Protein-coding gene in the species Homo sapiens
ADH1A |
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Available structures |
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PDB | Ortholog search: PDBe RCSB |
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List of PDB id codes |
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1HSO, 1U3T |
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Identifiers |
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Aliases | ADH1A, ADH1, alcohol dehydrogenase 1A (class I), alpha polypeptide |
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External IDs | OMIM: 103700; MGI: 87921; HomoloGene: 88335; GeneCards: ADH1A; OMA:ADH1A - orthologs |
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EC number | 1.1.1.1 |
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Gene location (Human) |
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| Chr. | Chromosome 4 (human)[1] |
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| Band | 4q23 | Start | 99,276,369 bp[1] |
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End | 99,291,003 bp[1] |
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Gene location (Mouse) |
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| Chr. | Chromosome 3 (mouse)[2] |
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| Band | 3 G3|3 64.16 cM | Start | 137,966,752 bp[2] |
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End | 137,996,459 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - right lobe of liver
- testicle
- Descending thoracic aorta
- gallbladder
- right coronary artery
- right lung
- subcutaneous adipose tissue
- left coronary artery
- duodenum
- ascending aorta
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| 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
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| More reference expression data |
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BioGPS | | More reference expression data |
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Gene ontology |
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Molecular function | - oxidoreductase activity
- zinc ion binding
- protein binding
- alcohol dehydrogenase (NAD+) activity
- metal ion binding
- alcohol dehydrogenase activity, zinc-dependent
- NAD-retinol dehydrogenase activity
| Cellular component | - cytoplasm
- nucleoplasm
- cytosol
- plasma membrane
| Biological process | - alcohol metabolic process
- ethanol oxidation
- retinol metabolic process
- retinoic acid metabolic process
| Sources:Amigo / QuickGO |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Alcohol dehydrogenase 1A is an enzyme that in humans is encoded by the ADH1A gene.[5][6]
This gene encodes class I alcohol dehydrogenase, alpha 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. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000187758 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074207 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Smith M (Mar 1986). "Genetics of Human Alcohol and Aldehyde Dehydrogenases". Advances in Human Genetics vol. 15. Vol. 15. pp. 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
- ^ a b "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide".
Further reading
- 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.
- van Ooij C, Snyder RC, Paeper BW, Duester G (1992). "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein". Mol. Cell. Biol. 12 (7): 3023–31. doi:10.1128/mcb.12.7.3023. PMC 364516. PMID 1620113.
- 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.
- Matsuo Y, Yokoyama S (1989). "Molecular structure of the human alcohol dehydrogenase 1 gene". FEBS Lett. 243 (1): 57–60. doi:10.1016/0014-5793(89)81217-7. PMID 2920825. S2CID 46240593.
- 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. Bibcode:1986PNAS...83..634I. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875.
- von Bahr-Lindström H, Höög JO, Hedén LO, et al. (1986). "cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase". Biochemistry. 25 (9): 2465–70. doi:10.1021/bi00357a026. PMID 3013304.
- 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.
- Rodriguez-Zavala JS, Weiner H (2002). "Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation". Biochemistry. 41 (26): 8229–37. doi:10.1021/bi012081x. PMID 12081471.
- Sandberg M, Yasar U, Strömberg P, et al. (2003). "Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase". British Journal of Clinical Pharmacology. 54 (4): 423–9. doi:10.1046/j.1365-2125.2002.01660.x. PMC 1874434. PMID 12392591.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- 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.
- Dannenberg LO, Chen HJ, Edenberg HJ (2006). "GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene". DNA Cell Biol. 24 (9): 543–52. doi:10.1089/dna.2005.24.543. PMID 16153155.
- Jelski W, Chrostek L, Szmitkowski M (2007). "The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer". Pancreas. 35 (2): 142–6. doi:10.1097/MPA.0b013e318053eae2. PMID 17632320. S2CID 519403.
External links
PDB gallery
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1deh: CRYSTALLIZATION OF HUMAN BETA1 ALCOHOL DEHYDROGENASE (15 MG/ML) IN 50 MM SODIUM PHOSPHATE (PH 7.5), 2.0 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 OC, 13% (W/V) PEG 8000 -
1hdx: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES -
1hdy: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES -
1hdz: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES -
1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A) -
1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1) -
1ht0: HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE -
1htb: CRYSTALLIZATION OF HUMAN BETA3 ALCOHOL DEHYDROGENASE (10 MG/ML) IN 100 MM SODIUM PHOSPHATE (PH 7.5), 7.5 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 C -
1u3t: Crystal Structure of Human Alcohol Dehydrogenase Alpha-Alpha Isoform Complexed with N-Cyclopentyl-N-Cyclobutylformamide Determined to 2.5 Angstrom Resolution -
1u3u: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Benzylformamide Determined to 1.6 Angstrom Resolution -
1u3v: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Heptylformamide Determined to 1.65 Angstrom Resolution -
1u3w: Crystal Structure of Human Alcohol Dehydrogenase Gamma-2-Gamma-2 Isoform Complexed with N-1-Methylheptylformamide Determined to 1.45 Angstrom Resolution -
3hud: THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS |
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