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. 2018 Jan 16;16(1):31. doi: 10.3390/md16010031

Figure 6.

Figure 6

The molecular signature of shrimp Type II crustins. (A) Amino acid sequence alignments of the C-terminal region holding the 12 conserved cysteine residues (the crustin signature [39]) of Type IIa and Type IIb crustins from penaeid shrimp: Litopenaeus vannamei (Crustin Lv1, Crustin Lv3, LvCrustin I, LvCrustin P, Crustin-like Lv), Litopenaeus setiferus (Crustin Ls1, Crustin Ls2, Crustin Ls3), Litopenaeus schmitti (CrusLsch), Farfantepenaeus paulensis (CrusFpau), Farfantepenaeus brasiliensis (CrusFbra), Farfantepenaeus subtilis (CrusFsub), Fenneropenaeus chinensis (Fc-crus 2, CruFc), Fenneropenaeus indicus (Fi-crustin), Penaeus monodon (crustinPm1, crustinPm4, crustinPm5, crustinPm6, crustinPm7, Crustin-like Pm), and Marsupenaeus japonicus (Crustin Mj, Crustin-like Mj). (B) Consensus amino acid sequence of shrimp Type IIa and Type IIb crustins. X indicates any amino acid. Identical residues are highlighted in black. Specific amino acid residues conserved in shrimp Type IIa and Type IIb crustins are highlighted in blue and yellow, respectively. Triangles (▼) indicate the 12 conserved cysteine residues found in crustins. The whey acidic protein (WAP) domain is underlined by a solid red line. (C) A not-to-scale representation of shrimp Type IIa and Type IIb crustins indicating the N-terminal glycine-rich region and the C-terminal crustin signature (cysteine-rich region + WAP domain). MW: molecular weight. pI: theoretical isoelectric point. * Sequence obtained from [16] (not deposited in any database).