Anti-PLA2G15

Protein function: Has dual calcium-independent phospholipase and O- acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:29724779, PubMed:25727495). Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity) (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:29724779, PubMed:25727495). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (PubMed:29724779). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines. Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (PubMed:29724779). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress (PubMed:30830753). Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance. At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (PubMed:10092508). [The UniProt Consortium]