Search Results
Overview
| Uniprot ID | P08319 |
|---|---|
| Protein Name | All-trans-retinol dehydrogenase [NAD(+)] ADH4 |
| Gene Name | ADH4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 103 | APLCRKCKFCLSPLT |
| 11 | KGKVIKCKAAIAWEA |
| 115 | PLTNLCGKISNLKSP |
| 120 | CGKISNLKSPASDQQ |
| 132 | DQQLMEDKTSRFTCK |
| 20 | AIAWEAGKPLCIEEV |
| 234 | GIDINSEKFVKAKAL |
| 239 | SEKFVKAKALGATDC |
| 254 | LNPRDLHKPIQEVII |
| 329 | GTFFGGWKSVDSIPK |
| 33 | EVEVAPPKAHEVRIQ |
| 336 | KSVDSIPKLVTDYKN |
| 342 | PKLVTDYKNKKFNLD |
| 345 | VTDYKNKKFNLDALV |
| 372 | FDLMNQGKSVRTILI |
| 86 | GPGVTNVKPGDKVIP |
Function
Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Also catalyzes the reduction of benzoquinones (PubMed:10514444)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Molecular Function | GO:0004022 | alcohol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0004032 | aldose reductase (NADPH) activity |
| Molecular Function | GO:0005503 | all-trans retinal binding |
| Molecular Function | GO:0004745 | all-trans-retinol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0018479 | benzaldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0003960 | quinone reductase (NADPH) activity |
| Molecular Function | GO:0019841 | retinol binding |
| Molecular Function | GO:0051903 | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0046164 | alcohol catabolic process |
| Biological Process | GO:0006066 | alcohol metabolic process |
| Biological Process | GO:0006081 | aldehyde metabolic process |
| Biological Process | GO:0010430 | fatty acid omega-oxidation |
| Biological Process | GO:0046294 | formaldehyde catabolic process |
| Biological Process | GO:1901661 | quinone metabolic process |
| Biological Process | GO:0001523 | retinoid metabolic process |
| Biological Process | GO:0042572 | retinol metabolic process |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.