Figure 3.

Amino acid alignment. Sea bass Slc11a2-α and Slc11a2-β's were aligned with striped bass Slc11 (AAG31225), turbot Slc11a2-β (ABB73023) and Slc11a2-γ (ABE97051), fugu Slc11a2-α (CAD43050) and Slc11a2-β (CAD43051), trout Slc11a2-α (AAD20721) and Slc11a2-β (AAD20722), human SLC11A1 (NP_000569), human SLC11A2 +IRE (NP_000608) and human SLC11A2 -IRE (AAC21459). Identical residues and gaps are indicated by dots and dashes, respectively. Signature features and putative motifs and highlighted as follows: yellow, transmembrane domains; red, conserved transport motif; violet, N-linked glycosilation site; pink, protein kinase C phosphorylation site; light green, casein kinase II phosphorylation site; olive green, tyrosine kinase phosphorylation site; gray, tyrosine based sorting signal; cyan, conserved cysteine residues; dark green, N-myristoylation sites

Neves et al. BMC Evolutionary Biology 2011 11:106   doi:10.1186/1471-2148-11-106
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