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. 2013 Sep 11;8(9):e73136. doi: 10.1371/journal.pone.0073136

Figure 2. Primary structure of OAIP-1.

Figure 2

(A) Sequence of transcript encoding the OAIP-1 prepropeptide precursor isolated from an S. plumipes venom-gland cDNA library. The 3′ and 5′ untranslated region (UTR), signal sequence, propeptide region, and mature toxin are labeled. The “GR” dipeptide sequence at the end of the mature toxin sequence is labeled AS (amidation signal) as it is a signal for C-terminal amidation. (B) Amino acid sequence of OAIP-1 prepropeptide precursor obtained from in silico translation of the cDNA sequence shown in panel (A). (C) Comparison of the amino acid sequence of the mature OAIP-1 toxin obtained from in silico translation of the venom-gland prepropeptide transcript with the N-terminal sequences obtained from Edman degradation of the native toxin at the APAF and APC protein sequencing facilities. (D) Alignment of OAIP-1 primary structure with the two closest hits obtained from a BLAST search against the ArachnoServer database. Identical residues are highlighted by white letters on a black background, while residues that are identical in two of the three sequences are shown on a gray background.