Recently, two novel mammalian aquaporins (AQPs), AQPs 11 and 12, have been identified and classified as members of a new AQP subfamily, the "subcellular AQPs". In members of this subfamily one of the two asparagine-proline-alanine (NPA) motifs, which play a crucial role in selective water conduction, are not completely conserved. Mouse AQP11 (mAQP11) was expressed in Sf9 cells and purified using the detergent Fos-choline 10. The protein was reconstituted into liposomes, which were used for water conduction studies with a stopped-flow device. Single water permeability (pf) of AQP11 was measured to be 1.72 ± 0.03 × 10- 13 cm3/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels. © 2006 Elsevier B.V. All rights reserved.
Yakata, K., Hiroaki, Y., Ishibashi, K., Sohara, E., Sasaki, S., Mitsuoka, K., & Fujiyoshi, Y. (2007). Aquaporin-11 containing a divergent NPA motif has normal water channel activity. Biochimica et Biophysica Acta - Biomembranes, 1768(3), 688–693. https://doi.org/10.1016/j.bbamem.2006.11.005