rhodopsin kinase


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rho·dop·sin ki·nase

[MIM*180381]
an enzyme that regulates rhodopsin function by phosphorylating activated rhodopsin at a number of sites; phosphorylated photoactivated rhodopsin binds to arrestin.
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When we started studies on the phosphorylation of muscarinic receptors, rhodopsin and [beta] adrenergic receptors were known to be phosphorylated in a light- or agonist-dependent manner by rhodopsin kinase (GRK1 in the present terminology (91)) and [beta] adrenergic receptor kinase (OARK, GRK2 in the present terminology (92)), respectively, and these phosphorylations were reported to affect their function (see review ref.
GRK2 is homologous to rhodopsin kinase except that GRK2 has an extra C-terminal domain of approximately 130 amino acid residues.
In some mammals, as well as other animals, S-antigen, rhodopsin kinase and retinoid-binding protein have been located in pineal glands.