EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR013818 Lipase, N-terminal

Protein matches Help

UniProtKB

Matches:

984 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR013818 Lipase_N

Secondary

IPR000734

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00151	Lipase	984
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000734 Lipase
IPR002330 Lipoprotein lipase
IPR002331 Pancreatic lipase
IPR002333 Hepatic lipase
IPR016272 Lipoprotein lipase, LIPH

Contains

IPR002334 Dol/Ves 1 allergen

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 catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Structural links Help

PDB - click here

SCOP: c.69.1.19

CATH: 3.40.50.1820

Database links Help

Enzyme: EC:3.1.1

Pfam Clan: CL0028.18

AC	CL0028.18
ID	AB_hydrolase
DE	Alpha/Beta hydrolase fold
PF00135	IPR002018	Carboxylesterase, type B
PF00151	IPR013818	Lipase, N-terminal
PF00326	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain
PF00450	IPR001563	Peptidase S10, serine carboxypeptidase
PF00561	IPR000073	Alpha/beta hydrolase fold-1
PF00756	IPR000801	Putative esterase
PF00975	IPR001031	Thioesterase
PF01083	IPR000675	Cutinase
PF01674	IPR002918	Lipase, class 2
PF01738	IPR002925	Dienelactone hydrolase
PF01764	IPR002921	Lipase, class 3
PF02089	IPR002472	Palmitoyl protein thioesterase
PF02129	IPR000383	Peptidase S15
PF02230	IPR003140	Phospholipase/carboxylesterase
PF02273	IPR003157	Acyl transferase, bacterial
PF02450	IPR003386	Lecithin:cholesterol acyltransferase
PF03096	IPR004142	Ndr
PF03403	IPR005065	Platelet-activating factor acetylhydrolase, plasma/intracellular isoform II
PF03583	IPR005152	Lipase, secreted
PF03959	IPR005645	Protein of unknown function DUF341
PF04301	IPR007398	Protein of unknown function DUF452
PF05057	IPR007751	Protein of unknown function DUF676, hydrolase-like
PF05448	IPR008391	Acetyl xylan esterase
PF05576	IPR008761	Peptidase S37, tripeptidyl aminopeptidase
PF05577	IPR008758	Peptidase S28
PF05677	IPR008536	Protein of unknown function DUF818, Chlamydia
PF05705	IPR008547	Protein of unknown function DUF829, transmembrane 53
PF05728	IPR008886	Uncharacterised protein family UPF0227
PF05990	IPR010297	Protein of unknown function DUF900, hydrolase-like
PF06028	IPR010315	Protein of unknown function DUF915, hydrolase-like
PF06057	IPR010333	Bacterial virulence
PF06259	IPR010427	Protein of unknown function DUF1023
PF06342	IPR010463	Protein of unknown function DUF1057, lipase putative
PF06500	IPR010520	Protein of unknown function DUF1100, hydrolase-like
PF06821	IPR010662	Protein of unknown function DUF1234
PF06850	IPR009656	PHB de-polymerase, C-terminal
PF07082	IPR010765	Protein of unknown function DUF1350
PF07176	IPR010802	Protein of unknown function DUF1400, cynaobacterial
PF07224	IPR010821	Chlorophyllase
PF07519	IPR011118	Tannase/feruloyl esterase
PF07819	IPR012908	PGAP1-like
PF07859	IPR013094	Alpha/beta hydrolase fold-3
PF08386	IPR013595	Peptidase S33, tripeptidyl-peptidase C-terminal
PF08538	IPR013744	Protein of unknown function DUF1749
PF08840	IPR014940	BAAT/Acyl-CoA thioester hydrolase C-terminal
PF10503	IPR010126	Esterase, PHB depolymerase

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013818

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
	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