Supplementary Figure 3: Sequence alignment between mHv1cc and other VSDs.
From: X-ray crystal structure of voltage-gated proton channel
Sequence alignment of Hv1 orthologs from different species. The red characters show the positions of conserved, periodically aligned arginine residues of S4. The orange and blue layers show the hydrophobic residues in a lower hydrophobic layer (HLin) and an upper layer (HLex), respectively. The green layers show the Zn2+ binding residues. Hv1 sequences of Homo sapiens (Hs), Mus musculus (Mm), Gallus gallus (Gg), Danio rerio (Dr), Xenopus laevis (Xl), Ciona intestinalis (Ci), Coccolithus pelagicu (Cp), Strongylocentrotus purpuratus (Sp, purple sea urchin), are aligned with mHv1cc, using Clustal W39. In S2–S3 linker of Hv1cc, the length increased by one residue when the original sequence of mHv1 was replaced by the corresponding region of Ci–VSP (underlined). Pro184 in Ci–VSP corresponds to Pro159 of mHv1cc. In order to avoid confusion, Pro159 (shown by the red asterisk) of mHv1cc was re–assigned to Pro158a.
