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Fig. 1. Comparison of the amino acid sequences of two types of medaka Wap65, mWap65-1 and mWap65-2, with those of fish Wap65s and mammalian hemopexins, including goldfish Wap65 (Kikuchi et al., 1995), carp Wap65 (Kinoshita et al., 2001), rainbow trout hemopexin-like protein (Miot et al., 1996) and hemopexins of rabbit (Morgan et al,. 1993), rat (Nikkilä et al., 1991) and human (Altruda et al., 1985; Takahashi et al., 1985). Amino acids identical to those of mWap65-1 are shown as dots; gaps introduced to maximize the alignment are represented by hyphens. Lightly shaded boxes indicate conserved cysteine residues, and heavily shaded boxes indicate conserved histidine residues that are thought to serve as heme axial ligands (Paoli et al., 1999). Conserved histidine residues in all Wap65s are shown by blue boxes, and conserved histidine residues in all except for mWap65-2 by green boxes. Black arrowheads in Wap65s and hemopexins (not mWap65-2) indicate cleavage sites for secreted proteins when data are available. The predicted signal peptide regions of mWap65-1 and mWap65-2 were defined using SignalP program and are underlined. White arrowheads in mWap65-1 and mWap65-2 indicate predicted cleavage sites used for the construction of expression vectors for recombinant mWap65-1 and mWap65-2. Potential N-glycosylation sites predicted using PROSITE are shown by red boxes. The numbers in the right margin represent those of amino acids from the N-terminal methionine in premature proteins.

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