ADH1C

Alcohol dehydrogenase 1C (class I), gamma polypeptide
PDB rendering based on 1deh.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1HT0, 1U3W
Identifiers
Symbols	ADH1C; ADH3
External IDs	OMIM: 103730 MGI: 87921 HomoloGene: 73888 ChEMBL: 3285 GeneCards: ADH1C Gene
EC number	1.1.1.1
Gene Ontology Molecular function • alcohol dehydrogenase (NAD) activity • zinc ion binding Cellular component • cytosol Biological process • ethanol oxidation • xenobiotic metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	126	11522
Ensembl	ENSG00000248144	ENSMUSG00000074207
UniProt	P00326	P00329
RefSeq (mRNA)	NM_000669	NM_007409
RefSeq (protein)	NP_000660	NP_031435
Location (UCSC)	Chr 4: 100.26 – 100.27 Mb	Chr 3: 138.26 – 138.29 Mb
PubMed search	[1]	[2]

Alcohol dehydrogenase 1C is an enzyme that in humans is encoded by the ADH1C gene.

This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.

Further reading

• Seitz HK, Meier P (2007). "The role of acetaldehyde in upper digestive tract cancer in alcoholics.". Translational research : the journal of laboratory and clinical medicine 149 (6): 293–7. doi:10.1016/j.trsl.2006.12.002. PMID 17543846. 
• Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features.". Biochemistry 15 (21): 4687–93. doi:10.1021/bi00666a023. PMID 9982. 
• Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R (1992). "Molecular structure of the human alcohol dehydrogenase 3 gene.". Jpn. J. Genet. 67 (2): 167–71. doi:10.1266/jjg.67.167. PMID 1524834. 
• Hurley TD, Bosron WF, Hamilton JA, Amzel LM (1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.". Proc. Natl. Acad. Sci. U.S.A. 88 (18): 8149–53. doi:10.1073/pnas.88.18.8149. PMC 52464. PMID 1896463. 
• Stewart MJ, McBride MS, Winter LA, Duester G (1990). "Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box.". Gene 90 (2): 271–9. doi:10.1016/0378-1119(90)90190-3. PMID 2169444. 
• Yasunami M, Kikuchi I, Sarapata D, Yoshida A (1990). "The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome.". Genomics 7 (2): 152–8. doi:10.1016/0888-7543(90)90535-3. PMID 2347582. 
• Tsukahara M, Yoshida A (1989). "Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization.". Genomics 4 (2): 218–20. doi:10.1016/0888-7543(89)90304-2. PMID 2737681. 
• Ikuta T, Szeto S, Yoshida A (1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.". Proc. Natl. Acad. Sci. U.S.A. 83 (3): 634–8. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875. 
• Xu YL, Carr LG, Bosron WF, et al. (1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.". Genomics 2 (3): 209–14. doi:10.1016/0888-7543(88)90004-3. PMID 3397059. 
• Höög JO, Hedén LO, Larsson K, et al. (1986). "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties.". Eur. J. Biochem. 159 (2): 215–8. doi:10.1111/j.1432-1033.1986.tb09855.x. PMID 3758060. 
• Bühler R, Hempel J, Kaiser R, et al. (1985). "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain.". Eur. J. Biochem. 145 (3): 447–53. doi:10.1111/j.1432-1033.1984.tb08575.x. PMID 6391921. 
• Cheung B, Anderson JK, Holmes RS, Beacham IR (1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis.". Alcohol. Clin. Exp. Res. 19 (1): 185–6. doi:10.1111/j.1530-0277.1995.tb01490.x. PMID 7771649. 
• Hurley TD, Bosron WF, Stone CL, Amzel LM (1994). "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.". J. Mol. Biol. 239 (3): 415–29. doi:10.1006/jmbi.1994.1382. PMID 8201622. 
• Cheung C, Smith CK, Hoog JO, Hotchkiss SA (1999). "Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin.". Biochem. Biophys. Res. Commun. 261 (1): 100–7. doi:10.1006/bbrc.1999.0943. PMID 10405330. 
• Duester G, Farrés J, Felder MR, et al. (1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family.". Biochem. Pharmacol. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757. 
• Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD (2001). "Three-dimensional structures of the three human class I alcohol dehydrogenases.". Protein Sci. 10 (4): 697–706. doi:10.1110/ps.45001. PMC 2373965. PMID 11274460. 
• 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. 
• Osier MV, Pakstis AJ, Goldman D, et al. (2003). "A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans.". Alcohol. Clin. Exp. Res. 26 (12): 1759–63. doi:10.1097/01.ALC.0000042013.13899.75. PMID 12500098.