ADH1C

Protein-coding gene in the species Homo sapiens
ADH1C
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1HT0, 1U3W

Identifiers
AliasesADH1C, ADH3, alcohol dehydrogenase 1C (class I), gamma polypeptide
External IDsOMIM: 103730; MGI: 87921; HomoloGene: 73888; GeneCards: ADH1C; OMA:ADH1C - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for ADH1C
Genomic location for ADH1C
Band4q23Start99,336,497 bp[1]
End99,352,746 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for ADH1C
Genomic location for ADH1C
Band3 G3|3 64.16 cMStart137,966,752 bp[2]
End137,996,459 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • jejunal mucosa

  • nasal epithelium

  • right lobe of liver

  • olfactory zone of nasal mucosa

  • duodenum

  • mucosa of sigmoid colon

  • rectum

  • palpebral conjunctiva

  • bronchial epithelial cell
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
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • oxidoreductase activity
  • zinc ion binding
  • alcohol dehydrogenase (NAD+) activity
  • metal ion binding
  • NAD-retinol dehydrogenase activity
  • alcohol dehydrogenase activity, zinc-dependent
Cellular component
  • cytoplasm
  • nucleoplasm
  • cytosol
  • plasma membrane
Biological process
  • ethanol oxidation
  • retinol metabolic process
  • retinoic acid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

126

11522

Ensembl

ENSG00000248144

ENSMUSG00000074207

UniProt

P00326

P00329

RefSeq (mRNA)

NM_000669

NM_007409

RefSeq (protein)

NP_000660

NP_031435

Location (UCSC)Chr 4: 99.34 – 99.35 MbChr 3: 137.97 – 138 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alcohol dehydrogenase 1C is an enzyme that in humans is encoded by the ADH1C gene.[5]

Function

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 (beverage alcohol), 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, exhibit high activity for ethanol oxidation and play 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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000248144 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074207 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Smith M (Mar 1986). "Genetics of Human Alcohol and Aldehyde Dehydrogenases". Advances in Human Genetics 15. Vol. 15. pp. 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
  6. ^ "Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide".

Further reading

  • Seitz HK, Meier P (Jun 2007). "The role of acetaldehyde in upper digestive tract cancer in alcoholics". Translational Research. 149 (6): 293–7. doi:10.1016/j.trsl.2006.12.002. PMID 17543846.
  • Lange LG, Sytkowski AJ, Vallee BL (Oct 1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features". Biochemistry. 15 (21): 4687–93. doi:10.1021/bi00666a023. PMID 9982.
  • Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R (Apr 1992). "Molecular structure of the human alcohol dehydrogenase 3 gene". Idengaku Zasshi. 67 (2): 167–71. doi:10.1266/jjg.67.167. PMID 1524834.
  • Hurley TD, Bosron WF, Hamilton JA, Amzel LM (Sep 1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions". Proceedings of the National Academy of Sciences of the United States of America. 88 (18): 8149–53. Bibcode:1991PNAS...88.8149H. doi:10.1073/pnas.88.18.8149. PMC 52464. PMID 1896463.
  • Stewart MJ, McBride MS, Winter LA, Duester G (Jun 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 (Jun 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 (Feb 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.
  • Ikuta T, Szeto S, Yoshida A (Feb 1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence". Proceedings of the National Academy of Sciences of the United States of America. 83 (3): 634–8. Bibcode:1986PNAS...83..634I. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875.
  • Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (Apr 1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification". Genomics. 2 (3): 209–14. doi:10.1016/0888-7543(88)90004-3. PMID 3397059.
  • Höög JO, Hedén LO, Larsson K, Jörnvall H, von Bahr-Lindström H (Sep 1986). "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties". European Journal of Biochemistry. 159 (2): 215–8. doi:10.1111/j.1432-1033.1986.tb09855.x. PMID 3758060.
  • Bühler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jörnvall H (Dec 1984). "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain". European Journal of Biochemistry. 145 (3): 447–53. doi:10.1111/j.1432-1033.1984.tb08575.x. PMID 6391921.
  • 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.
  • Hurley TD, Bosron WF, Stone CL, Amzel LM (Jun 1994). "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences". Journal of Molecular Biology. 239 (3): 415–29. doi:10.1006/jmbi.1994.1382. PMID 8201622.
  • Cheung C, Smith CK, Hoog JO, Hotchkiss SA (Jul 1999). "Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin". Biochemical and Biophysical Research Communications. 261 (1): 100–7. doi:10.1006/bbrc.1999.0943. PMID 10405330.
  • Duester G, Farrés J, Felder MR, Holmes RS, Höög JO, Parés X, Plapp BV, Yin SJ, Jörnvall H (Aug 1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family". Biochemical Pharmacology. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757.
  • Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD (Apr 2001). "Three-dimensional structures of the three human class I alcohol dehydrogenases". Protein Science. 10 (4): 697–706. doi:10.1110/ps.45001. PMC 2373965. PMID 11274460.
  • Osier MV, Pakstis AJ, Goldman D, Edenberg HJ, Kidd JR, Kidd KK (Dec 2002). "A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans". Alcoholism: Clinical and Experimental Research. 26 (12): 1759–63. doi:10.1111/j.1530-0277.2002.tb02481.x. PMID 12500098.

External links

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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
    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
    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
    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
    1hdz: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES
  • 1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A)
    1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A)
  • 1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)
    1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)
  • 1ht0: HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE
    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
    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
    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
    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
    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
    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
    3hud: THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS


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