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Literature summary for 2.3.1.20 extracted from
- Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein (2019), PLoS ONE, 14, e0210396 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| calnexin | calnexin is a diacylglycerol acyltransferase-2 interacting protein | Mus musculus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of FLAG- or myc-tagged DGAT-2 fused to biotin ligase in HEK-293T cells and in COS-7 cells | Mus musculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition by selective DGAT1 inhibitor PF-04620110 | Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum membrane | DGAT-2 is an integral membrane, it has two transmembrane domains separated by a short loop (about 5-8 amino acids) that extends into the endoplasmic reticulum (ER) lumen. The first transmembrane domain contains an ER targeting signal while the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol | Mus musculus | 5789 | - |
| lipid droplet | - |
Mus musculus | 5811 | - |
| microsome | - |
Mus musculus | - |
- |
| additional information | the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets | Mus musculus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Mus musculus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + 1,2-diacyl-sn-glycerol | Mus musculus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| additional information | Mus musculus | calnexin is a DGAT2-interacting protein | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | Q9DCV3 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | DGAT2 is degraded via the proteasome in a ubiquitin-dependent manner | Mus musculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant biotinylated FLAG- or myc-tagged DGAT-2 fused to biotin ligase from HEK-293T cells, biotinylated proteins are captured with magnetic streptavidin beads | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| 3T3-L1 cell | - |
Mus musculus | - |
| fibroblast | - |
Mus musculus | - |
| preadipocyte | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Mus musculus | CoA + 1,2,3-triacylglycerol | - |
? | |
| additional information | calnexin is a DGAT2-interacting protein | Mus musculus | ? | - |
- |
|
| palmitoyl-CoA + 1,2-oleoyl-sn-glycerol | usage of fluorescent NBD-tagged palmitoyl-CoA as substrate | Mus musculus | CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | DGAT2 is part of a high molecular weight (about 650 kD) complex | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyl CoA:diacylglycerol acyltransferase-2 | - |
Mus musculus |
| DGAT-2 | - |
Mus musculus |
| DGAT2 | - |
Mus musculus |
| diacylglycerol acyltransferase-2 | - |
Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | calnexin-deficient mouse embryonic fibroblasts have reduced intracellular triacylglycerol levels and fewer large lipid droplets | Mus musculus |
| metabolism | DGAT-2 atalyzes the final step of triacylglycerol (TG) biosynthesis | Mus musculus |
| additional information | DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin | Mus musculus |
| physiological function | DGAT2 catalyzes the formation of triacylglycerol (TG) using fatty acyl coenzyme A (CoA) and 1,2-diacylglycerol (DG) as substrates. TG is the major form of stored metabolic energy in eukaryotic organisms that is sequestered in the hydrophobic core of cytosolic lipid droplets until it is needed. DGAT-2 catalyzes TG synthesis for lipid droplet growth | Mus musculus |
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