134813.fig.001a
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134813.fig.001b
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Figure 1: Schematic representation of hCaMKP, hCaMKP-N(WT), hCaMKP-N(1–559), and zCaMKP-N. (a) Comparison of the primary structure of hCaMKP-N with that of hCaMKP. The regions that show significant homology are shown in grey. (b) Domain structures of hCaMKP-N(WT), hCaMKP-N(1–559), and z-CaMKP-N. Catalytic domains are shown in dark grey, and the hatched bars within them indicate the PP2C motif that is characteristic of PPM family phosphatases. Black bars show the antibody recognition site. In hCaMKP-N, the recognition site is located just to the N-terminal side of the putative processing site. The amino acid sequences of the antibody recognition site in human, rat, and zebrafish CaMKP-N are also indicated. Underline shows the amino acid sequence used for generating the anti-CaMKP-N antibody. Closed arrowheads show the position of Cys436, which may be responsible for redox regulation of the phosphatase activity (see text). It has been reported that two nuclear localization signals are located in the region that is C-terminal side to Arg668 on hCaMKP-N (shown in light grey). The 575–587 region of zCaMKP-N reportedly functions as a nuclear localization signal (shown in light grey) [8]. The amino acid residue numbers of the respective phosphatases are also shown.