Fig. 3. Amino acid sequences of three plateins, derived from their respective nucleotide sequences. The proteins are arrayed to display their respective repetitive domain structures. N-terminal signal sequences (predicted by SignalP V1.1 for 1 and 2; directly determined for ß/) are highlighted in yellow. The primary repetitive sequences (VP-rich 12-mers, with some degeneracy) are indicated in red; the secondary proline-rich pentameric repeats are shown in blue. Note the inversion of primary and secondary repeat domains between the - and ß/-plateins. Sequences found within one of the -isoforms, but missing from the other, are highlighted in light gray; the corresponding gaps in the other isoform (representing deletions from the aligned sequences) are indicated with lines. Sequences corresponding to the tryptic peptides from -platein (Table 1) are underlined. For ß/-platein, the ß-tryptic peptides are in double underline, and the -peptides (and actual N-terminal sequence) in single underline; sequences common to both are in wavy underline. Residues that show very high prediction values as phosphorylation substrates (0.9 output values using NetPhos 2.0) are highlighted in darker gray.