We determined the partial cDNA of Type II procollagen ${alpha}1$[pro-${alpha}1$(II)] chain (1802 bp) of the skate Raja kenojei, which codes 581 amino acid residues. The partial structure of the pro-${alpha}1$(II) chain consisted of a part of triple helical region (309 residues) and a C-domain (272 residues). Comparing the chain to other vertebrates showed relatively low homology (about 50%) at the amino acid level. However, eight Cys residues in the C-domain of the skate pro-${alpha}1$(II) chain were conserved in common with those of other vertebrates. The skate pro-${alpha}1$ (II) chain mRNA was detected by RT-PCR of various tissues, but was undetected in tissues containing Type II collagen. The low homology and unexpected expression pattern suggest the presence of another mRNA variant of the skate pro-${alpha}1$(II) chain. The present study is the first report of the primary structure of pro-${alpha}1$(II) chain in an elasmobranch.