Figure 5.
Sequence alignment of human JPH2, JPH1, JPH3, and JPH4. The different domains are color-coded in orange (MORNs), purple (joining domain), blue (α-helical domain), red (divergent domain), and green (TM domain). Residues that are identical or conserved among the four isoforms are indicated by asterisks or colons, respectively. The red underlining indicates the region of JPH1 that contains a binding site for CaV1.1 (Golini et al., 2011). The green underlining indicates the cysteine residues of JPH1 whose reactivity depends on the gating state of RYR1 (Phimister et al., 2007). Note that Cys 626 in the human JPH1 sequence reported here corresponds to Cys 627 of the rabbit JPH1 sequence described by Phimister et al. (2007). The residues highlighted in yellow near the C terminus of JPH3 indicates the region that appears to support a direct interaction of JPH3 with the cytoplasmic domain of RYR1.

Sequence alignment of human JPH2, JPH1, JPH3, and JPH4. The different domains are color-coded in orange (MORNs), purple (joining domain), blue (α-helical domain), red (divergent domain), and green (TM domain). Residues that are identical or conserved among the four isoforms are indicated by asterisks or colons, respectively. The red underlining indicates the region of JPH1 that contains a binding site for CaV1.1 (Golini et al., 2011). The green underlining indicates the cysteine residues of JPH1 whose reactivity depends on the gating state of RYR1 (Phimister et al., 2007). Note that Cys 626 in the human JPH1 sequence reported here corresponds to Cys 627 of the rabbit JPH1 sequence described by Phimister et al. (2007). The residues highlighted in yellow near the C terminus of JPH3 indicates the region that appears to support a direct interaction of JPH3 with the cytoplasmic domain of RYR1.

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