Aquaporins/major intrinsic proteins (MIP) are a family of water-selective membrane channels. Aquaporin-7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. Aquaporin-7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin-7 facilitates water, glycerol and urea transport. It may play an important role in thermoregulation in the form of perspiration, and sperm function.[6]
Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated water transport". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. doi:10.3181/00379727-219-44332. PMID9824541. S2CID28952956.
Kuriyama H, Kawamoto S, Ishida N, et al. (1998). "Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability". Biochem. Biophys. Res. Commun. 241 (1): 53–8. doi:10.1006/bbrc.1997.7769. PMID9405233.
Ishibashi K, Yamauchi K, Kageyama Y, et al. (1998). "Molecular characterization of human Aquaporin-7 gene and its chromosomal mapping". Biochim. Biophys. Acta. 1399 (1): 62–6. doi:10.1016/s0167-4781(98)00094-3. PMID9714739.
Suzuki-Toyota F, Ishibashi K, Yuasa S (1999). "Immunohistochemical localization of a water channel, aquaporin 7 (AQP7), in the rat testis". Cell Tissue Res. 295 (2): 279–85. doi:10.1007/s004410051234. PMID9931374. S2CID30916397.