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Aquaporin-2 phospho S256

Domain

Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

Function

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 (PubMed:15509592, PubMed:7510718, PubMed:7524315, PubMed:8140421, PubMed:8584435). Plays an essential role in renal water homeostasis (PubMed:15509592, PubMed:7524315, PubMed:8140421). Could also be permeable to glycerol (PubMed:8584435).

Involvement in disease

Diabetes insipidus, nephrogenic, 2, autosomal

NDI2

A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent.

N-glycosylated.

Sequence Similarities

Belongs to the MIP/aquaporin (TC 1.A.8) family.

Tissue Specificity

Expressed in collecting tubules in kidney medulla (at protein level) (PubMed:7510718). Detected in kidney (PubMed:7510718).

Cellular localization

Alternative names

Aquaporin-2, AQP-2, ADH water channel, Aquaporin-CD, Collecting duct water channel protein, WCH-CD, Water channel protein for renal collecting duct, AQP-CD, AQP2

swissprot:P41181