CLHM-1 is a pore-forming subunit of a voltage-gated ion channel. It exhibits permeability to monovalent cations, divalent cations, and anions, displaying a selectivity pattern of Ca(2+) > Mg(2+) > Na(+) = K(+) > Cl(-). This protein functions as both a voltage-gated and calcium-activated ion channel. CLHM-1 is essential for normal locomotion.
Gene References Into Functions
Mutations in ceCLHM-1, specifically at valine 9 and glutamine 13, resulted in alterations in half-maximal activation and voltage dependence, respectively. In the absence of Ca(2+) (0 Ca(2+) In) and presence of 2 mM Ca(2+) in the external environment (2 mM Ca(2+)o), the ceCLHM-1 NH2-terminal deletion and point mutant channels exhibited complete closure at hyperpolarized voltages. Notably, their apparent affinity for Ca(2+)o remained indistinguishable from that of the wild-type ceCLHM-1. PMID: 28515089
Research findings indicate that CLHM-1 is a functionally conserved ion channel that plays a crucial, albeit potentially toxic, role in the function of excitable cells. PMID: 23884934