We report the sequencing and identification on chromosome X of Sacchar
omyces cerevisiae of an open reading frame whose product, designated y
ClC-1, displays significant structural similarity to a voltage-gated C
l- channel family. This putative protein contains 13 hydrophobic domai
ns very similar to transmembrane domains exhibited by known members of
this family. Some amino acids in the domains and at the loops between
them are well conserved among all members. This is the first voltage-
gated Cl- channel described in the yeast S. cerevisiae. The identifica
tion of yClC-1 will facilitate the functional analysis of Cl- channels
in general, and should also assist in the identification of other ClC
genes in higher eukaryotes.