1.A.8.9.14 Glycerolaquaporin 9, Aqp9 of 295 aas and 6 TMSs. Transports water, glycerol and arsenic trioxide, As2O3 (Palmgren et al. 2017). Primary APL cells express AQP9 significantly (2-3 logs) higher than other acute myeloid leukemia cells (AMLs), explaining their exquisite As2O3 sensitivity (Leung et al. 2007). AQP-7 and AQP-9-mediated glycerol transport in tanycyte cells may be
under hormonal control to use glycerol as an energy source during the
mouse estrus cycle (Yaba et al. 2017). It transports multiple neutral and ionic arsenic species including arsenic trioxide, monomethylarsenous acid (MAs(III)) and dimethylarsenic acid (DMA(V)). It also transports clinically relevant selenium species including monomethylselenic acid (MSeA), especially at acidic pH. FCCP, valinomycin and nigericin do not significantly inhibit MSeA uptake, but AQP9 also transport ionic selenite and lactate, with low efficiency compared with MSeA uptake. Selenite and lactate uptake is pH dependent and inhibited by FCCP and nigericin but not valinomycin. The selenite and lactate uptake via AQP9 can be inhibited by different lactate analogs. AQP9 transport of MSeA, selenite and lactate is inhibited by an AQP9 inhibitor, phloretin, and the AQP9 substrate, arsenite (As(III)) (Geng et al. 2017).
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Accession Number: | O43315 |
Protein Name: | Aquaporin-9 |
Length: | 295 |
Molecular Weight: | 31431.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 6 |
Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
Substrate |
arsenic trioxide, As2O3, glycerol, water |
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1: MQPEGAEKGK SFKQRLVLKS SLAKETLSEF LGTFILIVLG CGCVAQAILS RGRFGGVITI
61: NVGFSMAVAM AIYVAGGVSG GHINPAVSLA MCLFGRMKWF KLPFYVGAQF LGAFVGAATV
121: FGIYYDGLMS FAGGKLLIVG ENATAHIFAT YPAPYLSLAN AFADQVVATM ILLIIVFAIF
181: DSRNLGAPRG LEPIAIGLLI IVIASSLGLN SGCAMNPARD LSPRLFTALA GWGFEVFRAG
241: NNFWWIPVVG PLVGAVIGGL IYVLVIEIHH PEPDSVFKTE QSEDKPEKYE LSVIM