Search Results
Overview
| Uniprot ID | O75452 |
|---|---|
| Protein Name | Retinol dehydrogenase 16 |
| Gene Name | RDH16 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 210 | MIEPGYFKTAVTSKE |
| 216 | FKTAVTSKERFLKSF |
| 235 | DRSSPEVKEAYGEKF |
| 241 | VKEAYGEKFVADYKK |
| 247 | EKFVADYKKSAEQME |
| 248 | KFVADYKKSAEQMEQ |
| 30 | VLSHLRDKYVFITGC |
| 64 | LAACLTEKGAEQLRG |
Function
Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes (PubMed:10329026, PubMed:12534290, PubMed:9677409). Has higher activity towards CRBP-bound retinol than with free retinol (PubMed:12534290). Also oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction (PubMed:10329026, PubMed:29541409, PubMed:9677409)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0043231 | intracellular membrane-bounded organelle |
| Molecular Function | GO:0106429 | 11-cis-retinol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0004745 | all-trans-retinol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0047044 | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0047023 | androsterone dehydrogenase [NAD(P)+] activity |
| Molecular Function | GO:0009055 | electron transfer activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Biological Process | GO:0006629 | lipid metabolic process |
| Biological Process | GO:0042572 | retinol metabolic process |
| Biological Process | GO:0008202 | steroid 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.