Fig. 2: Sequence alignment and homology model of Ci-Hv1.
From: Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel
a Sequence alignment of S1–S4 voltage-sensing domains for Ci-Hv1 and hHv1. Conserved residues are highlighted with dark blue. Residue numbers are marked above for reference and the helical schematic above the alignment marks the extent of the helices in the homology model of Ci-Hv1, while residues that were mutated to Cys or Ala/Trp are indicated by red rectangles. Sequences included in the alignment are: Ciona intestinalis Hv1 (UniProtKB - Q1JV40), Human Hv1 (UniProtKB - Q96D96), visualized by Jalview42. b Homology model of the S1-S4 voltage-sensing domains for Ci-Hv1 based on mHv1 structure (PDB ID: 3WKV). Predicted domains are color coded as follows: S1 (blue), S2 (cyan), S3 (light green), S4 (orange). Membrane boundaries are estimated from superposition with the Kv1.2/2.1 paddle chimera structure where detergents and PCs (phosphatidylcholine) are resolved. TAMRA -MTS attached to E241C is represented in yellow, while the two histidine residues at position 179 and 188 are highlighted by magenta. This panel was created with UCSF Chimera43 and the final image rendered with ChimeraX44.
