Protein Domain : Hepatic lipase IPR002333

Type	Family
Description	Triglyceride lipases ( ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides []. Lipases are widely distributed inanimals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates: pancreatic, hepatic and gastric/lingual. Theselipases are closely related to each other and to lipoprotein lipase (), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [].Familial human hepatic lipase deficiency is a rare recessive disorder that results from mutation in position 405 of the mature protein. The disease ischaracterised by premature atherosclerosis and abnormal circulating lipoproteins [].The structure of the human hepatic triglyceride lipase gene has beendetermined [ ]. The hepatic lipase gene spans ~60 kb, and contains 8 intronsand 9 exons: exon 1 encodes the signal peptide; exon 4, a region that binds to the lipoprotein substrate; exon 5, an evolutionarily highly-conserved region of potential catalytic function; and exons 6 and 9 encode sequences rich in basic amino acids, thought to be important in anchoring the enzymeto the endothelial surface by interacting with acidic domains of surface glycosaminoglycans []. The human lipoprotein lipase gene has an identicalexon-intron organisation, with analogous structural domains, supporting the common evolutionary origin of these two lipolytic enzymes [].
Short Name	Lipase_hep