| IED ID | IndEnz0010000406 |
| Enzyme Type ID | esterase000406 |
| Protein Name |
Monoacylglycerol lipase ABHD2 EC 3.1.1.23 2-arachidonoylglycerol hydrolase Abhydrolase domain-containing protein 2 Acetylesterase EC 3.1.1.6 Lung alpha/beta hydrolase 2 MmLABH2 Triacylglycerol lipase EC 3.1.1.79 |
| Gene Name | Abhd2 Labh-2 Labh2 |
| 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 | MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKRTYPQTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKSQCSDTEQMEAELE |
| Enzyme Length | 425 |
| Uniprot Accession Number | Q9QXM0 |
| Absorption | |
| Active Site | ACT_SITE 207; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q86WA6; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q86WA6; ACT_SITE 376; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q86WA6 |
| Activity Regulation | ACTIVITY REGULATION: Acylglycerol lipase activity is activated upon binding to progesterone. {ECO:0000250|UniProtKB:P08910}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P08910}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000250|UniProtKB:P08910};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000250|UniProtKB:P08910}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000250|UniProtKB:P08910};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P08910}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:P08910};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000250|UniProtKB:P08910}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000250|UniProtKB:P08910};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000250|UniProtKB:P08910}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000250|UniProtKB:P08910};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000250|UniProtKB:P08910}; |
| DNA Binding | |
| EC Number | 3.1.1.23; 3.1.1.6; 3.1.1.79 |
| Enzyme Function | FUNCTION: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester. Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation (By similarity). Involved in acrosomal reaction (Probable). May also play a role in smooth muscle cells migration (PubMed:15721306). {ECO:0000250|UniProtKB:P08910, ECO:0000269|PubMed:15721306, ECO:0000305|PubMed:26989199}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (2); Sequence conflict (3); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Serine esterase;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08910}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08910}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:26989199}. Note=Absent from the sperm flagellum. {ECO:0000269|PubMed:26989199}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 18799693; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,378 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12957; RHEA:12958; RHEA:12044; RHEA:12045; RHEA:26132; RHEA:26133; RHEA:47348; RHEA:47349; RHEA:47392; RHEA:47393 |
| Cross Reference Brenda |