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Lecithin retinol acyltransferase (LRAT) is a membrane bound enzyme that catalyzes the transfer of an acyl group from the sn-1 position of lecithin to vitamin A which generates all-trans-retinyl esters (tREs) in the liver, some extrahepatic tissues, such as the lung, and retinal pigmented epithelium. LRAT can also exchange palmitoyl groups between RPE65, a tRE binding protein essential for vision, and tREs, which is important for the operation of the visual pathway. LRAT is essential for the dietary mobilization, transport, and storage of vitamin A as well as the synthesis of the visual pigment chromophore. LRAT monomers interact in membranes to form homodimers through disulfide bond formation. A loss of LRAT correlates with an early onset severe retinal dystrophy and severe retinyl ester deprivation, while a reduction in LRAT expression may be associated with invasive bladder cancer.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Lecithin retinol acyltransferase; Phosphatidylcholine--retinol O-acyltransferase
Gene Aliases: LCA14; LRAT
UniProt ID: (Human) O95237
Entrez Gene ID: (Human) 9227
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