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. 2015 Mar 18;7(3):951–970. doi: 10.3390/toxins7030951

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Biosynthetic skin prepropeptides are identified from skin secretion of multiple species from Ranidae. (a) Three BRP precursors are identified from Lithobates palustris; (b) Four skin prepropeptides are identified from Rana guentheri; (c) Four prepropeptides were discovered from Rana chensinensis; (d) The skin prepropeptides containing single copies were discovered in skin secretion of multiple Ranidae species. The access numbers of the Uniprot database are shown at the head of each precursor. The regions shown in italic typeface are signal peptides. Classic prepropeptide convertase processing sites, –KR–, are shown in bold typeface. The regions with a single underline indicate highly conserved sequences as compared to conventional BK.

Biosynthetic skin prepropeptides are identified from skin secretion of multiple species from Ranidae. (a) Three BRP precursors are identified from Lithobates palustris; (b) Four skin prepropeptides are identified from Rana guentheri; (c) Four prepropeptides were discovered from Rana chensinensis; (d) The skin prepropeptides containing single copies were discovered in skin secretion of multiple Ranidae species. The access numbers of the Uniprot database are shown at the head of each precursor. The regions shown in italic typeface are signal peptides. Classic prepropeptide convertase processing sites, –KR–, are shown in bold typeface. The regions with a single underline indicate highly conserved sequences as compared to conventional BK.