AGPAT1

From Wikipedia, the free encyclopedia

1-acylglycerol-3-phosphate O-acyltransferase 1 (lysophosphatidic acid acyltransferase, alpha)

Identifiers

AGPAT1; G15; 1-AGPAT1; LPAAT-alpha; LPAATA; MGC4007; MGC5423

External IDs

OMIM: 603099 MGI: 1932075 HomoloGene: 55973

Gene ontology
Molecular Function:	• 1-acylglycerol-3-phosphate O-acyltransferase activity • acyltransferase activity • transferase activity
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• phosphatidic acid biosynthetic process • metabolic process • phospholipid biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006411 (mRNA)
NP_006402 (protein)

NM_018862 (mRNA)
NP_061350 (protein)

Location

Chr 6: 32.24 - 32.25 Mb

Chr 17: 34.21 - 34.22 Mb

Pubmed search

[1]

[2]

1-acylglycerol-3-phosphate O-acyltransferase 1 (lysophosphatidic acid acyltransferase, alpha), also known as AGPAT1, is a human gene.^[1]

This gene encodes an enzyme that converts lysophosphatidic acid (LPA) into phosphatidic acid (PA). LPA and PA are two phospholipids involved in signal transduction and in lipid biosynthesis in cells. This enzyme localizes to the endoplasmic reticulum. This gene is located in the class III region of the human major histocompatibility complex. Alternative splicing results in two transcript variants encoding the same protein.^[1]

[edit] References

^ ^a ^b Entrez Gene: AGPAT1 1-acylglycerol-3-phosphate O-acyltransferase 1 (lysophosphatidic acid acyltransferase, alpha).

[edit] Further reading

Leung DW (2001). "The structure and functions of human lysophosphatidic acid acyltransferases.". Front. Biosci. 6: D944–53. PMID 11487472.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
West J, Tompkins CK, Balantac N, et al. (1997). "Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells.". DNA Cell Biol. 16 (6): 691–701. PMID 9212163.
Stamps AC, Elmore MA, Hill ME, et al. (1997). "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases.". Biochem. J. 326 ( Pt 2): 455–61. PMID 9291118.
Aguado B, Campbell RD (1998). "Human lysophosphatidic acid acyltransferase is encoded by a gene located in the major histocompatibility complex.". Biochem. Soc. Trans. 25 (4): S597. PMID 9450025.
Aguado B, Campbell RD (1998). "Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex.". J. Biol. Chem. 273 (7): 4096–105. PMID 9461603.
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. PMID 12477932.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Xie T, Rowen L, Aguado B, et al. (2004). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.". Genome Res. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMID 14656967.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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. PMID 15489334.
Servillo L, Balestrieri C, Giovane A, et al. (2006). "Lysophospholipid transacetylase in the regulation of PAF levels in human monocytes and macrophages.". FASEB J. 20 (7): 1015–7. doi:10.1096/fj.05-5059fje. PMID 16571775.
Lloyd EE, Gaubatz JW, Burns AR, Pownall HJ (2007). "Sustained elevations in NEFA induce cyclooxygenase-2 activity and potentiate THP-1 macrophage foam cell formation.". Atherosclerosis 192 (1): 49–55. doi:10.1016/j.atherosclerosis.2006.06.014. PMID 16870193.