Anti-PNLIPRP2

This gene encodes a lipase that hydrolyzes galactolipids, the main components of plant membrane lipids. An allelic polymorphism in this gene results in both coding and non-coding variants, the reference genome represents the non-coding allele. Protein function: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:15287741, PubMed:17401110, PubMed:19451396, PubMed:21865348, PubMed:20083229, PubMed:26494624, PubMed:18702514). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long- chain triglycerides (PubMed:23732775, PubMed:19824014, PubMed:21652702). Hydrolyzes short- medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:15287741, PubMed:17401110, PubMed:21865348, PubMed:21652702, PubMed:18702514). Can completely deacylates triacylglycerols (PubMed:21865348). When liver matures and bile salt synthesis increases, it likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in plant-based diet releasing long-chain polyunsaturated fatty acids (PubMed:15287741, PubMed:17401110, PubMed:20083229, PubMed:26494624, PubMed:18702514). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:20083229, PubMed:18702514). May act together with LIPF to hydrolyze partially digested triglycerides (PubMed:23732775). Hydrolyzes long-chain monoglycerides with high efficiency (PubMed:17401110, PubMed:21652702, PubMed:23732775). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity. Has also low phospholipase activity, but its physiological relevance is not clear (PubMed:17401110, PubMed:18702514). [The UniProt Consortium]