|Protein Name||1-acylglycerol-3-phosphate O-acyltransferase 6 (Lysophosphatidic acid acyltransferase, zeta)|
|Milk Fraction||MFGM, Exosome|
|Ref Sequence ID||XP_005226162.1|
|Protein Existence Status||Unreviewed: Experimental evidence at transcript level|
|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)|
| Site(s) of PTM(s) |
|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.