ADH4

Alcohol dehydrogenase 4 (class II), pi polypeptide
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3COS​
Identifiers
Symbols	ADH4 ; ADH-2; HEL-S-4
External IDs	OMIM: 103740 MGI: 1349472 HomoloGene: 20162 ChEMBL: 2990 GeneCards: ADH4 Gene
EC number	1.1.1.1
Gene ontology Molecular function • NADPH:quinone reductase activity • alcohol dehydrogenase (NAD) activity • alcohol dehydrogenase activity, zinc-dependent • alditol:NADP+ 1-oxidoreductase activity • retinol dehydrogenase activity • all-trans retinal binding • zinc ion binding • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor • benzaldehyde dehydrogenase activity • retinol binding • ethanol binding • NAD binding Cellular component • cytosol Biological process • retinoid metabolic process • alcohol metabolic process • ethanol oxidation • cellular aldehyde metabolic process • xenobiotic metabolic process • retinol metabolic process • small molecule metabolic process • alcohol catabolic process • quinone metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	127	26876
Ensembl	ENSG00000198099	ENSMUSG00000037797
UniProt	P08319	Q9QYY9
RefSeq (mRNA)	NM_000670	NM_011996
RefSeq (protein)	NP_000661	NP_036126
Location (UCSC)	Chr 4: 99.12 – 99.16 Mb	Chr 3: 138.42 – 138.43 Mb
PubMed search

Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene.^[1]

This gene encodes class II alcohol dehydrogenase 4 pi 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 II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.^[1]

References

1. "Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide".

Further reading

• Jörnvall H (1994). "The alcohol dehydrogenase system.". EXS 71: 221–9. doi:10.1007/978-3-0348-7330-7_22. PMID 8032153.
• Edman K, Maret W (1993). "Alcohol dehydrogenase genes: restriction fragment length polymorphisms for ADH4 (pi-ADH) and ADH5 (chi-ADH) and construction of haplotypes among different ADH classes.". Hum. Genet. 90 (4): 395–401. doi:10.1007/bf00220466. PMID 1362387.
• von Bahr-Lindström H, Jörnvall H, Höög JO (1991). "Cloning and characterization of the human ADH4 gene.". Gene 103 (2): 269–74. doi:10.1016/0378-1119(91)90285-J. PMID 1889753.
• Höög JO, von Bahr-Lindström H, Hedén LO; et al. (1987). "Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit.". Biochemistry 26 (7): 1926–32. doi:10.1021/bi00381a021. PMID 3036213.
• Mårdh G, Dingley AL, Auld DS, Vallee BL (1987). "Human class II (pi) alcohol dehydrogenase has a redox-specific function in norepinephrine metabolism.". Proc. Natl. Acad. Sci. U.S.A. 83 (23): 8908–12. doi:10.1073/pnas.83.23.8908. PMC 387042. PMID 3466164.
• Li M, Edenberg HJ (1998). "Function of cis-acting elements in human alcohol dehydrogenase 4 (ADH4) promoter and role of C/EBP proteins in gene expression.". DNA Cell Biol. 17 (4): 387–97. doi:10.1089/dna.1998.17.387. PMID 9570155.
• Tryggvason K, Romert A, Eriksson U (2001). "Biosynthesis of 9-cis-retinoic acid in vivo. The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases.". J. Biol. Chem. 276 (22): 19253–8. doi:10.1074/jbc.M100215200. PMID 11279029.
• Xu XR, Huang J, Xu ZG; et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
• Iida A, Saito S, Sekine A; et al. (2002). "Thirteen single-nucleotide polymorphisms (SNPs) in the alcohol dehydrogenase 4 (ADH4) gene locus.". J. Hum. Genet. 47 (2): 74–6. doi:10.1007/s100380200003. PMID 11916005.
• Strömberg P, Svensson S, Hedberg JJ; et al. (2002). "Identification and characterisation of two allelic forms of human alcohol dehydrogenase 2.". Cell. Mol. Life Sci. 59 (3): 552–9. doi:10.1007/s00018-002-8447-1. PMID 11964133.
• Chou CF, Lai CL, Chang YC; et al. (2002). "Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase.". J. Biol. Chem. 277 (28): 25209–16. doi:10.1074/jbc.M201947200. PMID 11997393.
• 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.
• Galter D, Carmine A, Buervenich S; et al. (2003). "Distribution of class I, III and IV alcohol dehydrogenase mRNAs in the adult rat, mouse and human brain.". Eur. J. Biochem. 270 (6): 1316–26. doi:10.1046/j.1432-1033.2003.03502.x. PMID 12631290.
• Neumark YD, Friedlander Y, Durst R; et al. (2004). "Alcohol dehydrogenase polymorphisms influence alcohol-elimination rates in a male Jewish population.". Alcohol. Clin. Exp. Res. 28 (1): 10–4. doi:10.1097/01.ALC.0000108667.79219.4D. PMID 14745297.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Luo X, Kranzler HR, Zuo L; et al. (2006). "ADH4 gene variation is associated with alcohol and drug dependence: results from family controlled and population-structured association studies.". Pharmacogenet. Genomics 15 (11): 755–68. doi:10.1097/01.fpc.0000180141.77036.dc. PMID 16220108.
• Luo X, Kranzler HR, Zuo L; et al. (2006). "ADH4 gene variation is associated with alcohol dependence and drug dependence in European Americans: results from HWD tests and case-control association studies.". Neuropsychopharmacology 31 (5): 1085–95. doi:10.1038/sj.npp.1300925. PMID 16237392.
• Luo X, Kranzler HR, Zuo L; et al. (2007). "Personality traits of agreeableness and extraversion are associated with ADH4 variation.". Biol. Psychiatry 61 (5): 599–608. doi:10.1016/j.biopsych.2006.05.017. PMC 1853245. PMID 17069770.
• Carrigana, MA, Uryasev O; et al. (2014). "Hominids adapted to metabolize ethanol long before human-directed fermentation.". Proc. Natl. Acad. Sci. USA. 112 (2): 599–608. doi:10.1073/pnas.1404167111. PMC 4299227. PMID 25453080.