2.3.1.135	evolution	based on its secondary structure LRAT belongs to a superfamily of enzymes generically referred as NIpC/P60. Within this superfamily, a multiple sequence alignment of LRAT and LRAT-like family members shows that they share three conserved amino acid residues; cysteine, histidine and a polar residue that is thought to complete a catalytic triad similar to the papain-like thiol peptidases	719417	
2.3.1.135	malfunction	a truncated form of LRAT as well as its S175R mutant lead to retinis pigmentosa, a severe form of retinal dystrophy	719418	
2.3.1.135	malfunction	generation of an animal model in which the lrat gene is disrupted by homologous recombination gives Lrat-/- mice, which show slow degeneration of their retinas, essentially a shortening of rod outer segments and highly attenuated electroretinograms	719417	
2.3.1.135	malfunction	homozygous mutation S175R occurs in two patients diagnosed with severe early-onset retinal degeneration	719417	
2.3.1.135	malfunction	vitamin A uptake from recombinant holo-retinol-binding protein exhibited by wild-type mice is impaired in Lrat-deficient mice. Lrat-/- mice show elevated cellular vitamin A-binding protein 1, CRBP1, protein in the liver, lung, and adipose tissue as compared with wild type control animals	-, 720030	
2.3.1.135	metabolism	the key step of vitamin A metabolism is the esterification of all-trans retinol, catalyzed by lecithin/retinol acyltransferase, LRAT. Vitamin A metabolism in benign and malignant melanocytic skin cells with regard to expression, functional activity of LRAT, RPE65, and cRBP2 and their regulation, overview	715720	
2.3.1.135	additional information	malignant melanoma cells are able to esterify all-trans retinol and subsequently isomerize all-trans retinyl esters into 11-cis retinol, whereas their benign counterpart melanocytes are not able to catalyze these reactions	715720	
2.3.1.135	additional information	the catalytic triad includes histidine 60, tyrosine 154 and cysteine 161 in the LRAT structure	719418	
2.3.1.135	physiological function	activities of LRAT and RPE65 may be important for removal of all-trans retinal which is the substrate for retinoic acid production in skin cells. Decreasing cellular amount of retinoic acid and its precursor molecules might result in a change of gene regulation	715720	
2.3.1.135	physiological function	cellular retinol-binding protein CRBP I effectively conveys retinol to the LRAT, thereby circumventing the low enzymatic activity of LRAT in polar bear livers	758200