MBOAT5

LPCAT3
Identifiers
Aliases	LPCAT3, C3F, LPCAT, LPLAT 5, LPSAT, MBOAT5, OACT5, nessy, lysophosphatidylcholine acyltransferase 3
External IDs	OMIM: 611950 MGI: 1315211 HomoloGene: 14678 GeneCards: LPCAT3
EC number	2.3.1.23
Gene location (Human)
Chr.	Chromosome 12 (human)
End	7,018,477 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	124,681,381 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; right adrenal gland; ; body of stomach; ; rectum; ; left adrenal gland; ; body of pancreas; ; islet of Langerhans; ; upper lobe of left lung; ; minor salivary glands; ; right lung;
	Top expressed in
	yolk sac; ; lip; ; jejunum; ; duodenum; ; ileum; ; seminal vesicula; ; kidney; ; left lobe of liver; ; seminiferous tubule; ; parotid gland;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; 1-acylglycerophosphocholine O-acyltransferase activity; acyltransferase activity; 2-acylglycerol-3-phosphate O-acyltransferase activity; 1-acylglycerol-3-phosphate O-acyltransferase activity;
Cellular component	integral component of membrane; endoplasmic reticulum membrane; membrane; endoplasmic reticulum;
Biological process	phosphatidylserine acyl-chain remodeling; phosphatidylethanolamine acyl-chain remodeling; phosphatidylcholine acyl-chain remodeling; regulation of plasma lipoprotein particle levels; lipid metabolism; phospholipid biosynthetic process; phospholipid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	10162
	14792
	ENSG00000111684
	ENSMUSG00000004270
	Q6P1A2
	Q91V01
	NM_005768
	NM_145130
	NP_005759
	NP_660112
	Wikidata
View/Edit Human	View/Edit Mouse

Lysophospholipid acyltransferase 5 is an enzyme that in humans is encoded by the LPCAT3 gene.^[5]^[6]^[7]^[8] It is homologous to other membrane-bound O-acyltransferases.

Structure and function

Based on the crystalographic and cryo-EM studies of its homolog in chicken (cLPCAT3),^[9] humane MBOAT5 has a typical MBOAT folding as other members such as SOAT1 and DGAT1,^[10]^[11] and the transmembrane helices hold a "T"-shape reaction chamber allowing the co-occupancy of a lysophosphatidylcholine (lysoPC) and a long polyunsaturated acyl-CoA, such as arachidonic acyl CoA. With the assistance of catalytic residues H374 and N338, the acyl chain could be transferred from the acyl CoA to the sn-2 position of lysoPC, thereby generating a new, polyunsaturated phospholipid.

Inhibition of LPCAT3 has been found to alter the cellular lipidome and is partially protective against ferroptosis.^[12]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000111684 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000004270 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, et al. (April 1996). "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13". Genome Research. 6 (4): 314–326. doi:10.1101/gr.6.4.314. PMID 8723724.
^ Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA (March 1997). "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination". Genome Research. 7 (3): 268–280. doi:10.1101/gr.7.3.268. PMID 9074930.
^ Zhao Y, Chen YQ, Bonacci TM, Bredt DS, Li S, Bensch WR, et al. (March 2008). "Identification and characterization of a major liver lysophosphatidylcholine acyltransferase". The Journal of Biological Chemistry. 283 (13): 8258–8265. doi:10.1074/jbc.M710422200. PMID 18195019.
^ "Entrez Gene: MBOAT5 membrane bound O-acyltransferase domain containing 5".
^ Zhang Q, Yao D, Rao B, Jian L, Chen Y, Hu K, et al. (November 2021). "The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3". Nature Communications. 12 (1): 6869. Bibcode:2021NatCo..12.6869Z. doi:10.1038/s41467-021-27244-1. PMC 8617236. PMID 34824256.
^ Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, et al. (May 2020). "Structural basis for catalysis and substrate specificity of human ACAT1". Nature. 581 (7808): 333–338. Bibcode:2020Natur.581..333Q. doi:10.1038/s41586-020-2290-0. PMID 32433614. S2CID 214190451.
^ Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, et al. (May 2020). "Structure and mechanism of human diacylglycerol O-acyltransferase 1". Nature. 581 (7808): 329–332. Bibcode:2020Natur.581..329W. doi:10.1038/s41586-020-2280-2. PMC 7255049. PMID 32433610.
^ Reed A, Ichu TA, Milosevich N, Melillo B, Schafroth MA, Otsuka Y, et al. (June 2022). "LPCAT3 Inhibitors Remodel the Polyunsaturated Phospholipid Content of Human Cells and Protect from Ferroptosis". ACS Chemical Biology. 17 (6): 1607–1618. doi:10.1021/acschembio.2c00317. PMID 35658397. S2CID 249396449.

External links

LPCAT3 human gene location in the UCSC Genome Browser.
LPCAT3 human gene details in the UCSC Genome Browser.

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000111684 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000004270 – 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.

[pmid8723724-5] Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, et al. (April 1996). "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13". Genome Research. 6 (4): 314–326. doi:10.1101/gr.6.4.314. PMID 8723724.

[pmid9074930-6] Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA (March 1997). "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination". Genome Research. 7 (3): 268–280. doi:10.1101/gr.7.3.268. PMID 9074930.

[pmid18195019-7] Zhao Y, Chen YQ, Bonacci TM, Bredt DS, Li S, Bensch WR, et al. (March 2008). "Identification and characterization of a major liver lysophosphatidylcholine acyltransferase". The Journal of Biological Chemistry. 283 (13): 8258–8265. doi:10.1074/jbc.M710422200. PMID 18195019.

[entrez-8] "Entrez Gene: MBOAT5 membrane bound O-acyltransferase domain containing 5".

[9] Zhang Q, Yao D, Rao B, Jian L, Chen Y, Hu K, et al. (November 2021). "The structural basis for the phospholipid remodeling by lysophosphatidylcholine acyltransferase 3". Nature Communications. 12 (1): 6869. Bibcode:2021NatCo..12.6869Z. doi:10.1038/s41467-021-27244-1. PMC 8617236. PMID 34824256.

[10] Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, et al. (May 2020). "Structural basis for catalysis and substrate specificity of human ACAT1". Nature. 581 (7808): 333–338. Bibcode:2020Natur.581..333Q. doi:10.1038/s41586-020-2290-0. PMID 32433614. S2CID 214190451.

[11] Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, et al. (May 2020). "Structure and mechanism of human diacylglycerol O-acyltransferase 1". Nature. 581 (7808): 329–332. Bibcode:2020Natur.581..329W. doi:10.1038/s41586-020-2280-2. PMC 7255049. PMID 32433610.

[12] Reed A, Ichu TA, Milosevich N, Melillo B, Schafroth MA, Otsuka Y, et al. (June 2022). "LPCAT3 Inhibitors Remodel the Polyunsaturated Phospholipid Content of Human Cells and Protect from Ferroptosis". ACS Chemical Biology. 17 (6): 1607–1618. doi:10.1021/acschembio.2c00317. PMID 35658397. S2CID 249396449.

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MBOAT5

Structure and function

References

Further reading

External links

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MBOAT5

Structure and function

References

Further reading

External links

Navigation menu

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