Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver.
Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH: quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of zeta-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5' and 796 of the 3' nontranslated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.
Gonzalez
P
P
Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
Rao
P V
PV
Zigler
J S
JS
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D006224:Cricetinae; D003459:Crystallins / Q000235:genetics*; D004247:DNA / Q000235:genetics; D006801:Humans; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000235:genetics*; D015183:Restriction Mapping; D016415:Sequence Alignment
D003459:Crystallins; D004247:DNA; D016660:NAD(P)H Dehydrogenase (Quinone)