Search Results
Overview
| Uniprot ID | Q99536 |
|---|---|
| Protein Name | NADPH-dependent quinone oxidoreductase VAT1 |
| Gene Name | VAT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 225 | FGTASASKHEALKEN |
| 255 | EIKKISPKGVDIVMD |
| 295 | ANLLTGPKRNLMALA |
| 372 | EKVADAMKQMQEKKN |
| 382 | QEKKNVGKVLLVPGP |
Function
Multifunctional protein with enzymatic and transport activities (PubMed:17105775, PubMed:26394711, PubMed:32005660, PubMed:33483563). Probable NADPH-dependent quinone oxidoreductase which physiological substrates and function are unclear (PubMed:33483563). Alternatively, has also been suggested to mediate the transfer of negatively charged phospholipids including phosphatidic acid (PA), phosphatidylserine (PS) and phosphatidylglycerol (PG) between endoplasmic reticulum and mitochondrial membranes (PubMed:26394711, PubMed:32005660). Could regulate mitochondrial fusion through its interaction with mitofusins (PubMed:17105775)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0035578 | azurophil granule lumen |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Molecular Function | GO:0008753 | NADPH dehydrogenase (quinone) activity |
| Molecular Function | GO:0120014 | phospholipid transfer activity |
| Molecular Function | GO:0003960 | quinone reductase (NADPH) activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0120010 | intermembrane phospholipid transfer |
| Biological Process | GO:0010637 | negative regulation of mitochondrial fusion |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.