Cloning and characterization of a novel splicing variant of the ZADH1 gene.
We report here the cloning and characterization of a novel splicing variant of the human zinc binding alcohol dehydrogenase, domain containing 1 (ZADH1) gene. ZADH1 is localized on chromosome 14q24.2. The cDNA of this splicing variant is 1613 base pairs in length, and encodes a 351-amino acid protein with a putative molecular weight of 38.5 kDa. We named the novel splicing variant ZADH1b. By MTC- panel PCR analysis, it was found that ZADH1b was widely expressed in human tissues. Computer analysis revealed ZADH1 had a potential ADH_zinc_N domain and it had considerable homology with some dehydrogenases. It was speculated that ZADH1 may have definite metabolic roles in vivo as a dehydrogenase.
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, China.
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D011452:15-Oxoprostaglandin 13-Reductase; D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis; D006801:Humans; D008969:Molecular Sequence Data; D022821:RNA Splice Sites; D012326:RNA Splicing; D016415:Sequence Alignment; D014018:Tissue Distribution
D018076:DNA, Complementary; D022821:RNA Splice Sites; D000426:Alcohol Dehydrogenase; D011452:15-Oxoprostaglandin 13-Reductase; C485698:PTGR2 protein, human