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 |