Detail Information for IndEnz0005001067
IED ID IndEnz0005001067
Enzyme Type ID lipase001067
Protein Name Phospholipase ABHD3
EC 3.1.1.32
EC 3.1.1.4
Abhydrolase domain-containing protein 3
Lung alpha/beta hydrolase 3
MmLABH3
Gene Name Abhd3 Labh3
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MQRLAMDLRVLSRELALYLEHQVRVGFFGSGVGLSLILGFSVAYACYYLSSIAKKPQLVIGGESFSRFLQDHCPVVTETYYPTVWCWESRGQTLLRPFITSKPPVQYRNELIKTADGGQISLDWFDNNNSAYYVDASTRPTILLLPGLTGTSKESYILHMIHLSEELGYRCVVFNNRGVAGESLLTPRTYCCANTEDLEAVVHHVHSLYPGAPFLAAGVSMGGMLLLNYLGKIGSKTPLMAAATFSVGWNTFACSESLERPLNWLLFNYYLTTCLQSSVKKHRHMFVEQIDMDQVMKAKSIREFDKRFTAVMFGYRTLDDYYTDASPNRRLKSVGIPVLCLNATDDVFSPSHAIPIETAKQNPNVALVLTAYGGHIGFLEGIWPRQCTYMDRVFKQFVQAMVEHGHELSNM
Enzyme Length 411
Uniprot Accession Number Q91ZH7
Absorption
Active Site ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 346; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 375; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:76084, ChEBI:CHEBI:86094; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54389; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:54392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:64489, ChEBI:CHEBI:86094; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54393; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:76079, ChEBI:CHEBI:86102; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54397; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:76085, ChEBI:CHEBI:86162; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54401; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54405; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:54408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:73858, ChEBI:CHEBI:75220; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54409; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54457; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate; Xref=Rhea:RHEA:54460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011, ChEBI:CHEBI:73858, ChEBI:CHEBI:138211; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54461; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexanoate; Xref=Rhea:RHEA:54464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:73858, ChEBI:CHEBI:138212; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54465; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + octanoate; Xref=Rhea:RHEA:54468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:73858, ChEBI:CHEBI:138213; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54469; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-nonanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanoate; Xref=Rhea:RHEA:54472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32361, ChEBI:CHEBI:73858, ChEBI:CHEBI:138214; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54473; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate; Xref=Rhea:RHEA:54552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:78208, ChEBI:CHEBI:138269; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54553; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate; Xref=Rhea:RHEA:41388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:78207, ChEBI:CHEBI:78208; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41389; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate + H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+); Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160; Evidence={ECO:0000305|PubMed:21926997}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:21926997};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000305|PubMed:21926997};
DNA Binding
EC Number 3.1.1.32; 3.1.1.4
Enzyme Function FUNCTION: Phospholipase that may play a role in phospholipids remodeling. May selectively cleave myristate (C14)-containing phosphatidylcholines through its predominant phospholipase 1 activity, cleaving preferentially acyl groups in sn1 position. In parallel, may have a minor phospholipase 2 activity acting on acyl groups in position sn2. In addition to (C14)-containing phosphatidylcholines, may also act on other medium-chain-containing and oxidatively truncated phospholipids. {ECO:0000269|PubMed:21926997}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Domain (1); Mutagenesis (1); Sequence conflict (2); Transmembrane (1)
Keywords Alternative splicing;Hydrolase;Lipid metabolism;Membrane;Phospholipid metabolism;Reference proteome;Serine esterase;Signal-anchor;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 21267068; 25391964;
Motif
Gene Encoded By
Mass 46,232
Kinetics
Metal Binding
Rhea ID RHEA:15801; RHEA:15802; RHEA:18689; RHEA:18690; RHEA:54388; RHEA:54389; RHEA:54392; RHEA:54393; RHEA:54396; RHEA:54397; RHEA:54400; RHEA:54401; RHEA:54404; RHEA:54405; RHEA:54408; RHEA:54409; RHEA:54456; RHEA:54457; RHEA:54460; RHEA:54461; RHEA:54464; RHEA:54465; RHEA:54468; RHEA:54469; RHEA:54472; RHEA:54473; RHEA:54552; RHEA:54553; RHEA:41388; RHEA:41389; RHEA:41179; RHEA:41180; RHEA:40483; RHEA:40484; RHEA:41159; RHEA:41160; RHEA:40479; RHEA:40480
Cross Reference Brenda