| IED ID | IndEnz0005000635 |
| Enzyme Type ID | lipase000635 |
| Protein Name |
1-acylglycerol-3-phosphate O-acyltransferase Pnpla3 EC 2.3.1.51 Acylglycerol transacylase Adiponutrin ADPN Calcium-independent phospholipase A2-epsilon iPLA2-epsilon Lysophosphatidic acid acyltransferase Patatin-like phospholipase domain-containing protein 3 EC 3.1.1.3 |
| Gene Name | Pnpla3 Adpn |
| 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 | MYDPERRWSLSFAGCGFLGFYHVGATLCLSERAPHLLRDARTFFGCSAGALHAVTFVCSLPLGRIMEILMDLVRKARSRNIGTLHPFFNINKCIRDGLQESLPDNVHQVISGKVHISLTRVSDGENVLVSEFHSKDEVVDALVCSCFIPLFSGLIPPSFRGERYVDGGVSDNVPVLDAKTTITVSPFYGEHDICPKVKSTNFFHVNITNLSLRLCTGNLQLLTRALFPSDVKVMGELCYQGYLDAFRFLEENGICNGPQRSLSLSLVAPEACLENGKLVGDKVPVSLCFTDENIWETLSPELSTALSEAIKDREGYLSKVCNLLPVRILSYIMLPCSLPVESAIAAVHRLVTWLPDIQDDIQWLQWATSQVCARMTMCLLPSTRSRASKDDHRMLKHGHHPSPHKPQGNSAGL |
| Enzyme Length | 413 |
| Uniprot Accession Number | Q91WW7 |
| Absorption | |
| Active Site | ACT_SITE 47; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 166; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000269|PubMed:22560221}; 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=3.1.1.3; Evidence={ECO:0000269|PubMed:22560221}; CATALYTIC ACTIVITY: Reaction=a 1,3-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44440, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:47777; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44436, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=2 a 1-acylglycerol = a 1,2-diacylglycerol + glycerol; Xref=Rhea:RHEA:44432, ChEBI:CHEBI:17754, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:22560221};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000305|PubMed:22560221}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74544, ChEBI:CHEBI:74551; Evidence={ECO:0000269|PubMed:22560221};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000305|PubMed:22560221}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563; Evidence={ECO:0000269|PubMed:22560221};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160; Evidence={ECO:0000305|PubMed:22560221}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544, ChEBI:CHEBI:74928; Evidence={ECO:0000269|PubMed:22560221};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence={ECO:0000305|PubMed:22560221}; CATALYTIC ACTIVITY: Reaction=2 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38323, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q9NST1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38327, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q9NST1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38331, ChEBI:CHEBI:17754, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q9NST1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332; Evidence={ECO:0000250|UniProtKB:Q9NST1}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,3-di-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q9NST1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388; Evidence={ECO:0000250|UniProtKB:Q9NST1}; |
| DNA Binding | |
| EC Number | 2.3.1.51; 3.1.1.3 |
| Enzyme Function | FUNCTION: Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA (PubMed:22560221). Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides (By similarity). Has hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety (By similarity). {ECO:0000250|UniProtKB:Q9NST1, ECO:0000269|PubMed:22560221}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism. {ECO:0000269|PubMed:22560221}.; PATHWAY: Glycerolipid metabolism. {ECO:0000269|PubMed:22560221}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (2); Motif (3); Mutagenesis (1); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;Glycoprotein;Hydrolase;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to high-sucrose diet. {ECO:0000269|PubMed:22560221}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11431482, ECO:0000269|PubMed:22560221}; Single-pass membrane protein {ECO:0000269|PubMed:11431482}. Lipid droplet {ECO:0000269|PubMed:22560221}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16141072; 16380488; 20015565; 20648554; 21068004; 21145868; 21267068; 21677750; 23023705; 24114809; 24917523; 27180240; 28433418; 28520213; 29555681; 30272815; 30447270; 30772256; 31019090; 33347955; 33672787; |
| Motif | MOTIF 14..19; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 45..49; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 166..168; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 45,772 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.46 uM for oleoyl-CoA {ECO:0000269|PubMed:22560221}; Vmax=3.41 nmol/min/mg enzyme with oleoyl-CoA as acyl donor and 1-oleoyl-sn-glycero-3-phosphate as acyl acceptor {ECO:0000269|PubMed:22560221}; |
| Metal Binding | |
| Rhea ID | RHEA:19709; RHEA:12044; RHEA:44440; RHEA:44436; RHEA:44432; RHEA:37131; RHEA:37132; RHEA:37143; RHEA:37144; RHEA:37159; RHEA:37160; RHEA:37443; RHEA:37444; RHEA:38323; RHEA:38324; RHEA:38327; RHEA:38328; RHEA:38331; RHEA:38332; RHEA:38387; RHEA:38388 |
| Cross Reference Brenda |