Figure S1. PN1 protein sequences The alignment was performed using Clustal Omega multiple sequence alignment (EMBL-EBI) (Sievers et al., 2011). Identical amino acids are indicated with asterisks, similar residues with double points, and semi-conserved with single points. The RCL is indicated with a blue box and the SERPIN signature with a yellow box as determined by ScanProsite (http://prosite.expasy.org/scanprosite/) (Sigrist et al., 2010). The P1-P1’ reactive site scissile bond in the RCL is indicated with a downward arrow (McGrogan et al., 1988). (A) The signal peptide cleavage sites of Xenopus laevis PN1.a and PN1.b. were determined using SignalP 4.0 (Petersen et al., 2011) and are marked with an arrowhead. Boxes show the Heparin binding site (Stone et al., 1994) and the two N-Gly sites (predicted using the program NetNGlyc 1.0 Server (http://www.cbs.dtu.dk/services/NetNGlyc/). The numbers at the end of the sequences indicate the total length of the proteins. NCBI GenBank accession numbers are: PN1.a, DQ324047; PN1.b, BC077742. N-Gly, N-linked glycosylation; RCL, reactive center loop; SERPIN, serine protease inhibitor. (B) Conserved functional domains of vertebrate PN1 proteins. Positive and negative amino acids in the heparin binding side are indicated in green and red, respectively. Px indicates amino acid positions in the RCL. Dr, zebrafish; Gg, chicken, Hs, human; Mm, mouse; Xl, African claw frog; Xt, Western clawed frog.
Image published in: Acosta H et al. (2015)
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