IED Industry Enzyme Database

Detail Information for IndEnz0010000351
IED ID IndEnz0010000351
Enzyme Type ID esterase000351
Protein Name Lysophosphatidylserine lipase ABHD12
EC 3.1.1.-
2-arachidonoylglycerol hydrolase ABHD12
Abhydrolase domain-containing protein 12
Monoacylglycerol lipase ABHD12
EC 3.1.1.23
Oxidized phosphatidylserine lipase ABHD12
EC 3.1.-.-
Gene Name Abhd12
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 MRKRTEPVTLEHERCAASGSSSSGSAAAALDADCSLKQNLRLAGKGTAEPHSASDAGMKRALGRRKSLWFRLRKILLCVLGFYIAIPFLVKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEDDVTIGVWHTIPSVWWKNAQGKDQMWYEDALASNHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENMKHISCPLLILHAEDDPVVPFHLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPERQH
Enzyme Length 398
Uniprot Accession Number Q99LR1
Absorption
Active Site ACT_SITE 246; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q8N2K0; ACT_SITE 333; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0; ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0
Activity Regulation ACTIVITY REGULATION: Selectively inhibited by DO264 (N-3-pyridyl-N'-(1-[3-chloro-4-{2-chloro-4-(trifluoromethoxy)phenoxy}pyridine-2-yl]piperidin-4-yl)thiourea). {ECO:0000269|PubMed:30420694}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717, ChEBI:CHEBI:72828; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44585; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo-inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44589; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000269|PubMed:23297193}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) + hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64765, ChEBI:CHEBI:75020; Evidence={ECO:0000269|PubMed:23297193};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553; Evidence={ECO:0000269|PubMed:23297193}; 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:18096503};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:18096503}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:18096503}; CATALYTIC ACTIVITY: Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:30237167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:30237167}; CATALYTIC ACTIVITY: Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; Evidence={ECO:0000269|PubMed:30237167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; Evidence={ECO:0000269|PubMed:30237167}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:30237167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; Evidence={ECO:0000269|PubMed:30237167}; CATALYTIC ACTIVITY: Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629, ChEBI:CHEBI:75555; Evidence={ECO:0000269|PubMed:30237167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364; Evidence={ECO:0000269|PubMed:30237167}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, ChEBI:CHEBI:85195, ChEBI:CHEBI:143087; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, ChEBI:CHEBI:143088, ChEBI:CHEBI:143089; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020, ChEBI:CHEBI:143089, ChEBI:CHEBI:143094; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
DNA Binding
EC Number 3.1.1.-; 3.1.1.23; 3.1.-.-
Enzyme Function FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (PubMed:23297193, PubMed:25580854, PubMed:30420694). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (PubMed:23297193). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways (PubMed:18096503). Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (PubMed:30237167). {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:23297193, ECO:0000269|PubMed:25580854, ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30643283}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (1); Glycosylation (1); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Mitochondrion;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30237167}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:20657592}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:18096503}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10512203; 11217851; 12466851; 12904583; 14610273; 15010206; 15840001; 16615898; 20797687; 21267068; 22632720; 23806692; 25871848; 26779719; 27307232; 31213981; 32364701; 32462874;
Motif
Gene Encoded By
Mass 45,270
Kinetics
Metal Binding
Rhea ID RHEA:40499; RHEA:40500; RHEA:44584; RHEA:44585; RHEA:44588; RHEA:44589; RHEA:40895; RHEA:40896; RHEA:41091; RHEA:41092; RHEA:38491; RHEA:38492; RHEA:44552; RHEA:44553; RHEA:26132; RHEA:26133; RHEA:44320; RHEA:44316; RHEA:44312; RHEA:39963; RHEA:38487; RHEA:38488; RHEA:44732; RHEA:44728; RHEA:44729; RHEA:48428; RHEA:39959; RHEA:39960; RHEA:38363; RHEA:38364; RHEA:59364; RHEA:59368; RHEA:59372
Cross Reference Brenda