Recoverin Human

Recoverin was first identified in the late 1980s by researchers studying proteins involved in the visual process . It is encoded by the RCVRN gene in humans . The protein contains several calcium-binding sites of the EF-hand type, which are essential for its function . When recoverin binds calcium ions, it undergoes a conformational change that allows it to interact with target proteins or move to different regions within the cell .

Recoverin’s primary function is to inhibit rhodopsin kinase, an enzyme that regulates the phosphorylation of rhodopsin . This inhibition is crucial for controlling the life span of photoexcited rhodopsin, thereby prolonging light sensitivity . When calcium levels decrease in photoreceptors due to light exposure, the inhibition of rhodopsin kinase by calcium-bound recoverin is relieved, leading to a more rapid inactivation of metarhodopsin II (the activated form of rhodopsin) .

Recent studies have shown that recoverin also undergoes light-dependent intracellular translocation to rod synaptic terminals, enhancing signal transfer between rods and rod bipolar cells in the retina . This highlights its broader role in visual signal processing.

Human recombinant recoverin is produced using recombinant DNA technology, which involves inserting the human RCVRN gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant form is used in various research applications to study its structure, function, and potential therapeutic uses.