Cellular retinaldehyde-binding protein (CRALBP) plays an important role in the regeneration of 11-cis-retinal for use in rod visual pigments such as opsin and rhodopsin. Once 11-cis-retinal is photoisomerized in the rod outer segment, it is converted to all-trans-retinal and further modified into all-trans-retinol. All-trans-retinol then diffuses into the retinal pigment epithelium (RPE) to be converted back to 11-cis-retinol and further oxidized into 11-cis-retinal (both by CRALBP). Genetic mutations involving CRALBP's lack of function have been linked to visual disease such as bothnia dystrophy, retinitis punctata albescens, retina pigmentosa, and Newfoundland rod-cone dystrophy. The presence of CRALBP serves as a marker for RPE and Muller glial cells of the retina.
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Protein Aliases: Atp1a1; ATPase, Na+/K+ transporting, alpha 1 polypeptide; ATPase, Na+K+ transporting, alpha 1; Na(+)/K(+) ATPase alpha-1 subunit; Na+/K+ ATPase 1; Na, K-ATPase, alpha-A catalytic polypeptide; Na,K-ATPase alpha-1 subunit; Na,K-ATPase catalytic subunit alpha-A protein; Sodium pump subunit alpha-1; sodium-potassium ATPase catalytic subunit alpha-1; sodium-potassium-ATPase, alpha 1 polypeptide; Sodium/potassium-transporting ATPase subunit alpha-1
Gene Aliases: ATP1A1; Atpa-1; BC010319; Nkaa1b