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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Alcohol dehydrogenase class 4 mu/sigma chain''' is an [[enzyme]] that in humans is encoded by the ''ADH7'' [[gene]].<ref name="pmid8195208">{{cite journal | vauthors = Satre MA, Zgombić-Knight M, Duester G | title = The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene | journal = The Journal of Biological Chemistry | volume = 269 | issue = 22 | pages = 15606–12 | date = Jun 1994 | pmid = 8195208 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=131| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ADH7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1agn.
| PDB = {{PDB2|1agn}}, {{PDB2|1d1s}}, {{PDB2|1d1t}}
| Name = Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide
| HGNCid = 256
| Symbol = ADH7
| AltSymbols =; ADH-4
| OMIM = 600086
| ECnumber = 
| Homologene = 37333
| MGIid = 87926
| GeneAtlas_image1 = PBB_GE_ADH7_210505_at_tn.png
| Function = {{GNF_GO|id=GO:0004024 |text = alcohol dehydrogenase activity, zinc-dependent}} {{GNF_GO|id=GO:0004745 |text = retinol 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:0006069 |text = ethanol oxidation}} {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 131
    | Hs_Ensembl = ENSG00000196344
    | Hs_RefseqProtein = NP_000664
    | Hs_RefseqmRNA = NM_000673
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 100552441
    | Hs_GenLoc_end = 100575548
    | Hs_Uniprot = P40394
    | Mm_EntrezGene = 11529
    | Mm_Ensembl = ENSMUSG00000055301
    | Mm_RefseqmRNA = NM_009626
    | Mm_RefseqProtein = NP_033756
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 138159100
    | Mm_GenLoc_end = 138168593
    | Mm_Uniprot = Q3UMM7
  }}
}}
'''Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide''', also known as '''ADH7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=131| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes class IV [[alcohol dehydrogenase]] 7 mu or sigma subunit, which is a member of the alcohol dehydrogenase family. Members of this family [[metabolism|metabolize]] a wide variety of [[substrate (biochemistry)|substrate]]s, including [[ethanol]], [[retinol]], other [[aliphatic]] alcohols, [[hydroxysteroid]]s, and [[lipid peroxidation]] products. The enzyme encoded by this gene is inefficient in [[Ethanol#Oxidation|ethanol]] [[Alcohol oxidation|oxidation]], but is the most active as a [[retinol dehydrogenase]]; thus it may participate in the synthesis of [[retinoic acid]], a hormone important for [[cellular differentiation]]. The expression of this gene makes it much more abundant in the stomach than the liver, thus it differs from the other known gene family members.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes class IV alcohol dehydrogenase 7 mu or sigma subunit, which is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The enzyme encoded by this gene is inefficient in ethanol oxidation, but is the most active as a retinol dehydrogenase; thus it may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. The expression of this gene is much more abundant in stomach than liver, thus differing from the other known gene family members.<ref name="entrez">{{cite web | title = Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=131| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
| citations =
* {{cite journal | vauthors = Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD | title = X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity | journal = The Journal of Biological Chemistry | volume = 272 | issue = 30 | pages = 18558–63 | date = Jul 1997 | pmid = 9228021 | doi = 10.1074/jbc.272.30.18558 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Yokoyama H, Baraona E, Lieber CS | title = Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH | journal = Genomics | volume = 31 | issue = 2 | pages = 243–5 | date = Jan 1996 | pmid = 8824810 | doi = 10.1006/geno.1996.0040 }}
*{{cite journal | author=Xie P, Parsons SH, Speckhard DC, ''et al.'' |title=X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity. |journal=J. Biol. Chem. |volume=272 |issue= 30 |pages= 18558-63 |year= 1997 |pmid= 9228021 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Yokoyama H, Baraona E, Lieber CS |title=Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH. |journal=Genomics |volume=31 |issue= 2 |pages= 243-5 |year= 1997 |pmid= 8824810 |doi= 10.1006/geno.1996.0040 }}
* {{cite journal | vauthors = Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R | title = Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7) | journal = FEBS Letters | volume = 351 | issue = 3 | pages = 411–5 | date = Sep 1994 | pmid = 8082805 | doi = 10.1016/0014-5793(94)00895-7 }}
*{{cite journal | author=Satre MA, Zgombić-Knight M, Duester G |title=The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene. |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15606-12 |year= 1994 |pmid= 8195208 |doi=  }}
* {{cite journal | vauthors = Yokoyama H, Baraona E, Lieber CS | title = Molecular cloning of human class IV alcohol dehydrogenase cDNA | journal = Biochemical and Biophysical Research Communications | volume = 203 | issue = 1 | pages = 219–24 | date = Aug 1994 | pmid = 8074657 | doi = 10.1006/bbrc.1994.2170 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Farrés J, Moreno A, Crosas B, Peralba JM, Allali-Hassani A, Hjelmqvist L, Jörnvall H, Parés X | title = Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships | journal = European Journal of Biochemistry / FEBS | volume = 224 | issue = 2 | pages = 549–57 | date = Sep 1994 | pmid = 7925371 | doi = 10.1111/j.1432-1033.1994.00549.x }}
*{{cite journal | author=Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R |title=Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7). |journal=FEBS Lett. |volume=351 |issue= 3 |pages= 411-5 |year= 1994 |pmid= 8082805 |doi= }}
* {{cite journal | vauthors = Zgombić-Knight M, Foglio MH, Duester G | title = Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro | journal = The Journal of Biological Chemistry | volume = 270 | issue = 9 | pages = 4305–11 | date = Mar 1995 | pmid = 7876191 | doi = 10.1074/jbc.270.9.4305 }}
*{{cite journal | author=Yokoyama H, Baraona E, Lieber CS |title=Molecular cloning of human class IV alcohol dehydrogenase cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 1 |pages= 219-24 |year= 1994 |pmid= 8074657 |doi= 10.1006/bbrc.1994.2170 }}
* {{cite journal | vauthors = Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK | title = Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes | journal = The Journal of Biological Chemistry | volume = 270 | issue = 8 | pages = 3625–30 | date = Feb 1995 | pmid = 7876099 | doi = 10.1074/jbc.270.8.3625 }}
*{{cite journal | author=Farrés J, Moreno A, Crosas B, ''et al.'' |title=Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 549-57 |year= 1994 |pmid= 7925371 |doi= }}
* {{cite journal | vauthors = Cheung B, Anderson JK, Holmes RS, Beacham IR | title = Human stomach class IV alcohol dehydrogenase: molecular genetic analysis | journal = Alcoholism: Clinical and Experimental Research | volume = 19 | issue = 1 | pages = 185–6 | date = Feb 1995 | pmid = 7771649 | doi = 10.1111/j.1530-0277.1995.tb01490.x }}
*{{cite journal | author=Zgombić-Knight M, Foglio MH, Duester G |title=Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4305-11 |year= 1995 |pmid= 7876191 |doi= }}
* {{cite journal | vauthors = Parés X, Cederlund E, Moreno A, Saubi N, Höög JO, Jörnvall H | title = Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class | journal = FEBS Letters | volume = 303 | issue = 1 | pages = 69–72 | date = May 1992 | pmid = 1592118 | doi = 10.1016/0014-5793(92)80479-Z }}
*{{cite journal | author=Kedishvili NY, Bosron WF, Stone CL, ''et al.'' |title=Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes. |journal=J. Biol. Chem. |volume=270 |issue= 8 |pages= 3625-30 |year= 1995 |pmid= 7876099 |doi= }}
*{{cite journal | author=Cheung B, Anderson JK, Holmes RS, Beacham IR |title=Human stomach class IV alcohol dehydrogenase: molecular genetic analysis. |journal=Alcohol. Clin. Exp. Res. |volume=19 |issue= 1 |pages= 185-6 |year= 1995 |pmid= 7771649 |doi= }}
*{{cite journal | author=Parés X, Cederlund E, Moreno A, ''et al.'' |title=Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class. |journal=FEBS Lett. |volume=303 |issue= 1 |pages= 69-72 |year= 1992 |pmid= 1592118 |doi= }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|ADH4}}
* {{UCSC gene info|ADH7}}
{{PDB Gallery|geneid=131}}
 
