PNLIPRP2

PNLIPRP2 is 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.

Full Name

pancreatic lipase-related protein 2

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 deacylate triacylglycerols (PubMed:21865348).
When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a 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).
Also has low phospholipase activity (PubMed:17401110, PubMed:18702514).
In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity).
The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).

Biological Process

Galactolipid catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Lipid catabolic processManual Assertion Based On ExperimentIBA:GO_Central
Lipid digestionTAS:Reactome
Phosphatidylcholine catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Phospholipid catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Triglyceride catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Triglyceride metabolic processManual Assertion Based On ExperimentTAS:ProtInc

Cellular Location

Secreted
Zymogen granule membrane
Cell projection, neuron projection
Localizes to neurite tips in neuronal cells.