Domain

Lipase/vitellogenin (IPR013818)

Short name: Lipase/vitellogenin

Domain relationships

Description

Triglyceride lipases (EC:3.1.1.3) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [PMID: 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) [PMID: 2917565]. The most conserved region in all these proteins is centred around a serine residue which has been shown [PMID: 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) [PMID: 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 [PMID: 2917565].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam