Alternative titles; symbols
HGNC Approved Gene Symbol: ADH7
Cytogenetic location: 4q23 Genomic coordinates (GRCh38): 4:99,412,263-99,435,342 (from NCBI)
Satre et al. (1994) characterized the ADH7 gene and determined that it encodes a class IV alcohol dehydrogenase that is very active as a retinol dehydrogenase. They isolated a nearly full-length ADH7 cDNA from a human stomach cDNA library and a 5-prime genomic clone containing exons 1 and 2 from a human genomic library. The deduced full-length amino acid sequence predicted a protein of 373 amino acids following the initiator methionine. The class IV identity of the sequence was confirmed by agreement with previously determined sequences for several human stomach class IV ADH peptides. Sequence comparison suggested that human ADH classes I and IV may have diverged from a common ancestor after the separation of the other classes, and may still share common physiologic functions. Satre et al. (1994) discussed the possibility that one of these functions is retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation.
Zgombic-Knight et al. (1995) demonstrated that ADH7 showed greater sequence identity with class I ADH (69%) than with classes II (e.g., 103740), III (e.g., 103710), or V, with which it is only 59 to 61% homologous. Zgombic-Knight et al. (1995) also confirmed that ADH7 is the major stomach ADH, but, unlike the others, is absent from liver.
Zgombic-Knight et al. (1995) demonstrated that the ADH7 gene has 9 exons. Transcriptional regulation of the ADH7 gene appeared to be different from that of the other classes in that the ADH7 promoter lacks a TATA box and GC boxes upstream of the transcription initiation site.
Yokoyama et al. (1996) showed that ADH7 contains 9 exons and spans about 22 kb of genomic DNA.
In fluorescence in situ hybridization, Yokoyama et al. (1996) mapped the ADH7 gene to chromosome 4q23-q24, close to the ADH cluster.
As outlined by Osier et al. (2002), 7 genes encoding ADH enzymes exist in a cluster extending approximately 380 kb on the long arm of chromosome 4. The class I ADH genes exist in a tighter cluster of approximately 77 kb, flanked upstream by ADH7 and downstream by ADH6 (103735), ADH4 (103740), and ADH5 (103710), in that order.
For a discussion of a possible association between variation in the ADH7 gene and alcohol dependence, see 103780, and for possible association with protection against aerodigestive tract cancer in alcohol drinkers, see 103720.0001.
Osier, M. V., Pakstis, A. J., Soodyall, H., Comas, D., Goldman, D., Odunsi, A., Okonofua, F., Parnas, J., Schulz, L. O., Bertranpetit, J., Bonne-Tamir, B., Lu, R.-B., Kidd, J. R., Kidd, K. K. A global perspective on genetic variation at the ADH genes reveals unusual patterns of linkage disequilibrium and diversity. Am. J. Hum. Genet. 71: 84-99, 2002. [PubMed: 12050823] [Full Text: https://doi.org/10.1086/341290]
Satre, M. A., Zgombic-Knight, M., Duester, G. The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene. J. Biol. Chem. 269: 15606-15612, 1994. [PubMed: 8195208]
Yokoyama, H., Baraona, E., Lieber, C. S. Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH. Genomics 31: 243-245, 1996. [PubMed: 8824810] [Full Text: https://doi.org/10.1006/geno.1996.0040]
Zgombic-Knight, M., Foglio, M. H., Duester, G. Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro. J. Biol. Chem. 270: 4305-4311, 1995. [PubMed: 7876191] [Full Text: https://doi.org/10.1074/jbc.270.9.4305]