Q49HM9 · GRK7A_DANRE
- ProteinRhodopsin kinase grk7a
- Genegrk7a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids549 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- ATP + L-threonyl-[rhodopsin] = ADP + H+ + O-phospho-L-threonyl-[rhodopsin]
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.4 μM | rhodopsin |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
773 nmol/min/mg |
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | photoreceptor activity | |
Molecular Function | rhodopsin kinase activity | |
Biological Process | cone photoresponse recovery | |
Biological Process | phototransduction, visible light | |
Biological Process | regulation of signal transduction | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRhodopsin kinase grk7a
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ49HM9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Impaired cone response recovery and delayed dark adaptation.
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412812 | 1-546 | Rhodopsin kinase grk7a | |||
Sequence: MCDMGGLDNLVANTAYLKAQGGDDKEMKKRRRSLSLPKPEQCASLRTSLDKDFESLCEKQPIGKKLFRQYLSQGGPECTTAAEFLDDLNEWELSESAARDKARTNIINKFCKEGSKSSLTFLTGDVATKCKAVSDKDFEEVMGQVKTATKEFLKGKPFTEYQASPFFDKFLQWKEYEKQPISEKYFYEFRTLGKGGFGEVCAVQVKNTGQMYACKKLCKKRLKKKHGEKMALLEKKILERVNSLFIVSLAYAYDTKTHLCLVMSLMNGGDLKYHIYNIGEKGIEMDRIIYYTAQIATGILHLHDMDIVYRDMKPENVLLDSQGQCRLSDLGLAVEIAVGKTISQKAGTGAYMAPEILNETPYRTSVDWWALGCSIYEMVAGYTPFKGPDAKKEKVEKEEVQRRILNEEPKFEHKNFDAATIDIIKQFLKKKIDERLGCKNDDPRKHEWFKSINFARLEAGLIDPPWVPKPNVVYAKDTGDIAEFSEIKGIEFDAKDDKFFKEFSTGAVSIAWQQEMIDTGLFDELSDPNRKESSGGSDDDKKSGTC | ||||||
Modified residue | 33 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 546 | Cysteine methyl ester | ||||
Sequence: C | ||||||
Lipidation | 546 | S-geranylgeranyl cysteine | ||||
Sequence: C | ||||||
Propeptide | PRO_0000412813 | 547-549 | Removed in mature form | |||
Sequence: TLL |
Post-translational modification
Phosphorylation at Ser-33 is regulated by light and activated by cAMP.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 53-171 | RGS | ||||
Sequence: FESLCEKQPIGKKLFRQYLSQGGPECTTAAEFLDDLNEWELSESAARDKARTNIINKFCKEGSKSSLTFLTGDVATKCKAVSDKDFEEVMGQVKTATKEFLKGKPFTEYQASPFFDKFL | ||||||
Domain | 186-449 | Protein kinase | ||||
Sequence: FYEFRTLGKGGFGEVCAVQVKNTGQMYACKKLCKKRLKKKHGEKMALLEKKILERVNSLFIVSLAYAYDTKTHLCLVMSLMNGGDLKYHIYNIGEKGIEMDRIIYYTAQIATGILHLHDMDIVYRDMKPENVLLDSQGQCRLSDLGLAVEIAVGKTISQKAGTGAYMAPEILNETPYRTSVDWWALGCSIYEMVAGYTPFKGPDAKKEKVEKEEVQRRILNEEPKFEHKNFDAATIDIIKQFLKKKIDERLGCKNDDPRKHEWF | ||||||
Domain | 450-515 | AGC-kinase C-terminal | ||||
Sequence: KSINFARLEAGLIDPPWVPKPNVVYAKDTGDIAEFSEIKGIEFDAKDDKFFKEFSTGAVSIAWQQE | ||||||
Region | 522-549 | Disordered | ||||
Sequence: FDELSDPNRKESSGGSDDDKKSGTCTLL | ||||||
Compositional bias | 524-539 | Basic and acidic residues | ||||
Sequence: ELSDPNRKESSGGSDD |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length549
- Mass (Da)62,232
- Last updated2011-09-21 v2
- Checksum3F76C291F8BC9716
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 80 | in Ref. 1; AAX69081 | ||||
Sequence: T → I | ||||||
Sequence conflict | 385 | in Ref. 1; AAX69081 | ||||
Sequence: F → I | ||||||
Compositional bias | 524-539 | Basic and acidic residues | ||||
Sequence: ELSDPNRKESSGGSDD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |