Search Results
Overview
| Uniprot ID | P30838 |
|---|---|
| Protein Name | Aldehyde dehydrogenase, dimeric NADP-preferring |
| Gene Name | ALDH3A1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 194 | TGSTGVGKIIMTAAA |
| 202 | IIMTAAAKHLTPVTL |
| 221 | KSPCYVDKNCDLDVA |
| 269 | EKLKKSLKEFYGEDA |
| 302 | MGLIEGQKVAYGGTG |
| 360 | QFINQREKPLALYMF |
| 372 | YMFSSNDKVIKKMIA |
| 417 | MGSYHGKKSFETFSH |
| 449 | RYPPSPAKMTQH*** |
| 9 | SKISEAVKRARAAFS |
Function
ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:1737758). Preferentially oxidizes aromatic aldehyde substrates (PubMed:1737758). Comprises about 50 percent of corneal epithelial soluble proteins (By similarity). May play a role in preventing corneal damage caused by ultraviolet light (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0016020 | membrane |
| Molecular Function | GO:0004028 | 3-chloroallyl aldehyde dehydrogenase activity |
| Molecular Function | GO:0008106 | alcohol dehydrogenase (NADP+) activity |
| Molecular Function | GO:0004029 | aldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0004030 | aldehyde dehydrogenase [NAD(P)+] activity |
| Molecular Function | GO:0018479 | benzaldehyde dehydrogenase (NAD+) activity |
| Biological Process | GO:0006081 | aldehyde metabolic process |
| Biological Process | GO:0006629 | lipid metabolic process |
| Biological Process | GO:0006805 | xenobiotic 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] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.