Hmdb loader
Identification
HMDB Protein ID HMDBP12107
Secondary Accession Numbers None
Name Pancreatic lipase-related protein 2
Synonyms
  1. PL-RP2
  2. Cytotoxic T lymphocyte lipase
  3. GPL
  4. Galactolipase
  5. Triacylglycerol lipase
Gene Name PNLIPRP2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229, PubMed:8939760). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short- medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8490016, PubMed:8939760). Can completely deacylates triacylglycerols (By similarity). 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:20083229, PubMed:8939760). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. 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 (By similarity).
Pathways
  • triacylglycerol degradation
Reactions Not Available
GO Classification
Biological Process
phospholipid catabolic process
galactolipid catabolic process
triglyceride catabolic process
lipid metabolic process
Cellular Component
extracellular space
membrane
Molecular Function
phospholipase activity
triglyceride lipase activity
galactolipase activity
1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity
acylglycerol lipase activity
calcium ion binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 47677.355
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P81139
UniProtKB/Swiss-Prot Entry Name LIPR2_CAVPO
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Hjorth A, Carriere F, Cudrey C, Woldike H, Boel E, Lawson DM, Ferrato F, Cambillau C, Dodson GG, Thim L, et al.: A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. Biochemistry. 1993 May 11;32(18):4702-7. doi: 10.1021/bi00069a003. [PubMed:8490016 ]
  2. Eydoux C, De Caro J, Ferrato F, Boullanger P, Lafont D, Laugier R, Carriere F, De Caro A: Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells. J Lipid Res. 2007 Jul;48(7):1539-49. doi: 10.1194/jlr.M600486-JLR200. Epub 2007 Mar 30. [PubMed:17401110 ]
  3. Amara S, Barouh N, Lecomte J, Lafont D, Robert S, Villeneuve P, De Caro A, Carriere F: Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2. Biochim Biophys Acta. 2010 Apr;1801(4):508-16. doi: 10.1016/j.bbalip.2010.01.003. Epub 2010 Jan 18. [PubMed:20083229 ]