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. 2000 May;123(1):111–124. doi: 10.1104/pp.123.1.111

Figure 1.

Figure 1

Deduced protein sequences of two authentic aquaporins (MIP-A and MIP-B) and seven putative PM- and tonoplast-MIPs from M. crystallinum are compared with Arabidopsis RD28 and bean α-TIP. Three of the nine sequences have been reported previously (Yamada et al., 1995; accession nos: MIP-A, L36095; MIP-B, L36097; MIP-C, U73466; MIP-D, U26537; MIP-E, U73467; MIP-F, U43291; MIP-H, AF133530;MIP-I, AF133531; and MIP-K,AF133532). Putative transmembrane regions are marked by double arrows above the sequences. The signature motifs (NPA) for aquaporins are shown in bold. Sequences used for oligopeptide synthesis are underlined. Cys residues were added to the amino termini of MIP-F oligopeptides. Cys were acetylated for conjugation to agarose prior to affinity purification of the crude serum. The other oligopeptides utilized a Cys that was present in the sequences.