XB-IMG-147740
Xenbase Image ID: 147740
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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) Copyright © 2015. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View |
