| IED ID | IndEnz0005001190 |
| Enzyme Type ID | lipase001190 |
| Protein Name |
1-acylglycerol-3-phosphate O-acyltransferase ABHD5 EC 2.3.1.51 Abhydrolase domain-containing protein 5 Lipid droplet-binding protein CGI-58 |
| Gene Name | ABHD5 NCIE2 CGI-58 |
| 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 | MAAEEEEVDSADTGERSGWLTGWLPTWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD |
| Enzyme Length | 349 |
| Uniprot Accession Number | Q8WTS1 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. {ECO:0000250|UniProtKB:Q9DBL9}. |
| 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:18606822};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000305|PubMed:18606822}; 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:18606822};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000305|PubMed:18606822}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:74544, ChEBI:CHEBI:74552; Evidence={ECO:0000269|PubMed:18606822};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148; Evidence={ECO:0000305|PubMed:18606822}; 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:18606822};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000305|PubMed:18606822}; 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:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37451, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:74544, ChEBI:CHEBI:74937; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74560, ChEBI:CHEBI:74565; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938, ChEBI:CHEBI:74941; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; |
| DNA Binding | |
| EC Number | 2.3.1.51 |
| Enzyme Function | FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid (PubMed:18606822). Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (PubMed:18606822). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:18832586). Regulates lipid droplet fusion (By similarity). {ECO:0000250|UniProtKB:Q9DBL9, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822, ECO:0000269|PubMed:18832586}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1); Natural variant (6); Sequence conflict (1) |
| Keywords | Acetylation;Acyltransferase;Cataract;Cytoplasm;Deafness;Differentiation;Disease variant;Fatty acid metabolism;Ichthyosis;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase |
| Interact With | Q5T4B2; P51793; Q8NI60; Q6ZPD8; Q05329; O00258; P48058-2; Q9NQG6; A6NKB5-5; Q99541; O60664; Q00G26; Q8N0V3; Q9Y225-2; Q9BVN2; Q9Y371; Q8N4M1-3; Q9NUH8; O43399; Q6PEW1 |
| Induction | INDUCTION: Up-regulated upon keratinocyte differentiation (at protein level). {ECO:0000269|PubMed:18832586}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832586}. Lipid droplet {ECO:0000250|UniProtKB:Q9DBL9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9DBL9}. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). {ECO:0000250}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22814378; MOD_RES 122; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6QA69 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15292255; 17308334; 17631826; 18339307; 19061969; 19401457; 20307695; 20370797; 20467438; 20520629; 20711500; 21122093; 21757733; 22245374; 22373837; 22383684; 23557589; 24879803; 25054327; 25315780; 25421061; 25482557; 25682902; 26350461; 26353074; 26547112; 27124600; 27559856; 28827091; 28877685; 29023646; 29026202; 29475365; 29843625; 30527376; 30842415; 30954460; 31439546; 31497752; 31742248; 32046372; 32107051; 32542055; 32705602; 33569812; 34449947; 34795238; |
| Motif | MOTIF 327..332; /note=HXXXXD motif |
| Gene Encoded By | |
| Mass | 39,096 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19709; RHEA:19710; RHEA:37143; RHEA:37144; RHEA:37147; RHEA:37148; RHEA:37131; RHEA:37132; RHEA:37443; RHEA:37444; RHEA:37451; RHEA:37452; RHEA:33187; RHEA:33188; RHEA:37163; RHEA:37164; RHEA:37455; RHEA:37456 |
| Cross Reference Brenda |