Aliases for PNLIPRP2 Gene
External Ids for PNLIPRP2 Gene
Previous GeneCards Identifiers for PNLIPRP2 Gene
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. [provided by RefSeq, Aug 2015]
GeneCards Summary for PNLIPRP2 Gene
PNLIPRP2 (Pancreatic Lipase Related Protein 2 (Gene/Pseudogene)) is a Protein Coding gene. Among its related pathways are Salivary secretion and Metabolism. Gene Ontology (GO) annotations related to this gene include calcium ion binding and phospholipase activity. An important paralog of this gene is PNLIP.
UniProtKB/Swiss-Prot Summary for PNLIPRP2 Gene
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 (By similarity). Has also low phospholipase activity, but its physiological relevance is not clear (PubMed:17401110, PubMed:18702514).