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InterPro: IPR002921 Lipase, class 3

Protein matches Help

UniProtKB

Matches:

1725 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

IPR002921 Lipase_3

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01764	Lipase_3	1725
Signatures in BioMart

GO Term annotation Help

Process

GO:0006629 lipid metabolic process

Function

GO:0004806 triglyceride lipase activity

InterPro annotation

Entry Details in BioMart

Abstract

Triglyceride lipases are lipolytic enzymes that hydrolyse ester linkages of triglycerides [1]. Lipases are widely distributed in animals, plants and prokaryotes. This family of lipases have been called Class 3 as they are not closely related to other lipase families.

Structural links Help

PDB - click here

SCOP: c.69.1.17

CATH: 3.40.50.1820

Database links Help

Enzyme: EC:3.1.1

PANDIT: PF01764

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

Example proteins Help

A6ZTP2 Putative lipase ATG15

Q680C0 GDSL esterase/lipase At4g10955

Q6WQJ1 Sn1-specific diacylglycerol lipase alpha

Q8NCG7 Sn1-specific diacylglycerol lipase beta

Q9XTR8 Lipase ZK262.3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002921	Lipase, class 3
	SWISS-MODEL
	ModBase

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

Additional Reading Open in usermanual
	McAuley KE, Svendsen A, Patkar SA, Wilson KS. Structure of a feruloyl esterase from Aspergillus niger. Acta Crystallogr. D Biol. Crystallogr. 60 2004 878-87 [PubMed: 15103133] http://dx.doi.org/10.1107/S0907444904004937
	Yapoudjian S, Ivanova MG, Brzozowski AM, Patkar SA, Vind J, Svendsen A, Verger R. Binding of Thermomyces (Humicola) lanuginosa lipase to the mixed micelles of cis-parinaric acid/NaTDC. Eur. J. Biochem. 269 2002 1613-21 [PubMed: 11895431] http://dx.doi.org/10.1046/j.1432-1327.2002.02786.x
	Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C. Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A. FEBS Lett. 580 2006 5815-21 [PubMed: 17027758] http://dx.doi.org/10.1016/j.febslet.2006.09.039
	Faulds CB, Molina R, Gonzalez R, Husband F, Juge N, Sanz-Aparicio J, Hermoso JA. Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger. FEBS J. 272 2005 4362-71 [PubMed: 16128806] http://dx.doi.org/10.1111/j.1742-4658.2005.04849.x
	Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB. The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family. J. Mol. Biol. 338 2004 495-506 [PubMed: 15081808] http://dx.doi.org/10.1016/j.jmb.2004.03.003

InterPro 23.1