Figure 1.
Bayesian phylogeny of TRPV1 illustrates that there is a single copy of this gene is conserved across different vertebrates.
Bayesian phylogenetic tree of TRPV1 proteins from mammals (red) birds-reptiles (yellow) and fishes (green) was generated using MrBayes 3.2 [52]. Percentage posterior probabilities are marked at the node of the branches while mean branch length is marked in decimal on the respective branch. Putative TRPV like gene (JGI accession id e_gw1.02q.75.1) from “Ciona intestinalis” served as out-group in this phylogenetic tree.
Figure 2.
Conservation analysis with TRPV1 in comparison to histone H4 and cytochrome C.
Figure 3.
Analysis of conservation of different domains, motifs and interacting sites in TRPV1.
The lower value indicates more conservation and higher value indicates less conservation. Different regions of the TRPV1 are indicated by different colors. Ank: Ankyrin repeat region, TM: Transmembrane region, L: Loop region, CBD: Cholesterol-binding domain, P-loop; Pore loop, TRP-box: Signature motif for TRP box, TBS-1: Tubulin binding sequence 1, TBS-2: Tubulin binding sequence 2, TAD-1: Tetrameric assembly domain 1, TAD-2: Tetrameric assembly domain 2, Cam: Calmodulin binding region, NT: N-terminal cytoplasmic domain of TRPV1, MID: Middle portion of TRPV1, CT: C-terminus of TRPV1, FL: Full length TRPV1, Histone 4: Histone 4. All values are significant (P<0.0001, Kuskal-Wallis test).
Figure 4.
The primary sequence of TBS-1 and TBS-2 are semi-conserved throughout the evolution.
The conservation of the basic amino acids is indicated.
Figure 5.
Distribution of positively charged residues within the TBS-1 and TBS-2 are evolutionary conserved.
a. The distribution of positively charged residues located within TBS-1 and TBS-2 of human TRPV1 are represented in a 360° circular wheel. b. The helix formed by TBS-1 and TBS-2 from different species are superimposed and the distribution of positively charged residues are represented in a 360° circular wheel. The positions are marked by alphabets and A indicated the position of first positively charged residues in the helical wheel that has been placed at 0° angle. The distribution of positively charged residues in both TBS-1 and TBS-2 remain much conserved. Residues - lysine (K), arginine (R) and histidine (H) are represented by red green, and the indigo dots, respectively.
Table 1.
Description of different domains and motifs.