Lecithin retinol acyltransferase

Lecithin retinol acyltransferase is an enzyme that in humans is encoded by the LRAT gene.[5][6]

LRAT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4Q95
Identifiers
Aliases	LRAT, LCA14, lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase), lecithin retinol acyltransferase
External IDs	OMIM: 604863 MGI: 1891259 HomoloGene: 3483 GeneCards: LRAT
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q32.1 Start 154,626,945 bp[1] End 154,753,120 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 E3 Start 82,892,579 bp[2] End 82,903,973 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity, transferring acyl groups • retinol binding • O-acyltransferase activity • transferase activity • retinoic acid binding • lecithin:11-cis retinol acyltransferase activity • O-palmitoyltransferase activity • phosphatidylcholine-retinol O-acyltransferase activity Cellular component • endoplasmic reticulum • cytoplasm • endosome • integral component of membrane • membrane • intracellular membrane-bounded organelle • endoplasmic reticulum membrane • multivesicular body • rough endoplasmic reticulum • perinuclear region of cytoplasm Biological process • vitamin A metabolic process • visual perception • retinoid metabolic process • response to stimulus • positive regulation of lipid transport • cellular response to leukemia inhibitory factor • retinol metabolic process • response to retinoic acid • response to vitamin A • response to bacterium Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9227	79235
Ensembl	ENSG00000121207	ENSMUSG00000028003
UniProt	O95237	Q9JI60
RefSeq (mRNA)	NM_001301645 NM_004744	NM_023624
RefSeq (protein)	NP_001288574 NP_004735	NP_076113
Location (UCSC)	Chr 4: 154.63 – 154.75 Mb	Chr 3: 82.89 – 82.9 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Lecithin retinol acyltransferase is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester during phototransduction, an essential reaction for the retinoid cycle in visual system and vitamin A status in liver.

Clinical significance

Mutations in this gene have been associated with early-onset severe retinal dystrophy.[6]

LRAT was overexpressed in colorectal cancer cells compared to normal colonic epithelium. Strong LRAT expression was associated with a poor prognosis in patients with colorectal cancer.[7]

See also

• The Visual Cycle

References

1. GRCh38: Ensembl release 89: ENSG00000121207 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028003 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D (Feb 1999). "Molecular and biochemical characterization of lecithin retinol acyltransferase". J Biol Chem. 274 (6): 3834–41. doi:10.1074/jbc.274.6.3834. PMID 9920938.
6. "Entrez Gene: LRAT lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase)".
7. Brown, Gordon; Beatriz Cash; Daniela Blihoghe; Petronella Johansson; Ayham Alnabulsi; Graeme Murray (2014-03-07). "The Expression and Prognostic Significance of Retinoic Acid Metabolising Enzymes in Colorectal Cancer". PLOS ONE. 9 (3): e90776. doi:10.1371/journal.pone.0090776. PMC 3946526. PMID 24608339.

Further reading

• Ross AC, Zolfaghari R (2004). "Regulation of hepatic retinol metabolism: perspectives from studies on vitamin A status". J. Nutr. 134 (1): 269S–275S. doi:10.1093/jn/134.1.269S. PMID 14704332.
• Herr FM, Ong DE (1992). "Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins". Biochemistry. 31 (29): 6748–55. doi:10.1021/bi00144a014. PMID 1322170.
• Mata NL, Tsin AT (1998). "Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes". Biochim. Biophys. Acta. 1394 (1): 16–22. doi:10.1016/s0005-2760(98)00078-2. PMID 9767084.
• Mondal MS, Ruiz A, Bok D, Rando RR (2000). "Lecithin retinol acyltransferase contains cysteine residues essential for catalysis". Biochemistry. 39 (17): 5215–20. doi:10.1021/bi9929554. PMID 10819989.
• Ruiz A, Kuehn MH, Andorf JL, et al. (2001). "Genomic organization and mutation analysis of the gene encoding lecithin retinol acyltransferase in human retinal pigment epithelium". Invest. Ophthalmol. Vis. Sci. 42 (1): 31–7. PMID 11133845.
• Andreola F, Giandomenico V, Spero R, De Luca LM (2001). "Expression of a smaller lecithin:retinol acyl transferase transcript and reduced retinol esterification in MCF-7 cells". Biochem. Biophys. Res. Commun. 279 (3): 920–4. doi:10.1006/bbrc.2000.3995. PMID 11162450.
• Thompson DA, Li Y, McHenry CL, et al. (2001). "Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy". Nat. Genet. 28 (2): 123–4. doi:10.1038/88828. PMID 11381255. S2CID 19391022.
• Jahng WJ, Cheung E, Rando RR (2002). "Lecithin retinol acyltransferase forms functional homodimers". Biochemistry. 41 (20): 6311–9. doi:10.1021/bi015710b. PMC 5503676. PMID 12009892.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Zhan HC, Gudas LJ, Bok D, et al. (2004). "Differential expression of the enzyme that esterifies retinol, lecithin:retinol acyltransferase, in subtypes of human renal cancer and normal kidney". Clin. Cancer Res. 9 (13): 4897–905. PMID 14581364.
• Jahng WJ, Xue L, Rando RR (2004). "Lecithin retinol acyltransferase is a founder member of a novel family of enzymes". Biochemistry. 42 (44): 12805–12. doi:10.1021/bi035370p. PMC 5511752. PMID 14596594.
• Boorjian S, Tickoo SK, Mongan NP, et al. (2004). "Reduced lecithin: retinol acyltransferase expression correlates with increased pathologic tumor stage in bladder cancer". Clin. Cancer Res. 10 (10): 3429–37. doi:10.1158/1078-0432.CCR-03-0756. PMID 15161698.
• Zolfaghari R, Ross AC (2005). "Cloning, gene organization and identification of an alternative splicing process in lecithin:retinol acyltransferase cDNA from human liver". Gene. 341: 181–8. doi:10.1016/j.gene.2004.06.043. PMC 3843125. PMID 15474300.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• O'Byrne SM, Wongsiriroj N, Libien J, et al. (2005). "Retinoid absorption and storage is impaired in mice lacking lecithin:retinol acyltransferase (LRAT)". J. Biol. Chem. 280 (42): 35647–57. doi:10.1074/jbc.M507924200. PMC 1352312. PMID 16115871.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Xue L, Jahng WJ, Gollapalli D, Rando RR (2006). "Palmitoyl transferase activity of lecithin retinol acyl transferase". Biochemistry. 45 (35): 10710–8. doi:10.1021/bi060897y. PMC 2529161. PMID 16939223.
• Sénéchal A, Humbert G, Surget MO, et al. (2006). "Screening genes of the retinoid metabolism: novel LRAT mutation in leber congenital amaurosis". Am. J. Ophthalmol. 142 (4): 702–4. doi:10.1016/j.ajo.2006.04.057. PMID 17011878.

External links

• GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview