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. Author manuscript; available in PMC: 2017 Sep 1.
Published in final edited form as: Ecology. 2016 Sep;97(9):2232–2239. doi: 10.1002/ecy.1455

Fig. 1.

Fig. 1

Structural architecture and domain organization of barnacle (Balanus glandula) MULTIFUNCin (from Ferrier 2010, Ferrier et al. submitted), a 199.6 kDa glycoprotein cue with 1567 amino acids (1 = amino terminus; 1567 = carboxy terminus). A signal peptide, modified thioester motif, and conserved domains and regions are denoted by color-specific rectangles. Amino acid positions of N-glycosylation sites are provided (closed circles), as well as the site of a putative catalytic histidine (*). Vertical lines with bold numbers denote cysteine positions. The estimated location of disulfide bridges are marked with horizontal lines connecting bold cysteine residues. Abbreviations: A2M, α2-macroglobulin; KGD, lysine-glycine-aspartic acid; C3, C4, and C5, complement factor proteins 3, 4 and 5.