Lecithin Retinol Acyltransferase (LRAT)

Phosphatidylcholine--Retinol O-Acyltransferase

Lecithin Retinol Acyltransferase (LRAT)
Lecithin Retinol Acyltransferase is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester, an essential reaction for the retinoid cycle in visual system and vitamin A status in liver. Mutations in this gene have been associated with early-onset severe retinal dystrophy.
The predicted 230-amino acid human LRAT protein contains 2 putative transmembrane domains. Western blot analysis detected an approximately 25- to 26-kD LRAT protein in human RPE cells; the calculated molecular mass of LRAT is 25.3 kD. Northern blot analysis detected a major 5.0-kb LRAT transcript in several human tissues, particularly those known for their high vitamin A-processing activity. In fetal tissues, LRAT was expressed in the RPE and liver, and slightly in brain.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)