Detail Information for IndEnz0005001071
IED ID IndEnz0005001071
Enzyme Type ID lipase001071
Protein Name Phosphatidylserine lipase ABHD16A
EC 3.1.-.-
Alpha/beta hydrolase domain-containing protein 16A
Abhydrolase domain-containing protein 16A
HLA-B-associated transcript 5
hBAT5
Monoacylglycerol lipase ABHD16A
EC 3.1.1.23
Protein G5
Gene Name ABHD16A BAT5 G5 NG26 PP199
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 MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIIIYAWSIGGFTATWAAMSYPDVSAMILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTKDEIITTTVPEDIMSNRGNDLLLKLLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPDFPWSVGEDMSADGRRQLALFLARKHLHNFEATHCTPLPAQNFQMPWHL
Enzyme Length 558
Uniprot Accession Number O95870
Absorption
Active Site ACT_SITE 355; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0; ACT_SITE 430; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0; ACT_SITE 507; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8N2K0
Activity Regulation ACTIVITY REGULATION: Inhibited by beta-lactone-based lipid inhibitors, such as beta-lactone palmostatin-B. {ECO:0000269|PubMed:25290914}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:84466, ChEBI:CHEBI:84467; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72833, ChEBI:CHEBI:72837; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:25290914}; 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:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; Evidence={ECO:0000269|PubMed:25290914}; 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:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000269|PubMed:25290914}; 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:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:25290914}; 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:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000269|PubMed:25290914}; 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:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; Evidence={ECO:0000269|PubMed:25290914}; 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:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; Evidence={ECO:0000269|PubMed:25290914}; 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:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) + prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406, ChEBI:CHEBI:85232; Evidence={ECO:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45413; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy-Delta(12,14)-prostaglandin J2 + glycerol + H(+); Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238; Evidence={ECO:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45417; Evidence={ECO:0000269|PubMed:25290914}; 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:0000269|PubMed:25290914};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; Evidence={ECO:0000269|PubMed:25290914};
DNA Binding
EC Number 3.1.-.-; 3.1.1.23
Enzyme Function FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS) (By similarity). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (PubMed:25290914). Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (PubMed:25290914). {ECO:0000250|UniProtKB:Q9Z1Q2, ECO:0000269|PubMed:25290914}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-8.0. {ECO:0000269|PubMed:25290914};
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Domain (1); Sequence conflict (1); Topological domain (1); Transmembrane (2)
Keywords Alternative splicing;Direct protein sequencing;Hydrolase;Lipid metabolism;Membrane;Reference proteome;Transmembrane;Transmembrane helix
Interact With Q9NRZ7; Q13520; Q6P5T0; P18859; O95415; Q8N350-4; Q9UHD4; P05177; Q86UW9; Q15125; Q9Y282; P14324; Q9Y680; Q8TB36; P36382; Q6ZVE7; Q5T7V8; Q8TDT2; P04921; Q7Z5P4; Q01628; P11215; P01374; Q96FX8; Q99640-2; Q07864; O60831; Q86VR2; Q6NTF9-3; O75783; Q99942; O75396; O75920; Q14973; Q9BRI3; Q9UHI5; Q9NPE6; Q9H169-2; P61266; Q96DZ7; Q8IV31; Q96AN5; Q9BVK8; Q9NUH8; Q96Q45-2; Q6PI78; O60636; Q86WB7-2; O95183; Q3ZAQ7; Q9NX94; P0DTC6
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi-pass membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14667819; 15231747; 18835879; 19115949; 19116923; 19423540; 19851445; 20406964; 20438785; 20626023; 20706999; 21044367; 21516116; 25416956; 26496610; 29794032; 32462874; 33763481; 34587489;
Motif
Gene Encoded By
Mass 63,243
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in absence of BSA) {ECO:0000269|PubMed:25290914}; KM=137.8 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in presence of BSA) {ECO:0000269|PubMed:25290914}; KM=20.9 uM for 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (in presence of BSA) {ECO:0000269|PubMed:25290914}; Vmax=7.3 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) as substrate (in absence of BSA) {ECO:0000269|PubMed:25290914}; Vmax=13.2 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) as substrate (in presence of BSA) {ECO:0000269|PubMed:25290914};
Metal Binding
Rhea ID RHEA:44500; RHEA:41752; RHEA:44516; RHEA:44520; RHEA:44524; RHEA:44528; RHEA:44540; RHEA:40919; RHEA:44312; RHEA:44313; RHEA:39963; RHEA:39964; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492; RHEA:44732; RHEA:44733; RHEA:44728; RHEA:44729; RHEA:26132; RHEA:26133; RHEA:45412; RHEA:45413; RHEA:45416; RHEA:45417; RHEA:48428; RHEA:48429
Cross Reference Brenda