| Identification |
|---|
| HMDB Protein ID
| HMDBP12107 |
| Secondary Accession Numbers
| None |
| Name
| Pancreatic lipase-related protein 2 |
| Synonyms
|
- PL-RP2
- Cytotoxic T lymphocyte lipase
- GPL
- Galactolipase
- 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 |
| triglyceride catabolic process |
| lipid metabolic process |
| phospholipid catabolic process |
| galactolipid catabolic process |
| Cellular Component |
| extracellular space |
| membrane |
| Molecular Function |
| triglyceride lipase activity |
| acylglycerol lipase activity |
| calcium ion binding |
| phospholipase activity |
| galactolipase activity |
| 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity |
|
| 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
|
| External Links |
|---|
| 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
| - 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 ]
- 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 ]
- 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 ]
|
