Recombinant Human Aquaporin-2 (AQP2) Protein

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)

Subcellular Location

Apical cell membrane (Multi-pass membrane protein); Basolateral cell membrane (Multi-pass membrane protein); Cell membrane (Multi-pass membrane protein); Cytoplasmic vesicle membrane (Multi-pass membrane protein); Golgi apparatus, trans-Golgi network membrane (Multi-pass membrane protein)

Disease Association

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

Tissue Specificity

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

Subunit

Homotetramer (PubMed:24733887). Interacts with micropeptide MIAC; the interaction leads to a reduction of filamentous actin fibers and inhibition of the EREG/EGFR signaling pathway (PubMed:32176498, PubMed:36117171)

• Deen P.M.T. et al. Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. — Science (1994)
• Uchida S. et al. Isolation of human aquaporin-CD gene. — J. Biol. Chem. (1994)
• van Lieburg A.F. et al. Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene. — Am. J. Hum. Genet. (1994)
• Sasaki S. et al. Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct. — J. Clin. Invest. (1994)
• Marr N. et al. Heterooligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus. — Hum. Mol. Genet. (2002)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Abrami L. et al. Glycerol permeability of mutant aquaporin 1 and other AQP-MIP proteins: inhibition studies. — Pflugers Arch. (1996)
• van Balkom B.W.M. et al. The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel. — J. Biol. Chem. (2002)