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1.A.8.9.6
Glycerol/water/urea/arsenic trioxide-transporting channel protein, aqaporin 7 or Aqp7, but water is a poor substrate (Palmgren et al. 2017).  Present in adipose tissue where it allows glycerol efflux.  Defects result in increased accumulation of triglycerides, obesity and adult onset (type 2) diabetes (Lebeck 2014). It may be a drug target for anti-type 2 diabetes (Méndez-Giménez et al. 2018). 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 may also influence whole body energy metabolism (Iena and Lebeck 2018) including in the kidney (Schlosser et al. 2023). Aquaporin-7-mediated glycerol permeability is linked to human sperm motility in asthenozoospermia and during sperm capacitation (Ribeiro et al. 2023).  AQP7 is also involved in the regulation of lipid synthesis, gluconeogenesis, and energy homeostasis, and it is intimately linked to a variety of diseases, such as obesity, type 2 diabetes mellitus, cardiovascular diseases, cancer, and inflammatory bowel disease (Liu et al. 2024).

Accession Number:O14520
Protein Name:Aquaporin-7
Length:342
Molecular Weight:37232.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate water, urea, glycerol, diarsenic trioxide

Cross database links:

Structure:
6KXW   6N1G   6QZI   6QZJ     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MVQASGHRRS TRGSKMVSWS VIAKIQEILQ RKMVREFLAE FMSTYVMMVF GLGSVAHMVL 
61:	NKKYGSYLGV NLGFGFGVTM GVHVAGRISG AHMNAAVTFA NCALGRVPWR KFPVYVLGQF 
121:	LGSFLAAATI YSLFYTAILH FSGGQLMVTG PVATAGIFAT YLPDHMTLWR GFLNEAWLTG 
181:	MLQLCLFAIT DQENNPALPG TEALVIGILV VIIGVSLGMN TGYAINPSRD LPPRIFTFIA 
241:	GWGKQVFSNG ENWWWVPVVA PLLGAYLGGI IYLVFIGSTI PREPLKLEDS VAYEDHGITV 
301:	LPKMGSHEPT ISPLTPVSVS PANRSSVHPA PPLHESMALE HF