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ADH1C
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HT0, 1U3W
Identifiers
Aliases	ADH1C, ADH3, alcohol dehydrogenase 1C (class I), gamma polypeptide
External IDs	OMIM: 103730; MGI: 87921; HomoloGene: 73888; GeneCards: ADH1C; OMA:ADH1C - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q23 Start 99,336,497 bp End 99,352,746 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 G3|3 64.16 cM Start 137,966,752 bp End 137,996,459 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon jejunal mucosa nasal epithelium right lobe of liver olfactory zone of nasal mucosa duodenum mucosa of sigmoid colon rectum palpebral conjunctiva bronchial epithelial cell Top expressed in conjunctival fornix left lung lobe transitional epithelium of urinary bladder left colon adrenal gland left lobe of liver gallbladder seminal vesicula efferent ductule right kidney More reference expression data BioGPS n/a
Gene ontology Molecular function oxidoreductase activity zinc ion binding alcohol dehydrogenase (NAD+) activity metal ion binding NAD-retinol dehydrogenase activity alcohol dehydrogenase activity, zinc-dependent Cellular component cytoplasm nucleoplasm cytosol plasma membrane Biological process ethanol oxidation retinol metabolic process retinoic acid 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: 99.34 – 99.35 Mb Chr 3: 137.97 – 138 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Function

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 (beverage alcohol), 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, exhibit high activity for ethanol oxidation and play 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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000248144 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000074207 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Smith M (Mar 1986). "Genetics of Human Alcohol and Aldehyde Dehydrogenases". Advances in Human Genetics 15. Vol. 15. pp. 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
6. "Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide".

Further reading

• Seitz HK, Meier P (Jun 2007). "The role of acetaldehyde in upper digestive tract cancer in alcoholics". Translational Research. 149 (6): 293–7. doi:10.1016/j.trsl.2006.12.002. PMID 17543846.
• Lange LG, Sytkowski AJ, Vallee BL (Oct 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 (Apr 1992). "Molecular structure of the human alcohol dehydrogenase 3 gene". Idengaku Zasshi. 67 (2): 167–71. doi:10.1266/jjg.67.167. PMID 1524834.
• Hurley TD, Bosron WF, Hamilton JA, Amzel LM (Sep 1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions". Proceedings of the National Academy of Sciences of the United States of America. 88 (18): 8149–53. Bibcode:1991PNAS...88.8149H. doi:10.1073/pnas.88.18.8149. PMC 52464. PMID 1896463.
• Stewart MJ, McBride MS, Winter LA, Duester G (Jun 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 (Jun 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 (Feb 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 (Feb 1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence". Proceedings of the National Academy of Sciences of the United States of America. 83 (3): 634–8. Bibcode:1986PNAS...83..634I. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875.
• Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (Apr 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, Jörnvall H, von Bahr-Lindström H (Sep 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". European Journal of Biochemistry. 159 (2): 215–8. doi:10.1111/j.1432-1033.1986.tb09855.x. PMID 3758060.
• Bühler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jörnvall H (Dec 1984). "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain". European Journal of Biochemistry. 145 (3): 447–53. doi:10.1111/j.1432-1033.1984.tb08575.x. PMID 6391921.
• Cheung B, Anderson JK, Holmes RS, Beacham IR (Feb 1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis". Alcoholism: Clinical and Experimental Research. 19 (1): 185–6. doi:10.1111/j.1530-0277.1995.tb01490.x. PMID 7771649.
• Hurley TD, Bosron WF, Stone CL, Amzel LM (Jun 1994). "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences". Journal of Molecular Biology. 239 (3): 415–29. doi:10.1006/jmbi.1994.1382. PMID 8201622.
• Cheung C, Smith CK, Hoog JO, Hotchkiss SA (Jul 1999). "Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin". Biochemical and Biophysical Research Communications. 261 (1): 100–7. doi:10.1006/bbrc.1999.0943. PMID 10405330.
• Duester G, Farrés J, Felder MR, Holmes RS, Höög JO, Parés X, Plapp BV, Yin SJ, Jörnvall H (Aug 1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family". Biochemical Pharmacology. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757.
• Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD (Apr 2001). "Three-dimensional structures of the three human class I alcohol dehydrogenases". Protein Science. 10 (4): 697–706. doi:10.1110/ps.45001. PMC 2373965. PMID 11274460.
• Osier MV, Pakstis AJ, Goldman D, Edenberg HJ, Kidd JR, Kidd KK (Dec 2002). "A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans". Alcoholism: Clinical and Experimental Research. 26 (12): 1759–63. doi:10.1111/j.1530-0277.2002.tb02481.x. PMID 12500098.

External links

• Human ADH1C genome location and ADH1C gene details page in the UCSC Genome Browser.

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