1gpl is a 1 chain structure with sequence from Cavia porcellus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
LIPP_HUMANLIPR2_CAVPO 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 deacylate triacylglycerols (By similarity). 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: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). Also has low phospholipase activity (By similarity). 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).[UniProtKB:P17892][UniProtKB:P54317][UniProtKB:P54318][1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Eydoux C, De Caro J, Ferrato F, Boullanger P, Lafont D, Laugier R, Carrière 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. PMID:17401110 doi:10.1194/jlr.M600486-JLR200
↑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. PMID:20083229 doi:https://dx.doi.org/10.1016/j.bbalip.2010.01.003
↑Hjorth A, Carrière F, Cudrey C, Wöldike 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. PMID:8490016 doi:10.1021/bi00069a003
↑Withers-Martinez C, Carriere F, Verger R, Bourgeois D, Cambillau C. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure. 1996 Nov 15;4(11):1363-74. PMID:8939760
