Search by BoMiProt ID - Bomi186


Primary Information

BoMiProt ID Bomi186
Protein Name 1-acylglycerol-3-phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta)
Organism Bos taurus
Uniprot IdA6H7D4
Milk FractionMFGM, Exosome
Ref Sequence Id XP_005226162.1
Amino Acid Lenth 456
Molecular Weight 52065
Fasta Sequence https://www.uniprot.org/uniprot/A6H7D4.fasta
Gene Name AGPAT6
Gene Id 511614
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells expressed at very high levels in the liver and pancreas, at low levels in the placenta and certain regions of the brain, and at intermediate levels in numerous other tissues; LPAAT-ß is highly expressed in adipocytes
Protein Function Lysophosphatidic acid (LPA) is converted to phosphatidic acid by an LPA acyltransferase; modulates the intercellular signaling function of the LPA produced by activated cells or if it primarily serves to generate the PA intermediate in the membrane phospholipid synthetic pathway; mammary gland
Biochemical Properties Six human LPAAT isoforms (α–ζ) are detceted so far; LPAAT-α and LPAAT-ß showed differences in their preference for different acyl-CoAs; hydropathic profile of bovine LPAAT is identical to that of the human LPAAT alpha
Significance in milk Expressed in milk in response to various fatty acids; the expression of showed a significant positive correlation with diacylglycerol acyltransferase-1 in mammary gland tissue; LPAAT is a tissue-specific enzyme, and PKC site may be a signature of the mammary gland LPAAT - PKC site may be involved in a feedback signaling mechanism in the production of triglycerides during lactation
PTMs in humans, predicted N-glycosylation site (Asn-59) and O-glycosylation sites (Thr- 233, Thr-262; predicted protein kinase phosphorylation sites (Thr-174)
Bibliography 1. Mistry, D. H., & Medrano, J. F. (2002). Cloning and localization of the bovine and ovine lysophosphatidic acid acyltransferase (LPAAT) genes that codes for an enzyme involved in triglyceride biosynthesis. Journal of Dairy Science, 85(1), 28–35. https://doi.org/10.3168/jds.S0022-0302(02)74049-6.
2. Eberhardt, C., Gray, P. W., & Tjoelker, L. W. (1997). Human lysophosphatidic acid acyltransferase: cDNA cloning, expression, and localization to chromosome 9q34.3. Journal of Biological Chemistry, 272(32), 20299–20305. https://doi.org/10.1074/jbc.272.32.20299.
3. Hollenback, D., Bonham, L., Law, L., Rossnagle, E., Romero, L., Carew, H., … White, T. (2006). Substrate specificity of lysophosphatidic acid acyltransferase beta -- evidence from membrane and whole cell assays. Journal of Lipid Research, 47(3), 593–604. https://doi.org/10.1194/jlr.M500435-JLR200.
4. Sørensen, B. M., Chris Kazala, E., Murdoch, G. K., Keating, A. F., Cruz-Hernandez, C., Wegner, J., … Weselake, R. J. (2008). Effect of CLA and other C18 unsaturated fatty acids on DGAT in bovine milk fat biosynthetic systems. Lipids, 43(10), 903–912. https://doi.org/10.1007/s11745-008-3216-z.