Aqp3
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
Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient (PubMed:7517548, PubMed:7526388). Could also be permeable to urea (PubMed:7517548, PubMed:7526388). Also participates in cell permeability to H2O2 and H2O2-mediated signaling (By similarity). In skin, transports glycerol to the epidermis and stratum corneum, where it maintains hydration, elasticity, and supports lipid biosynthesis for barrier repair. In kidney, contributes to the reabsorption of water, helping the body maintain proper fluid balance (By similarity).
Sequence Similarities
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Tissue Specificity
Detected in kidney medulla and papilla, in collecting duct cells (PubMed:7517548, PubMed:7526388). Detected in colon (PubMed:7517548).
Cellular localization
- Cell membrane
- Multi-pass membrane protein
- Basolateral cell membrane
- Multi-pass membrane protein
Alternative names
Aquaporin-3, AQP-3, 31.4 kDa water channel protein, Aquaglyceroporin-3