Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Urine water channel) (Water channel protein for red blood cells and kidney proximal tubule)
1_MASEF 6_ KKKLF 11_ WRAVV 16_ AEFLA 21_ TTLFV 26_ FISIG 31_ SALGF 36_ KYPVG 41_ NNQTA 46_ VQDNV 51_ KVSLA 56_ FGLSI 61_ ATLAQ 66_ SVGHI 71_ SGAHL 76_ NPAVT 81_ LGLLL 86_ SCQIS 91_ IFRAL 96_ MYIIA 101_ QCVGA 106_ IVATA 111_ ILSGI 116_ TSSLT 121_ GNSLG 126_ RNDLA 131_ DGVNS 136_ GQGLG 141_ IEIIG 146_ TLQLV 151_ LCVLA 156_ TTDRR 161_ RRDLG 166_ GSAPL 171_ AIGLS 176_ VALGH 181_ LLAID 186_ YTGCG 191_ INPAR 196_ SFGSA 201_ VITHN 206_ FSNHW 211_ IFWVG 216_ PFIGG 221_ ALAVL 226_ IYDFI 231_ LAPRS 236_ SDLTD 241_ RVKVW 246_ TSGQV 251_ EEYDL 256_ DADDI 261_NSRVE
1: Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues (PubMed:1373524, PubMed:23219802). Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2) (PubMed:16682607, PubMed:17012249, PubMed:19273840, PubMed:33028705, PubMed:8584435). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol (PubMed:17012249, PubMed:35835865). In vitro, it shows non-selective gated cation channel activity and may be permeable to cations like K(+) and Na(+) in vivo (PubMed:36949749, PubMed:8703053)