SMART: Pfam domain Lipase

The domain within your query sequence starts at position 14 and ends at position 350; the E-value for the Lipase domain shown below is 1.1e-136.

CIFIQSSACGQGVGTEPFGRSLGATEASKPLKKPETRFLLFQDENDRLGCRLRPQHPETL
QECGFNSSQPLIMIIHGWSVDGLLENWIWKIVSALKSRQSQPVNVGLVDWISLAYQHYTI
AVQNTRIVGQDVAALLLWLEESAKFSRSKVHLIGYSLGAHVSGFAGSSMDGKNKIGRITG
LDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQP
GCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSDLQSIGFQCSDMGSFSQGL
CLSCKKGRCNTLGYDIRKDRSGKSKRLFLITRAQSPF

Lipase

PFAM accession number:	PF00151
Interpro abstract (IPR013818):	Triglyceride lipases ( EC 3.1.1.3 ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [ (PUBMED:3147715) ]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase ( EC 3.1.1.34 ), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [ (PUBMED:2917565) ]. The most conserved region in all these proteins is centred around a serine residue which has been shown [ (PUBMED:2304545) ] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase ( EC 2.3.1.43 ) (LCAT) [ (PUBMED:3458198) ], which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol. Lipoprotein lipases also exhibit homology with a region of Drosophila vitellogenins. That region, represented by this entry, is entirely within the N-terminal domain of lipoprotein lipase and constitutes the segment where the similarity to hepatic and pancreatic lipases is most pronounced [ (PUBMED:2917565) ].
GO function:	triglyceride lipase activity (GO:0004806)

PFAM accession number:

PF00151

Interpro abstract (IPR013818):

Triglyceride lipases ( EC 3.1.1.3 ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [ (PUBMED:3147715) ]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase ( EC 3.1.1.34 ), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [ (PUBMED:2917565) ]. The most conserved region in all these proteins is centred around a serine residue which has been shown [ (PUBMED:2304545) ] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase ( EC 2.3.1.43 ) (LCAT) [ (PUBMED:3458198) ], which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Lipoprotein lipases also exhibit homology with a region of Drosophila vitellogenins. That region, represented by this entry, is entirely within the N-terminal domain of lipoprotein lipase and constitutes the segment where the similarity to hepatic and pancreatic lipases is most pronounced [ (PUBMED:2917565) ].

GO function:

triglyceride lipase activity (GO:0004806)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lipase