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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
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'''Alcohol dehydrogenase 1A''' is an [[enzyme]] that in humans is encoded by the ''ADH1A'' [[gene]].<ref name="pmid3006456">{{cite journal | author = Smith M | title = Genetics of human alcohol and aldehyde dehydrogenases | journal = Adv Hum Genet | volume = 15 | issue =  | pages = 249–90 |date=Mar 1986| pmid = 3006456 | pmc =  | doi =10.1007/978-1-4615-8356-1_5 | isbn = 978-1-4615-8358-5 }}</ref><ref name="entrez"/>
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{{GNF_Protein_box
| image = PBB_Protein_ADH1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1deh.
| PDB = {{PDB2|1deh}}, {{PDB2|1hdx}}, {{PDB2|1hdy}}, {{PDB2|1hdz}}, {{PDB2|1hso}}, {{PDB2|1hsz}}, {{PDB2|1ht0}}, {{PDB2|1htb}}, {{PDB2|1u3t}}, {{PDB2|1u3u}}, {{PDB2|1u3v}}, {{PDB2|1u3w}}, {{PDB2|3hud}}
| Name = Alcohol dehydrogenase 1A (class I), alpha polypeptide
| HGNCid = 249
| Symbol = ADH1A
| AltSymbols =; ADH1
  | OMIM = 103700
| ECnumber =
| Homologene = 88335
| MGIid =
  | GeneAtlas_image1 = PBB_GE_ADH1A_207820_at_tn.png
| Function = {{GNF_GO|id=GO:0004024 |text = alcohol dehydrogenase activity, zinc-dependent}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
  | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}  
| Process = {{GNF_GO|id=GO:0006066 |text = alcohol metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 124
    | Hs_Ensembl = ENSG00000187758
    | Hs_RefseqProtein = NP_000658
    | Hs_RefseqmRNA = NM_000667
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 100416547
    | Hs_GenLoc_end = 100431165
    | Hs_Uniprot = P07327
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Alcohol dehydrogenase 1A (class I), alpha polypeptide''', also known as '''ADH1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Smith M |title=Genetics of human alcohol and aldehyde dehydrogenases. |journal=Adv. Hum. Genet. |volume=15 |issue=  |pages= 249-90 |year= 1986 |pmid= 3006456 |doi=  }}
*{{cite journal  | vauthors=Lange LG, Sytkowski AJ, Vallee BL |title=Human liver alcohol dehydrogenase: purification, composition, and catalytic features |journal=Biochemistry |volume=15 |issue= 21 |pages= 4687–93 |year= 1976 |pmid= 9982 |doi=10.1021/bi00666a023 }}
*{{cite journal  | author=Lange LG, Sytkowski AJ, Vallee BL |title=Human liver alcohol dehydrogenase: purification, composition, and catalytic features. |journal=Biochemistry |volume=15 |issue= 21 |pages= 4687-93 |year= 1976 |pmid= 9982 |doi=  }}
*{{cite journal  | vauthors=van Ooij C, Snyder RC, Paeper BW, Duester G |title=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 |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 3023–31 |year= 1992 |pmid= 1620113 |doi= | pmc=364516 }}
*{{cite journal  | author=van Ooij C, Snyder RC, Paeper BW, Duester G |title=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. |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 3023-31 |year= 1992 |pmid= 1620113 |doi=  }}
*{{cite journal  | vauthors=Stewart MJ, McBride MS, Winter LA, Duester G |title=Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box |journal=Gene |volume=90 |issue= 2 |pages= 271–9 |year= 1990 |pmid= 2169444 |doi=10.1016/0378-1119(90)90190-3 }}
*{{cite journal  | author=Stewart MJ, McBride MS, Winter LA, Duester G |title=Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box. |journal=Gene |volume=90 |issue= 2 |pages= 271-9 |year= 1990 |pmid= 2169444 |doi=  }}
*{{cite journal  | vauthors=Yasunami M, Kikuchi I, Sarapata D, Yoshida A |title=The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome |journal=Genomics |volume=7 |issue= 2 |pages= 152–8 |year= 1990 |pmid= 2347582 |doi=10.1016/0888-7543(90)90535-3 }}
*{{cite journal  | author=Yasunami M, Kikuchi I, Sarapata D, Yoshida A |title=The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. |journal=Genomics |volume=7 |issue= 2 |pages= 152-8 |year= 1990 |pmid= 2347582 |doi=  }}
*{{cite journal  | vauthors=Tsukahara M, Yoshida A |title=Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization |journal=Genomics |volume=4 |issue= 2 |pages= 218–20 |year= 1989 |pmid= 2737681 |doi=10.1016/0888-7543(89)90304-2 }}
*{{cite journal  | author=Tsukahara M, Yoshida A |title=Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization. |journal=Genomics |volume=4 |issue= 2 |pages= 218-20 |year= 1989 |pmid= 2737681 |doi=  }}
