PLA2G16 Protein, Human (His)

PLA2G16 protein exhibits a dual functionality, encompassing both phospholipase A1/2 and acyltransferase activities. As a phospholipase, it displays both calcium-independent PLA1 and PLA2 activities, efficiently releasing fatty acids from the sn-1 or sn-2 position of glycerophospholipids, with a notable prevalence of PLA1 activity. Additionally, PLA2G16 acts as an O-acyltransferase, facilitating the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid, and as an N-acyltransferase, catalyzing the calcium-independent transfer of a fatty acyl group from phosphatidylcholine and other glycerophospholipids to the primary amine of phosphatidylethanolamine. This process forms N-acylphosphatidylethanolamine, a precursor for N-acylethanolamines. Beyond its lipid-modifying enzymatic activities, PLA2G16 plays a crucial role in organelle rupture and degradation during eye lens terminal differentiation, contributing to lens transparency. Moreover, in the context of microbial infection, it acts as a host factor for picornaviruses, facilitating viral genome release into the cytoplasm during early infection and serving as a cellular sensor of membrane damage at virus entry sites. This multifaceted functionality underscores the diverse roles of PLA2G16 in cellular and infection-related processes.