 
{{gene-4-stub}}

Latest revision as of 12:05, 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 class 4 mu/sigma chain is an enzyme that in humans is encoded by the ADH7 gene.[1][2]

Function

This gene encodes class IV alcohol dehydrogenase 7 mu or sigma subunit, which is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The enzyme encoded by this gene is inefficient in ethanol oxidation, but is the most active as a retinol dehydrogenase; thus it may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. The expression of this gene makes it much more abundant in the stomach than the liver, thus it differs from the other known gene family members.[2]

References

  1. ↑ Satre MA, Zgombić-Knight M, Duester G (Jun 1994). "The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene". The Journal of Biological Chemistry. 269 (22): 15606–12. PMID 8195208.
  2. ↑ 2.0 2.1 "Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide".

Further reading

  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD (Jul 1997). "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity". The Journal of Biological Chemistry. 272 (30): 18558–63. doi:10.1074/jbc.272.30.18558. PMID 9228021.
  • Yokoyama H, Baraona E, Lieber CS (Jan 1996). "Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH". Genomics. 31 (2): 243–5. doi:10.1006/geno.1996.0040. PMID 8824810.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R (Sep 1994). "Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)". FEBS Letters. 351 (3): 411–5. doi:10.1016/0014-5793(94)00895-7. PMID 8082805.
  • Yokoyama H, Baraona E, Lieber CS (Aug 1994). "Molecular cloning of human class IV alcohol dehydrogenase cDNA". Biochemical and Biophysical Research Communications. 203 (1): 219–24. doi:10.1006/bbrc.1994.2170. PMID 8074657.
  • Farrés J, Moreno A, Crosas B, Peralba JM, Allali-Hassani A, Hjelmqvist L, Jörnvall H, Parés X (Sep 1994). "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships". European Journal of Biochemistry / FEBS. 224 (2): 549–57. doi:10.1111/j.1432-1033.1994.00549.x. PMID 7925371.
  • Zgombić-Knight M, Foglio MH, Duester G (Mar 1995). "Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro". The Journal of Biological Chemistry. 270 (9): 4305–11. doi:10.1074/jbc.270.9.4305. PMID 7876191.
  • Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK (Feb 1995). "Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes". The Journal of Biological Chemistry. 270 (8): 3625–30. doi:10.1074/jbc.270.8.3625. PMID 7876099.
  • 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.
  • Parés X, Cederlund E, Moreno A, Saubi N, Höög JO, Jörnvall H (May 1992). "Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class". FEBS Letters. 303 (1): 69–72. doi:10.1016/0014-5793(92)80479-Z. PMID 1592118.

External links


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