ADH4: Difference between revisions

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{{Infobox_gene}}
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'''Alcohol dehydrogenase 4''' is an [[enzyme]] that in humans is encoded by the ''ADH4'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Alcohol dehydrogenase 4 (class II), pi polypeptide
| HGNCid = 252
| Symbol = ADH4
| AltSymbols =; ADH-2
| OMIM = 103740
| ECnumber = 
| Homologene = 20162
| MGIid = 1349472
| GeneAtlas_image1 = PBB_GE_ADH4_gnf1h00032_at_tn.png
| Function = {{GNF_GO|id=GO:0004022 |text = alcohol dehydrogenase activity}} {{GNF_GO|id=GO:0004174 |text = electron-transferring-flavoprotein dehydrogenase activity}} {{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 =
| Process = {{GNF_GO|id=GO:0006066 |text = alcohol metabolic process}} {{GNF_GO|id=GO:0006069 |text = ethanol oxidation}} {{GNF_GO|id=GO:0006081 |text = aldehyde metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 127
    | Hs_Ensembl = ENSG00000198099
    | Hs_RefseqProtein = NP_000661
    | Hs_RefseqmRNA = NM_000670
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 100263855
    | Hs_GenLoc_end = 100284472
    | Hs_Uniprot = P08319
    | Mm_EntrezGene = 26876
    | Mm_Ensembl = ENSMUSG00000037797
    | Mm_RefseqmRNA = NM_011996
    | Mm_RefseqProtein = NP_036126
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 138352896
    | Mm_GenLoc_end = 138368183
    | Mm_Uniprot = Q3V0P5
  }}
}}
'''Alcohol dehydrogenase 4 (class II), pi polypeptide''', also known as '''ADH4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=127| accessdate = }}</ref>
| summary_text = 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 (human)|chromosome 4]] in the cluster of alcohol dehydrogenase genes.<ref name="entrez" />
}}
}}


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


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|ADH4}}
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{{gene-4-stub}}

Latest revision as of 12:04, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

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. 1.0 1.1 "Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide".

Further reading

External links