| 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 |