biostudies-literatureChauvigne FNorges Forskningsråd462https://www.ebi.ac.uk/biostudies/studies/S-EPMC6906440biostudies-literatureUnknown2Water channels (aquaporins) were originally discovered in mammals with fourteen subfamilies now identified (AQP0-13). Here we show that a functional Aqp14 subfamily phylogenetically related to AQP4-type channels exists in all vertebrate lineages except hagfishes and eutherian mammals. In contrast to the water-selective classical aquaporins, which have four aromatic-arginine constriction residues, Aqp14 proteins present five non-aromatic constriction residues and facilitate the permeation of water, urea, ammonia, H₂O₂ and glycerol. Immunocytochemical assays suggest that Aqp14 channels play important osmoregulatory roles in piscine seawater adaptation. Our data indicate that Aqp14 intracellular trafficking is tightly regulated by the vasotocinergic/isotocinergic neuropeCommunications biologyThe vertebrate Aqp14 water channel is a neuropeptide-regulated polytransporter.PMC6906440294768/E40254872/E40Fjelldal PGCerda JFinn RNYilmaz OChauvigne FFerre AfalseThe vertebrate Aqp14 water channel is a neuropeptide-regulated polytransporter.Water channels (aquaporins) were originally discovered in mammals with fourteen subfamilies now identified (AQP0-13). Here we show that a functional Aqp14 subfamily phylogenetically related to AQP4-type channels exists in all vertebrate lineages except hagfishes and eutherian mammals. In contrast to the water-selective classical aquaporins, which have four aromatic-arginine constriction residues, Aqp14 proteins present five non-aromatic constriction residues and facilitate the permeation of water, urea, ammonia, H₂O₂ and glycerol. Immunocytochemical assays suggest that Aqp14 channels play important osmoregulatory roles in piscine seawater adaptation. Our data indicate that Aqp14 intracellular trafficking is tightly regulated by the vasotocinergic/isotocinergic neurope2019-01-01T00:00:00Z20192026-05-01T22:04:13.72Z2020-05-21T23:48:52ZS-EPMC69064403184010710.1038/s42003-019-0713-y