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Figure 1 | BMC Physiology

Figure 1

From: Functional and pharmacological characterization of a Shal-related K+ channel subunit in Zebrafish

Figure 1

Comparison of zShals and mammalian Kv4s. A: Alignment of Danio rerio zShal3 amino acid sequence (NM_199802.1) with those of human Kv4.1 (NP_004970), human Kv4.2 (NP_036413) and the short splice variant of human Kv4.3 (AAF01045). Putative transmembrane domains and the pore region are indicated by horizontal bars. Potential PKC phosphorylation sites are indicated by open symbols, a potential PKA phosphorylation site is indicted by a solid symbol and a putative tyrosine phosphorylation site by a diamond. The T1 (or K+ channel tetramerisation domain) is a N-terminal, cytoplasmic tetramerisation domain of voltage-gated K+ channels encodes molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. This domain is present between amino acids 42 to 131 of zShal3 (IILNVS ... PEIISDC). zShal3 also contains the K+ channel signature sequence, which is a highly conserved stretch of amino acids (G- [YF]-G.-D) in the P-region. B: Phylogenetic tree comparing zShals with representative mammalian Kv channel subunits. The mammalian (all human) sequences used were Kv4.1 (NP_004970), Kv4.2 (NP_036413) and Kv4.3 (AAF01045): Multiple sequence alignment, tree bootstrapping and tree generation was performed using ClustalW.

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