Structural highlights
Function
[HRSL3_HUMAN] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.[1] [2]
References
- ↑ Nazarenko I, Schafer R, Sers C. Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells. J Cell Sci. 2007 Apr 15;120(Pt 8):1393-404. Epub 2007 Mar 20. PMID:17374643 doi:http://dx.doi.org/10.1242/jcs.000018
- ↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001