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InterPro: IPR000734 Lipase

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UniProtKB

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999 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR000734 Lipase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00821	TAGLIPASE	710
PANTHER	PTHR11610	Lipase	992
Signatures in BioMart

InterPro Relationships Help

Children

IPR016272 Lipoprotein lipase, LIPH

Contains

IPR001024 Lipoxygenase, LH2
IPR002334 Dol/Ves 1 allergen
IPR013818 Lipase, N-terminal

GO Term annotation Help

Process

GO:0006629 lipid metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

Triglyceride lipases (EC:3.1.1.3) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [1]. 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) [2]. The most conserved region in all these proteins is centred around a serine residue which has been shown [3] 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) [4], which catalyses fatty acid transfer between phosphatidylcholine and cholesterol.

Structural links Help

PDB - click here

SCOP: b.12.1.2 , c.69.1.19

CATH: 2.60.60.20 , 3.40.50.1820

Database links Help

Enzyme: EC:3.1.1

Blocks: IPB000734

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000734

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2VBC4 Venom phospholipase A1

P00591 Pancreatic triacylglycerol lipase

P02843 Vitellogenin-1

P11152 Lipoprotein lipase

P16233 Pancreatic triacylglycerol lipase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002330	Lipoprotein lipase
IPR002331	Pancreatic lipase
IPR013818	Lipase, N-terminal
IPR002334	Dol/Ves 1 allergen
IPR001024	Lipoxygenase, LH2
IPR008976	Lipase/lipooxygenase, PLAT/LH2
IPR000734	Lipase
IPR016272	Lipoprotein lipase, LIPH
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Chapus C, Rovery M, Sarda L, Verger R. Minireview on pancreatic lipase and colipase. Biochimie 70 1223-34 1988 [PubMed: 3147715] http://dx.doi.org/10.1016/0300-9084(88)90188-5
2.	Persson B, Bengtsson-Olivecrona G, Enerback S, Olivecrona T, Jornvall H. Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase. Eur. J. Biochem. 179 39-45 1989 [PubMed: 2917565] http://dx.doi.org/10.1111/j.1432-1033.1989.tb14518.x
3.	Blow D. Enzymology. More of the catalytic triad. Nature 343 694-5 1990 [PubMed: 2304545] http://dx.doi.org/10.1038/343694a0
4.	McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R. Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc. Natl. Acad. Sci. U.S.A. 83 2335-9 1986 [PubMed: 3458198] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=3458198&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Winkler FK, D'Arcy A, Hunziker W. Structure of human pancreatic lipase. Nature 343 1990 771-4 [PubMed: 2106079] http://dx.doi.org/10.1038/343771a0
	Roussel A, de Caro J, Bezzine S, Gastinel L, de Caro A, Carriere F, Leydier S, Verger R, Cambillau C. Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations. Proteins 32 1998 523-31 [PubMed: 9726421] http://dx.doi.org/10.1002/(SICI)1097-0134(19980901)32:4<523::AID-PROT10>3.3.CO;2-9
	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 4 1996 1363-74 [PubMed: 8939760] http://dx.doi.org/10.1016/S0969-2126(96)00143-8
	Hermoso J, Pignol D, Kerfelec B, Crenon I, Chapus C, Fontecilla-Camps JC. Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J. Biol. Chem. 271 1996 18007-16 [PubMed: 8663362] http://dx.doi.org/10.1074/jbc.271.30.18007
	Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M. Structure and activity of rat pancreatic lipase-related protein 2. J. Biol. Chem. 273 1998 32121-8 [PubMed: 9822688] http://dx.doi.org/10.1074/jbc.273.48.32121
	Mancheno JM, Jayne S, Kerfelec B, Chapus C, Crenon I, Hermoso JA. Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement. Acta Crystallogr. D Biol. Crystallogr. 60 2004 2107-9 [PubMed: 15502342] http://dx.doi.org/10.1107/S0907444904024229

InterPro 23.1