Q49HM9 · GRK7A_DANRE

Function

function

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

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.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
4.4 μMrhodopsin
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
773 nmol/min/mg

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site192-200ATP (UniProtKB | ChEBI)
Binding site215ATP (UniProtKB | ChEBI)
Active site311Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionphotoreceptor activity
Molecular Functionrhodopsin kinase activity
Biological Processcone photoresponse recovery
Biological Processphototransduction, visible light
Biological Processregulation of signal transduction
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rhodopsin kinase grk7a
  • EC number
  • Alternative names
    • G protein-coupled receptor kinase 7-1
    • G-protein-coupled receptor kinase 7A

Gene names

    • Name
      grk7a
    • Synonyms
      grk7-1
    • ORF names
      dkeyp-13a3.1

Organism names

  • Taxonomic identifier
  • Strain
    • Tuebingen
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q49HM9
  • Secondary accessions
    • Q1XHL8

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Lipid-anchor

Keywords

Phenotypes & Variants

Disruption phenotype

Impaired cone response recovery and delayed dark adaptation.

PTM/Processing

Features

Showing features for chain, modified residue, lipidation, propeptide.

TypeIDPosition(s)Description
ChainPRO_00004128121-546Rhodopsin kinase grk7a
Modified residue33Phosphoserine
Modified residue546Cysteine methyl ester
Lipidation546S-geranylgeranyl cysteine
PropeptidePRO_0000412813547-549Removed in mature form

Post-translational modification

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

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain53-171RGS
Domain186-449Protein kinase
Domain450-515AGC-kinase C-terminal
Region522-549Disordered
Compositional bias524-539Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    549
  • Mass (Da)
    62,232
  • Last updated
    2011-09-21 v2
  • Checksum
    3F76C291F8BC9716
MCDMGGLDNLVANTAYLKAQGGDDKEMKKRRRSLSLPKPEQCASLRTSLDKDFESLCEKQPIGKKLFRQYLSQGGPECTTAAEFLDDLNEWELSESAARDKARTNIINKFCKEGSKSSLTFLTGDVATKCKAVSDKDFEEVMGQVKTATKEFLKGKPFTEYQASPFFDKFLQWKEYEKQPISEKYFYEFRTLGKGGFGEVCAVQVKNTGQMYACKKLCKKRLKKKHGEKMALLEKKILERVNSLFIVSLAYAYDTKTHLCLVMSLMNGGDLKYHIYNIGEKGIEMDRIIYYTAQIATGILHLHDMDIVYRDMKPENVLLDSQGQCRLSDLGLAVEIAVGKTISQKAGTGAYMAPEILNETPYRTSVDWWALGCSIYEMVAGYTPFKGPDAKKEKVEKEEVQRRILNEEPKFEHKNFDAATIDIIKQFLKKKIDERLGCKNDDPRKHEWFKSINFARLEAGLIDPPWVPKPNVVYAKDTGDIAEFSEIKGIEFDAKDDKFFKEFSTGAVSIAWQQEMIDTGLFDELSDPNRKESSGGSDDDKKSGTCTLL

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict80in Ref. 1; AAX69081
Sequence conflict385in Ref. 1; AAX69081
Compositional bias524-539Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY900004
EMBL· GenBank· DDBJ
AAX69081.1
EMBL· GenBank· DDBJ
mRNA
AB212995
EMBL· GenBank· DDBJ
BAE92858.1
EMBL· GenBank· DDBJ
mRNA
CR377211
EMBL· GenBank· DDBJ
CAQ13370.1
EMBL· GenBank· DDBJ
Genomic DNA
BC163587
EMBL· GenBank· DDBJ
AAI63587.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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