The present study reports spontaneous tyrosinase gene mutations identified in oculocutaneous albinos of three Japanese wild frog species, Pelophylax nigromaculatus, Glandirana rugosa and Fejervarya kawamurai. This represents the first molecular analyses of albinic phenotypes in frogs. Albinos of P. nigromaculatus collected from two different populations were found to suffer from frameshift mutations. These mutations were caused by the insertion of a thymine residue within each of exons 1 and 4, while albinos in a third population lacked three nucleotides encoding lysine in exon 1. Albinos from the former two P. nigromaculatus populations were also associated with splicing variants of mRNA that lacked either exons 2-4 or exon 4. In the other two frog species examined, missense mutations that resulted in amino acid substitutions from glycine to arginine and glycine to aspartic acid were identified in exons 1 and 3, respectively. The two glycines in F. kawamurai and G. rugosa, and the lysine deleted in one P. nigromaculatus albino, were highly conserved in vertebrates, which suggested that they were critically important to tyrosinase function. In fact, the glycine of G. rugosa is located within a predicted copper-binding domain. The five mutations identified in the present study are candidates for causing the albinic phenotypes, and, if directly confirmed, they are all unique to the vertebrates, which suggests that molecular analysis of albino frogs could contribute to research on albinos in humans and vertebrates by providing new information about tyrosinase structure and transcript processing.