NameLecithin retinol acyltransferase
Synonyms
  • 2.3.1.135
  • Phosphatidylcholine--retinol O-acyltransferase
Gene NameLRAT
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010633|Lecithin retinol acyltransferase
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
Number of residues230
Molecular Weight25702.635
Theoretical pI7.54
GO Classification
Functions
  • retinol binding
  • retinoic acid binding
  • phosphatidylcholine-retinol O-acyltransferase activity
  • transferase activity, transferring acyl groups
Processes
  • phototransduction, visible light
  • retinoid metabolic process
  • vitamin A metabolic process
  • retinol metabolic process
  • retinoic acid metabolic process
  • positive regulation of lipid transport
  • visual perception
Components
  • perinuclear region of cytoplasm
  • rough endoplasmic reticulum
  • multivesicular body
  • endoplasmic reticulum membrane
  • integral component of membrane
General FunctionTransferase activity, transferring acyl groups
Specific FunctionTransfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments.
Pfam Domain Function
Transmembrane Regions195-215
GenBank Protein ID4240391
UniProtKB IDO95237
UniProtKB Entry NameLRAT_HUMAN
Cellular LocationEndoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0010634|Lecithin retinol acyltransferase (LRAT)
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCGAAGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGCACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
GenBank Gene IDAF071510
GeneCard IDNot Available
GenAtlas IDLRAT
HGNC IDHGNC:6685
Chromosome Location4
Locus4q32.1
References
  1. Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D: Molecular and biochemical characterization of lecithin retinol acyltransferase. J Biol Chem. 1999 Feb 5;274(6):3834-41. 9920938
  2. Zolfaghari R, Ross AC: Cloning, gene organization and identification of an alternative splicing process in lecithin:retinol acyltransferase cDNA from human liver. Gene. 2004 Oct 27;341:181-8. 15474300
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  5. Mondal MS, Ruiz A, Bok D, Rando RR: Lecithin retinol acyltransferase contains cysteine residues essential for catalysis. Biochemistry. 2000 May 2;39(17):5215-20. 10819989
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