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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). 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).

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 glycerol, water, Urea

Cross database links:

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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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