slo protein has seven hydrophobic domains near

the amino terminus, a structure that is similar to other known

K+-channel polypeptides. Similarities are observed between the slo

protein and other voltage-gated channels in the S4 domain which is thought

to mediate voltage sensitivity. The greatest similarity to other

K+-channel polypeptides is in the H5 domain, an integral part of the ion

conduction pore. Outside of these two regions, the slo protein is

distinct from all known K+ channels. A putative EF-hand domain and an

ATP-binding site were identified. The protein sequence is probably

incomplete at the amino terminus.