*{{cite journal  | vauthors=Matsuo Y, Yokoyama S |title=Molecular structure of the human alcohol dehydrogenase 1 gene |journal=FEBS Lett. |volume=243 |issue= 1 |pages= 57–60 |year= 1989 |pmid= 2920825 |doi=10.1016/0014-5793(89)81217-7 }}
*{{cite journal  | author=Matsuo Y, Yokoyama S |title=Molecular structure of the human alcohol dehydrogenase 1 gene. |journal=FEBS Lett. |volume=243 |issue= 1 |pages= 57-60 |year= 1989 |pmid= 2920825 |doi=  }}
*{{cite journal  | vauthors=Ikuta T, Szeto S, Yoshida A |title=Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 3 |pages= 634–8 |year= 1986 |pmid= 2935875 |doi=10.1073/pnas.83.3.634  | pmc=322918 }}
*{{cite journal  | author=Ikuta T, Szeto S, Yoshida A |title=Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 3 |pages= 634-8 |year= 1986 |pmid= 2935875 |doi=  }}
*{{cite journal  | vauthors=von Bahr-Lindström H, Höög JO, Hedén LO |title=cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase |journal=Biochemistry |volume=25 |issue= 9 |pages= 2465–70 |year= 1986 |pmid= 3013304 |doi=10.1021/bi00357a026 |display-authors=etal}}
*{{cite journal  | author=von Bahr-Lindström H, Höög JO, Hedén LO, ''et al.'' |title=cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. |journal=Biochemistry |volume=25 |issue= 9 |pages= 2465-70 |year= 1986 |pmid= 3013304 |doi=  }}
*{{cite journal  | vauthors=Duester G, Farrés J, Felder MR |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389–95 |year= 1999 |pmid= 10424757 |doi=10.1016/S0006-2952(99)00065-9 |display-authors=etal}}
*{{cite journal  | author=Duester G, Farrés J, Felder MR, ''et al.'' |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family. |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389-95 |year= 1999 |pmid= 10424757 |doi=  }}
*{{cite journal  | vauthors=Rodriguez-Zavala JS, Weiner H |title=Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation |journal=Biochemistry |volume=41 |issue= 26 |pages= 8229–37 |year= 2002 |pmid= 12081471 |doi=10.1021/bi012081x }}
*{{cite journal  | author=Rodriguez-Zavala JS, Weiner H |title=Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. |journal=Biochemistry |volume=41 |issue= 26 |pages= 8229-37 |year= 2002 |pmid= 12081471 |doi=  }}
*{{cite journal  | vauthors=Sandberg M, Yasar U, Strömberg P |title=Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase |journal=British Journal of Clinical Pharmacology |volume=54 |issue= 4 |pages= 423–9 |year= 2003 |pmid= 12392591 |doi=10.1046/j.1365-2125.2002.01660.x  | pmc=1874434 |display-authors=etal}}
*{{cite journal  | author=Sandberg M, Yasar U, Strömberg P, ''et al.'' |title=Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase. |journal=British journal of clinical pharmacology |volume=54 |issue= 4 |pages= 423-9 |year= 2003 |pmid= 12392591 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Dannenberg LO, Chen HJ, Edenberg HJ |title=GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene |journal=DNA Cell Biol. |volume=24 |issue= 9 |pages= 543–52 |year= 2006 |pmid= 16153155 |doi= 10.1089/dna.2005.24.543 }}
*{{cite journal  | author=Dannenberg LO, Chen HJ, Edenberg HJ |title=GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene. |journal=DNA Cell Biol. |volume=24 |issue= 9 |pages= 543-52 |year= 2006 |pmid= 16153155 |doi= 10.1089/dna.2005.24.543 }}
*{{cite journal  | vauthors=Jelski W, Chrostek L, Szmitkowski M |title=The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer |journal=Pancreas |volume=35 |issue= 2 |pages= 142–6 |year= 2007 |pmid= 17632320 |doi= 10.1097/MPA.0b013e318053eae2 }}
*{{cite journal  | author=Jelski W, Chrostek L, Szmitkowski M |title=The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer. |journal=Pancreas |volume=35 |issue= 2 |pages= 142-6 |year= 2007 |pmid= 17632320 |doi= 10.1097/MPA.0b013e318053eae2 }}
}}
}}
{{refend}}
{{refend}}
==External links==
* {{UCSC gene info|ADH1A}}
{{PDB Gallery|geneid=124}}
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Latest revision as of 12:06, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Alcohol dehydrogenase 1A is an enzyme that in humans is encoded by the ADH1A gene.[1][2]

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.[2]

References

  1. ↑ Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
  2. ↑ 2.0 2.1 "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide".

Further reading

External links


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