Structural highlights
Function
AQP3_RAT 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).[UniProtKB:Q8R2N1][UniProtKB:Q92482][1] [2]
References
- ↑ Ishibashi K, Sasaki S, Fushimi K, Uchida S, Kuwahara M, Saito H, Furukawa T, Nakajima K, Yamaguchi Y, Gojobori T, et al.. Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6269-73. PMID:7517548 doi:10.1073/pnas.91.14.6269
- ↑ Echevarria M, Windhager EE, Tate SS, Frindt G. Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10997-1001. PMID:7526388 doi:10.1073/pnas.91.23.10997
