Supplementary Figure 1: Sequence alignment for PC2 and related orthologs.
From: Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)
The sequence of human PC2P185-D723 (hsPC2; TRPP1) is shown along with the corresponding PC2 sequences from C. elegans (ce) and D. melanogaster (dm). The alignment also includes sequences for human PKD2L1 (TRPP2; aa 65-603), PKD2L2 (TRPP3; aa 1-534), PKD1 (aa 3635-4147) and PKDREJ (aa 1677-2208). Residues conserved in all sequences are boxed and colored dark blue. Secondary structural elements derived from the PC2 EM model (see Fig. 2a and b) are shown above the alignment and colored by domain. Dashed regions represent residues that were not resolved in the EM model. Glycosylation sites in the human PC2 protein are highlighted by green hexagons. A selection of residues that are mutated in ADPKD patients in PC1 or PC2 are shown as colored circles under the alignment with the amino acid change indicated. The color of the circles indicates the predicted impact of the variant on the structure of the protein (colored according to classification in Supplementary Table 1; yellow: minimal predicted impact on the structure; magenta: serious predicted impact on the structure). Uniprot accession codes: hsPC2 (Q13563), cePC2 (Q9U1S7), dmPC2 (Q9VK95), hsPKD2L1 (Q9P0L9), hsPKD2L2 (Q9NZM6), hsPC1 (P98161) and hsPKDREJ (Q9NTG1). The asterisk (*) indicates the location of a large 90 amino acid insertion in the α2b-β0 loop in the fruit fly sequence (dmPC2, residues 328-418) that has been omitted for clarity.
