IED ID | IndEnz0005000568 |
Enzyme Type ID | lipase000568 |
Protein Name |
Diacylglycerol O-acyltransferase 2 EC 2.3.1.20 Acyl-CoA retinol O-fatty-acyltransferase ARAT Retinol O-fatty-acyltransferase EC 2.3.1.76 Diglyceride acyltransferase 2 |
Gene Name | Dgat2 |
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 | MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLKNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHAMYMEALVKLFDNHKTKFGLPETEVLEVN |
Enzyme Length | 388 |
Uniprot Accession Number | Q9DCV3 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by niacin. {ECO:0000250}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:15834126, ECO:0000269|PubMed:16106050};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76;PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75583; Evidence={ECO:0000269|PubMed:15834126, ECO:0000269|PubMed:16106050};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164; Evidence={ECO:0000269|PubMed:15834126, ECO:0000305|PubMed:16106050}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:21680734, ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; Evidence={ECO:0000305|PubMed:21680734, ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75735; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75824; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:73990, ChEBI:CHEBI:75466; Evidence={ECO:0000269|PubMed:15834126};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; Evidence={ECO:0000305|PubMed:15834126}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q96PD7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; Evidence={ECO:0000250|UniProtKB:Q96PD7}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000250|UniProtKB:Q96PD7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; Evidence={ECO:0000250|UniProtKB:Q96PD7}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:138734; Evidence={ECO:0000250|UniProtKB:Q96PD7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; Evidence={ECO:0000250|UniProtKB:Q96PD7}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q96PD7};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; Evidence={ECO:0000250|UniProtKB:Q96PD7}; |
DNA Binding | |
EC Number | 2.3.1.20; 2.3.1.76 |
Enzyme Function | FUNCTION: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q96PD7, ECO:0000269|PubMed:11481335, ECO:0000269|PubMed:15797871, ECO:0000269|PubMed:21680734, ECO:0000269|PubMed:22493088}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. |
nucleotide Binding | |
Features | Chain (1); Topological domain (3); Transmembrane (2) |
Keywords | Acyltransferase;Cytoplasm;Endoplasmic reticulum;Glycerol metabolism;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | INDUCTION: In white adipose tissue, it is regulated by leptin. By insulin. Up-regulated in diabetic mice. Down-regulated upon fasting and replenished upon refeeding in adipose tissue and liver. Down-regulation in obese animals can reduce hepatic lipogenesis and hepatic steatosis as well as attenuate hyperlipidemia, thereby leading to an improvement in metabolic syndrome. {ECO:0000269|PubMed:12413942, ECO:0000269|PubMed:14521909, ECO:0000269|PubMed:16001399}. |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11217851; 12077311; 12466851; 14681479; 15550388; 16751624; 18175806; 18252207; 18757836; 19049983; 19092943; 20562862; 21267068; 21317108; 21436037; 22055502; 22355095; 22872236; 22927462; 23489367; 23643496; 23988655; 24358267; 24953780; 25602705; 26508642; 27531967; 27731369; 27754788; 27858140; 28249764; 28369476; 29563512; 30397187; 30929916; 30936184; 31693883; 32561790; 32749667; 33147469; |
Motif | |
Gene Encoded By | |
Mass | 43,770 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:10868; RHEA:10869; RHEA:11488; RHEA:11489; RHEA:38163; RHEA:38164; RHEA:38219; RHEA:38220; RHEA:38435; RHEA:38436; RHEA:38439; RHEA:38440; RHEA:38071; RHEA:38072; RHEA:37911; RHEA:37912; RHEA:38175; RHEA:38176; RHEA:55340; RHEA:55341; RHEA:37915; RHEA:37916 |
Cross Reference Brenda | 2.3.1.20; |