Molecular cloning and functional analysis of a cDNA coding for human DOPAchrome tautomerase/tyrosinase-related protein-2.
We have cloned the cDNAs encoding tyrosinase-related protein-2 (TRP-2) from a human melanoma cDNA library. Transient expression of the isolated cDNA in HeLa cells established that TRP-2 is DOPAchrome tautomerase. Human TRP-2/DOPAchrome tautomerase is composed of 519 amino acids with a molecular weight of 59,000 and has about 84% identity with the mouse counterpart.
Yokoyama
K
K
Department of Applied Physiology and Molecular Biology, Tohoku University School of Medicine, Miyagi, Japan.
Suzuki
H
H
Yasumoto
K
K
Tomita
Y
Y
Shibahara
S
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000096:biosynthesis* / Q000737:chemistry; D015870:Gene Expression; D006367:HeLa Cells; D006801:Humans; D019746:Intramolecular Oxidoreductases; D007535:Isomerases / Q000235:genetics*; D008545:Melanoma / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D018076:DNA, Complementary; D007535:Isomerases; D019746:Intramolecular Oxidoreductases; C042501:dopachrome isomerase