTT AAEFLDDLNE WELSESAARD KARTNIINKF CKEGSKSSLT 

       130        140        150        160        170        180 
FLTGDVATKC KAVSDKDFEE VMGQVKTATK EFLKGKPFTE YQASPFFDKF LQWKEYEKQP 

       190        200        210        220        230        240 
ISEKYFYEFR TLGKGGFGEV CAVQVKNTGQ MYACKKLCKK RLKKKHGEKM ALLEKKILER 

       250        260        270        280        290        300 
VNSLFIVSLA YAYDTKTHLC LVMSLMNGGD LKYHIYNIGE KGIEMDRIIY YTAQIATGIL 

       310        320        330        340        350        360 
HLHDMDIVYR DMKPENVLLD SQGQCRLSDL GLAVEIAVGK TISQKAGTGA YMAPEILNET 

       370        380        390        400        410        420 
PYRTSVDWWA LGCSIYEMVA GYTPFKGPDA KKEKVEKEEV QRRILNEEPK FEHKNFDAAT 

       430        440        450        460        470        480 
IDIIKQFLKK KIDERLGCKN DDPRKHEWFK SINFARLEAG LIDPPWVPKP NVVYAKDTGD 

       490        500        510        520        530        540 
IAEFSEIKGI EFDAKDDKFF KEFSTGAVSI AWQQEMIDTG LFDELSDPNR KESSGGSDDD 


KKSGTCTLL 

« Hide

References

« Hide 'large scale' references
[1]"Knockdown of cone-specific kinase GRK7 in larval zebrafish leads to impaired cone response recovery and delayed dark adaptation."
Rinner O., Makhankov Y.V., Biehlmaier O., Neuhauss S.C.
Neuron 47:231-242(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
[2]"GRK1 and GRK7: unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones."
Wada Y., Sugiyama J., Okano T., Fukada Y.
J. Neurochem. 98:824-837(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[3]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[4]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY900004 mRNA. Translation: AAX69081.1.
AB212995 mRNA. Translation: BAE92858.1.
CR377211 Genomic DNA. Translation: CAQ13370.1.
BC163587 mRNA. Translation: AAI63587.1.
RefSeqNP_001027011.2. NM_001031841.3.
UniGeneDr.82672.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000091060.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000100287; ENSDARP00000091060; ENSDARG00000020602.
GeneID566120.
KEGGdre:566120.

Organism-specific databases

CTD566120.
ZFINZDB-GENE-050824-1. grk7a.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110751.
HOGENOMHOG000006742.
HOVERGENHBG004532.
KOK00909.
OMAAYAFESK.
OrthoDBEOG7V1FQK.
TreeFamTF313940.

Enzyme and pathway databases

BRENDA2.7.11.14. 96826.

Gene expression databases

BgeeQ49HM9.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
SMARTSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

NextBio20888040.
PROQ49HM9.

Entry information

Entry nameGRK7A_DANRE
AccessionPrimary (citable) accession number: Q49HM9
Secondary accession number(s): Q1XHL8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: June 11, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families