ADH6

ADH6
Identifiers
Aliases	ADH6, ADH-5, alcohol dehydrogenase 6 (class V)
External IDs	HomoloGene: 68077 GeneCards: ADH6
Gene ontology Molecular function • oxidoreductase activity • zinc ion binding • alcohol dehydrogenase (NAD) activity • metal ion binding • alcohol dehydrogenase activity, zinc-dependent Cellular component • cytoplasm • cytosol • extracellular exosome Biological process • response to ethanol • oxidation-reduction process • ethanol oxidation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	130	n/a
Ensembl	ENSG00000172955	n/a
UniProt	P28332	n/a
RefSeq (mRNA)	NM_000672 NM_001102470	n/a
RefSeq (protein)	NP_000663.1 NP_001095940.1	n/a
Location (UCSC)	Chr 4: 99.2 – 99.22 Mb	n/a
PubMed search	[1]	n/a
Wikidata

View/Edit Human

Alcohol dehydrogenase 6 is an enzyme that in humans is encoded by the ADH6 gene.^[2][3]

This gene encodes class V alcohol dehydrogenase, which is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. This gene is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5' UTR, which is a steroid hormone receptor binding site. The deduced amino acid sequence of the open reading frame of this gene shows about 60% positional identity with other known alcohol dehydrogenases. This gene may have a distinct physiologic function.^[3]

References

1. "Human PubMed Reference:".
2. Yasunami M, Chen CS, Yoshida A (Oct 1991). "A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme". Proc Natl Acad Sci U S A. 88 (17): 7610–4. doi:10.1073/pnas.88.17.7610. PMC 52351. PMID 1881901.
3. "Entrez Gene: ADH6 alcohol dehydrogenase 6 (class V)".

External links

• Human ADH6 genome location and ADH6 gene details page in the UCSC Genome Browser.

Further reading

• Lieber CS (1990). "Interaction of ethanol with drugs, hepatotoxic agents, carcinogens and vitamins". Alcohol Alcohol. 25 (2–3): 157–76. PMID 2198032.
• Yoshida A (1995). "Genetic polymorphisms of alcohol metabolizing enzymes related to alcohol sensitivity and alcoholic diseases". Alcohol Alcohol. 29 (6): 693–6. PMID 7695785.
• Chen CS, Yoshida A (1992). "Enzymatic properties of the protein encoded by newly cloned human alcohol dehydrogenase ADH6 gene". Biochem. Biophys. Res. Commun. 181 (2): 743–7. doi:10.1016/0006-291X(91)91253-9. PMID 1755855.
• Zhi X, Chan EM, Edenberg HJ (2000). "Tissue-specific regulatory elements in the human alcohol dehydrogenase 6 gene". DNA Cell Biol. 19 (8): 487–97. doi:10.1089/10445490050128412. PMID 10975466.
• Strömberg P, Höög JO (2001). "Human class V alcohol dehydrogenase (ADH5): A complex transcription unit generates C-terminal multiplicity". Biochem. Biophys. Res. Commun. 278 (3): 544–9. doi:10.1006/bbrc.2000.3837. PMID 11095947.
• Osier MV, Pakstis AJ, Soodyall H, et al. (2002). "A global perspective on genetic variation at the ADH genes reveals unusual patterns of linkage disequilibrium and diversity". Am. J. Hum. Genet. 71 (1): 84–99. doi:10.1086/341290. PMC 384995. PMID 12050823.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.