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lecithin retinol acyltransferase family protein
The full-length members of this family, eg Swiss:P53816, are representatives of a novel class II tumour-suppressor family, designated as H-REV107-like. This domain is the catalytic N-terminal proline-rich region of the protein. The downstream region is a putative C-terminal transmembrane domain which is found to be crucial for cellular localisation, but not necessary for the enzyme activity [1]. H-REV107-like proteins are homologous to lecithin retinol acyltransferase (LRAT), an enzyme that catalyses the transfer of the sn-1 acyl group of phosphatidylcholine to all-trans-retinol and forming a retinyl ester [2]. [1]. 20837014. Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain. Ren X, Lin J, Jin C, Xia B;. FEBS Lett. 2010;584:4222-4226. [2]. 3410848. Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine. MacDonald PN, Ong DE;. J Biol Chem. 1988;263:12478-12482. (from Pfam)
lecithin retinol acyltransferase family protein which may catalyze transacylation and/or phospholipase (PL)A1/2-type hydrolysis of glycerophospholipids
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