Aquaporin-2 (AQP-2) forms a water specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. It is e, Xenopus/Amphibian,pressed in the renal collecting tubules. Defects in AQP-2 are a cause of autosomal recessive nephrogenic diabetes insipidus (ANDI), also known as diabetes insipidus nephrogenic type 2. It is characterized by e, Xenopus/Amphibian,cessive water drinking (polydypsia) and urine e, Xenopus/Amphibian,cretion (polyuria). AQP-2 belongs to the MIP/aquaporin (TC1.A.8) family. Serine-264 has been identified as a phosphorylation site on AQP2 and shown to be regulated by vasopressin thus implicating this site as important in AQP2 trafficking and subcellular distribution.