Figure 1

Prediction of secondary structure and putative post-translational modification sites in the human STC1 amino acid sequence. Linear representation of STC1-HT amino acid sequence with assignment of its different regions from N- to C-terminus: signal peptide (purple), pro-peptide (dark gray), mature protein (black), linker regions (light grey), TEV protease cleavage site (green) and 6 × His-tag (light blue). In the amino acid sequence, relevant residues are emphasized by the following color code: Cys: red, Asp predicted to be N-glycosylated: green, Lys predicted to be sumoylated: magenta, Ser, Thr e Tyr residues predicted to be phosphorylated: blue. The conserved pattern of experimentally determined disulfide bridges from salmon STC1 is indicated by black horizontal brackets. Similarly the homo-dimerization Cys is indicated in black (dimer). Below the sequence there is a schematic representation of the predicted consensus secondary structure, obtained by six different prediction programs (red: alpha helix, yellow: beta-sheet, green: coil regions, black: not assigned). The numbers below the secondary structure represent the score (1-6, indicating how many of the six programs predicted the respective secondary structure element). Furthermore, in a second line, a prediction indicates whether a residue is exposed (e) or buried (b). At the bottom, predictions of three programs for ordered/disordered regions are given: FoldIndex (red: unfolded, green: folded), GlobPlot (green: globular, blue: disordered) and DisEMBL (blue: loops or coils, red: hot loops, green: missing coordinates).