Required for normal hearing. It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti. Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture. Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens. Component of a multimeric complex consisting of several cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin, and IQGAP1. Colocalizes with AKAP9 at the Golgi apparatus as well as, to a lesser extent, the centrosome (By similarity). Associates with the cortical actin cytoskeleton (By similarity). Localizes to the apical region of cochlear hair cells, at the base of the actin-rich hair bundle (PubMed:17021174). Colocalizes with podocalyxin at the apical cell membrane in renal glomeruli (By similarity). May localize to the centrosome in lens epithelial cells (By similarity). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). Detected in cochlea, in cochlear and vestibular hair cell bundles in the organ of Corti (at protein level). Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity). Belongs to the chloride channel CLIC family.