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. 2013 Dec 6;8(12):e81285. doi: 10.1371/journal.pone.0081285

Figure 3. Representative type I AFPs showing their diversity both within species and between species.

Figure 3

Symbols and coloring are as in Fig. 2A. A) Alignment of smaller skin and circulatory isoforms from winter flounder liver (WF-Liv, M63478.1) and skin (WF-skin, M63478.1), cunner (JF937681.2), shorthorn sculpin (SHS) SS-8 [38]and Liv5, longhorn sculpin (LHS, AF306348.1) and cunner (JF937681.2). Only WF-Liv possesses a signal peptide (lower case font, difference relative to WF-hyp in blue) and pro-peptide (italics) which is shown on the line above the mature AFP sequence. Amino acids encoded by codons interrupted by an intron in the cunner [71] and flounder liver sequences are indicated with a wavy underline. The intron within the flounder skin gene lies within the 5′ UTR. B) Sequence of the hyperactive type I AFP from winter flounder (WF-hyp, EU188795.1) denoted as in Fig. 2A. This circulating isoform is dimeric and possesses a signal peptide (lower case font) but no pro-sequence. C) Sequence of the two atypical type I AFPs of intermediate length from shorthorn sculpin skin (SHS-skin, AF305502.1) and dusky snailfish (AY455863.1). Thr is seldom found in position i of the 11 aa i, i+4, i+8 pattern of ice-binding residues and this pattern is not necessarily continuous in these longer AFPs. Neither AFP possesses a signal peptide or prosequence.