An alignment of vertebrate preproendothelin-1 protein sequences.

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An alignment of vertebrate preproendothelin-1 protein sequences. An alignment of vertebrate preproendothelin-1 protein sequences. (A) Similar amino acid residues [based on the BLOSUM 62 score table (Eddy, 2004)] are highlighted in gray, as compared to human preproendothelin-1. The cleavage sites for furin (inverted triangles) and ECE1 (†) are indicated. Asterisks mark every 20th amino acid. (B) Predicted active EDN1 structure from the killifish, modeled after Webb (Webb, 1997). Amino acids different from human EDN1 are highlighted in gray. Two disulfide bonds are indicated at Cys1–Cys15 and Cys3–Cys10. GenBank and Ensembl accession numbers are listed in Fig. 1, except for platypus EDN1, ENSOANP00000011454 and opossum EDN1, XP_001377153.1. Kelly A. Hyndman, and David H. Evans J Exp Biol 2007;210:4286-4297 © The Company of Biologists Limited 2007