Search Results
Overview
| Uniprot ID | P11766 |
|---|---|
| Protein Name | Alcohol dehydrogenase class-3 |
| Gene Name | ADH5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 107 | CKFCLNPKTNLCQKI |
| 113 | PKTNLCQKIRVTQGK |
| 120 | KIRVTQGKGLMPDGT |
| 226 | IIGVDINKDKFARAK |
| 233 | KDKFARAKEFGATEC |
| 284 | AALEACHKGWGVSVV |
| 315 | LVTGRTWKGTAFGGW |
| 323 | GTAFGGWKSVESVPK |
| 338 | LVSEYMSKKIKVDEF |
| 366 | FELMHSGKSIRTVVK |
| 84 | GEGVTKLKAGDTVIP |
Function
Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). 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). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed:33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0004022 | alcohol dehydrogenase (NAD+) activity |
| Molecular Function | GO:0009055 | electron transfer activity |
| Molecular Function | GO:0005504 | fatty acid binding |
| Molecular Function | GO:0018467 | formaldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0106322 | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
| Molecular Function | GO:0106321 | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
| Molecular Function | GO:0051903 | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| Molecular Function | GO:0080007 | S-nitrosoglutathione reductase (NADH) activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0010430 | fatty acid omega-oxidation |
| Biological Process | GO:0046294 | formaldehyde catabolic process |
| Biological Process | GO:0051775 | response to redox state |
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.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.