ClC-5 can form both homo- and hetero-dimers due to its marked sequence homology with ClC-3 and ClC-4, and has 18 membrane spanning -helices.
ClC-5 is mainly expressed in the kidney, in particular in proximal tubules where it participates to the uptake of albumin and low-molecular-weight proteins, which is one of the principal physiological role of proximal tubular cells. ClC-5 can form both homo- and hetero-dimers due to its marked sequence homology with ClC-3 and ClC-4. The canonical 746-amino acid ClC-5 protein has 18 membrane spanning -helices (named A to R), an intracellular N- terminal domain and a cytoplasmic C-terminus containing two cystathionine beta-synthase (CBS) domains which are known to be involved in the regulation of ClC-5 activity. 
