EC Number   |
General Information |
Reference |
|---|
   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 | 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 | 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 | 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 |
| 2.3.1.135 | physiological function |
downregulation of LRAT expression in rat hepatic stellate cells is required for mobilization of retinyl ester in liver injury for tissue repair and wound healing, interleukin-1 is a potent suppressor of LRAT with a hierarchy role in the transcriptional regulation, interleukin-1 does not regulate the stability of LRAT protein. Interleukin-1 is a key mediator to down-regulate LRAT in liver injury |
720839 |
| 2.3.1.135 | physiological function |
function of LRAT is to catalyze a trans-esterification reaction that occurs between the sn-1 position of lecithin molecules in the lipid bilayer of the smooth endoplasmic reticulum and all-trans-retinol in the formation of all-trans-retinyl esters. Functional role of LRAT in the visual cycle |
719417 |
| 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 | physiological function |
lecithin:retinol acyltransferase is critical for cellular uptake of vitamin A from serum retinol-binding protein, which depends on functional coupling of STRA6 with intracellular lecithin:retinol acyltransferase. Vitamin A uptake is regulated by all-trans-retinoic acid in nonocular tissues of mice. When in excess, vitamin A is rapidly taken up and converted to its inert ester form in peripheral tissues, such as lung, whereas in vitamin A deficiency, ocular retinoid uptake is favored |
-, 720030 |
| 2.3.1.135 | physiological function |
lecithin:retinol acyltransferase, LRAT, is a membrane-bound protein that plays an essential function in the visual cycle. It catalyzes the esterification of retinol into retinyl esters in the retinal pigment epithelium as well as in other tissues including testis, liver, and intestine |
720353 |
