Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Adh1. (This text reflects annotations as of Wednesday, January 23, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of September 10, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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, 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. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Adh1
  • participates in the following biological processes:
    • ethanol catabolic process ^[6]
    • oxidation-reduction process ^{[1, 3, 6, 7, 11]}
    • response to retinoic acid ^[12]
    • response to steroid hormone stimulus ^[2]
    • response to testosterone stimulus ^[13]
  • performs the following molecular functions:
    • alcohol dehydrogenase (NAD) activity ^{[1, 3, 6, 7, 11]}
  • is located in the following cellular components:
    • intracellular ^[4]
    • mitochondrion ^[1]
• Researchers have inferred, based on physical interactions, that the gene product of Adh1
  • performs the following molecular functions:
    • protein homodimerization activity ^[1]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Adh1
  • participates in the following biological processes:
    • behavioral response to ethanol ^[5]
    • ethanol catabolic process ^[5]
    • retinoic acid metabolic process ^{[5, 9, 10]}
    • retinoid metabolic process ^[8]
    • retinol metabolic process ^{[5, 9, 10]}
• Researchers have inferred, based on genetic interactions, that the gene product of Adh1
  • participates in the following biological processes:
    • retinoic acid metabolic process based on interactions with Rbp1 ^[10]
    • retinol metabolic process based on interactions with Rbp1 ^[10]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Adh1:
  • participates in the following biological processes:
    • acetaldehyde biosynthetic process
    • ethanol oxidation
  • performs the following molecular functions:
    • alcohol dehydrogenase (NAD) activity
    • drug binding
    • ethanol binding
    • NAD binding
    • retinol dehydrogenase activity
  • is located in the following cellular components:
    • cytosol

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Summary text based on GO annotations supported by structural data

• Adh1 encodes a protein or proteins that contain the following InterPro domains: Alcohol dehydrogenase GroES-like, Alcohol dehydrogenase superfamily, zinc-type, Alcohol dehydrogenase, C-terminal, Alcohol dehydrogenase, zinc-type, conserved site, GroES-like, NAD(P)-binding domain, indicating that the gene product:
  • performs the following molecular functions:
    • nucleotide binding
    • oxidoreductase activity
    • zinc ion binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Adh1 indicates that it:
  • performs the following molecular functions:
    • metal ion binding
    • oxidoreductase activity
  • is located in the following cellular components:
    • cytoplasm

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References

1. Algar EM et al. (1985) Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties. Int J Biochem, 17:51-60. (PubMed:3996732)
2. Asadi FK et al. (1994) Androgen regulation of gene expression in primary epithelial cells of the mouse kidney. Endocrinology, 134:1179-87. (PubMed:8119157)
3. Balak KJ et al. (1982) Genetic and developmental regulation of mouse liver alcohol dehydrogenase. J Biol Chem, 257:15000-7. (PubMed:6816803)
4. Deltour L et al. (1997) Localization of class I and class IV alcohol dehydrogenases in mouse testis and epididymis: potential retinol dehydrogenases for endogenous retinoic acid synthesis. Biol Reprod, 56:102-9. (PubMed:9002638)
5. Deltour L et al. (1999) Metabolic deficiencies in alcohol dehydrogenase Adh1, Adh3, and Adh4 null mutant mice. Overlapping roles of Adh1 and Adh4 in ethanol clearance and metabolism of retinol to retinoic acid. J Biol Chem, 274:16796-801. (PubMed:10358022)
6. Holmes RS. (1979) Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: evidence for a cis-acting regulator gene (Adt-i) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-i on chromosome 3. Biochem Genet, 17:461-72. (PubMed:518534)
7. Holmes RS et al. (1981) Mouse alcohol dehydrogenase isozymes: products of closely localized duplicate genes exhibiting divergent kinetic properties. J Exp Zool, 217:151-7. (PubMed:7026729)
8. Molotkov A et al. (2002) Excessive vitamin A toxicity in mice genetically deficient in either alcohol dehydrogenase Adh1 or Adh3. Eur J Biochem, 269:2607-12. (PubMed:12027900)
9. Molotkov A et al. (2003) Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1) functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol to retinoic acid. J Biol Chem, 278:36085-90. (PubMed:12851412)
10. Molotkov A et al. (2004) Opposing actions of cellular retinol-binding protein and alcohol dehydrogenase control the balance between retinol storage and degradation. Biochem J, 383:295-302. (PubMed:15193143)
11. Rex DK et al. (1984) Purification and characterization of mouse alcohol dehydrogenase from two inbred strains that differ in total liver enzyme activity. Biochem Genet, 22:115-24. (PubMed:6370228)
12. Shean ML et al. (1993) The role of alcohol dehydrogenase in retinoic acid homeostasis and fetal alcohol syndrome. Alcohol Alcohol Suppl, 2:51-6. (PubMed:7748347)
13. Xie D et al. (1996) Ten kilobases of 5'-flanking region confers proper regulation of the mouse alcohol dehydrogenase-1 (Adh-1) gene in kidney and adrenal of transgenic mice. Gene, 181:173-8. (PubMed:8973327)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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