Detail Information for IndEnz0010001246
IED ID IndEnz0010001246
Enzyme Type ID esterase001246
Protein Name Lysophosphatidylserine lipase ABHD12
EC 3.1.-.-
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 QtsA-16132
Organism Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
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 Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Macaca (macaques) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Enzyme Sequence MRKRTEPVALEHERCAAAGSSSSGSAAAALDADCRLKQNLRLTGTGAAEPRCAADAGMKRALGRRKGLWLRLRKILFCVLGLYIAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAVWWKNAQGKDQMWYEDALASSHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENVKHISCPLLILHAEDDPVVPFQLGRKLYSIAAPARSFRDFKVQFVPFHSDLGYRHKYIYKSPELPRILREFLGKSEPEHQH
Enzyme Length 398
Uniprot Accession Number Q4R766
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
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:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q99LR1}; 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:0000250|UniProtKB:Q99LR1}; 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:0000250|UniProtKB:Q99LR1}; 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:0000250|UniProtKB:Q99LR1}; 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:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q8N2K0}; 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:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q8N2K0}; 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:0000250|UniProtKB:Q8N2K0}; 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.-.-; 3.1.1.23
Enzyme Function FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity). {ECO:0000250|UniProtKB:Q8N2K0, ECO:0000250|UniProtKB:Q99LR1}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1)
Keywords Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,075
Kinetics
Metal Binding
Rhea ID RHEA:40499; RHEA:44584; RHEA:44588; RHEA:40895; RHEA:41091; RHEA:38491; RHEA:44552; RHEA:26132; RHEA:44320; RHEA:44316; RHEA:44312; RHEA:39963; RHEA:38487; RHEA:44732; RHEA:44728; RHEA:48428; RHEA:39959; RHEA:38363; RHEA:59364; RHEA:59368; RHEA:59372
Cross Reference Brenda