| IED ID | IndEnz0005000203 |
| Enzyme Type ID | lipase000203 |
| 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 Progesterone-sensitive lipase EC 3.1.1.79 Protein PHPS1-2 |
| Gene Name | ABHD2 LABH2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKKTYPLTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKLQCSDTEQVEADLE |
| Enzyme Length | 425 |
| Uniprot Accession Number | P08910 |
| 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:0000269|PubMed:26989199}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:0000269|PubMed:27247428};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000305|PubMed:27247428}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:26989199}; 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:0000269|PubMed:27247428};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:27247428}; 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:0000269|PubMed:26989199};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000305|PubMed:26989199}; 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:0000269|PubMed:27247428};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000305|PubMed:27247428}; 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:0000269|PubMed:27247428};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000305|PubMed:27247428}; |
| 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 (PubMed:26989199). 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) (PubMed:26989199). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester (PubMed:27247428). 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 (PubMed:26989199). May also play a role in smooth muscle cells migration (By similarity). {ECO:0000250|UniProtKB:Q9QXM0, ECO:0000269|PubMed:26989199, ECO:0000269|PubMed:27247428}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with p-nitrophenyl palmitate and 30 degrees Celsius with p-nitrophenyl acetate and p-nitrophenyl butyrate. {ECO:0000269|PubMed:27247428}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for p-nitrophenyl palmitate and 7.5 for p-nitrophenyl acetate and p-nitrophenyl butyrate. {ECO:0000269|PubMed:27247428}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (1); Natural variant (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cell projection;Cilium;Flagellum;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Serine esterase;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000305|PubMed:26989199}; Single-pass type II membrane protein {ECO:0000305}. Cell 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 | 17980156; 20007591; 25880496; 27323405; 28813576; 33648800; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,315 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.4 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:27247428}; KM=11.76 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:27247428}; KM=17.66 mM for p-nitrophenyl palmitate {ECO:0000269|PubMed:27247428}; Vmax=2.69 umol/sec/mg enzyme toward p-nitrophenyl acetate {ECO:0000269|PubMed:27247428}; Vmax=3.71 umol/sec/mg enzyme toward p-nitrophenyl butyrate {ECO:0000269|PubMed:27247428}; Vmax=1.27 umol/sec/mg enzyme toward p-nitrophenyl palmitate {ECO:0000269|PubMed:27247428}; |
| 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 |