| Identification |
| HMDB Protein ID
| HMDBP12122 |
| Secondary Accession Numbers
| None |
| Name
| Diacylglycerol kinase alpha |
| Synonyms
|
- DAG kinase alpha
- 80 kDa diacylglycerol kinase
- Diglyceride kinase alpha
- DGK-alpha
|
| Gene Name
| DGKA |
| Protein Type
| Unknown |
| Biological Properties |
| General Function
| Not Available |
| Specific Function
| Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:8034597). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:8034597). Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol (By similarity). |
| Pathways
|
- Choline metabolism in cancer
- Glycerolipid metabolism
- Glycerophospholipid metabolism
- Phosphatidylinositol signaling system
- Phospholipase D signaling pathway
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| phosphatidic acid biosynthetic process |
| intracellular signal transduction |
| diacylglycerol metabolic process |
| protein kinase C-activating G-protein coupled receptor signaling pathway |
| lipid phosphorylation |
| Cellular Component |
| cytosol |
| plasma membrane |
| Molecular Function |
| ATP binding |
| calcium ion binding |
| NAD+ kinase activity |
| diacylglycerol kinase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
| Number of Residues
| 734 |
| Molecular Weight
| 82605.375 |
| Theoretical pI
| 6.531 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P20192 |
| UniProtKB/Swiss-Prot Entry Name
| DGKA_PIG |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
| General References
| - Kai M, Sakane F, Imai S, Wada I, Kanoh H: Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells. J Biol Chem. 1994 Jul 15;269(28):18492-8. [PubMed:8034597 ]
- Sakane F, Yamada K, Kanoh H, Yokoyama C, Tanabe T: Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Nature. 1990 Mar 22;344(6264):345-8. doi: 10.1038/344345a0. [PubMed:2156169 ]
- Sakane F, Kai M, Wada I, Imai S, Kanoh H: The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers serves as a catalytic domain. Biochem J. 1996 Sep 1;318 ( Pt 2):583-90. doi: 10.1042/bj3180583. [PubMed:8809050 ]
- Sato M, Liu K, Sasaki S, Kunii N, Sakai H, Mizuno H, Saga H, Sakane F: Evaluations of the selectivities of the diacylglycerol kinase inhibitors R59022 and R59949 among diacylglycerol kinase isozymes using a new non-radioactive assay method. Pharmacology. 2013;92(1-2):99-107. doi: 10.1159/000351849. Epub 2013 Aug 16. [PubMed:23949095 ]
|