| IED ID | IndEnz0005001351 |
| Enzyme Type ID | lipase001351 |
| 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 Protein CGI-58 |
| Gene Name | Abhd5 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MKAMAAEEEVDSADAGGGSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNGNSIWTLMFSHNMSSKTPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGGLHPDIPVSVIFGARSCIDGNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEICHTVD |
| Enzyme Length | 351 |
| Uniprot Accession Number | Q6QA69 |
| 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:0000250|UniProtKB:Q8WTS1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000250|UniProtKB:Q8WTS1}; 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:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; 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:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; 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:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; 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. 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 (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity). {ECO:0000250|UniProtKB:Q8WTS1, ECO:0000250|UniProtKB:Q9DBL9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Modified residue (1); Motif (1); Mutagenesis (3) |
| Keywords | Acyltransferase;Cytoplasm;Differentiation;Fatty acid metabolism;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Increased in the early stage of adipocyte differentiation. {ECO:0000269|PubMed:15136565}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15136565}. Lipid droplet {ECO:0000269|PubMed:15136565}. 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. |
| Modified Residue | MOD_RES 124; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 23398201; |
| Motif | MOTIF 329..334; /note=HXXXXD motif |
| Gene Encoded By | |
| Mass | 39,104 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19709; RHEA:19710; RHEA:37131; RHEA:37132; RHEA:37143; RHEA:37144; RHEA:37147; RHEA:37148; RHEA:37443; RHEA:37444; RHEA:37451; RHEA:37452; RHEA:33187; RHEA:33188; RHEA:37163; RHEA:37164; RHEA:37455; RHEA:37456 |
| Cross Reference Brenda |