A novel variant of mouse MATE-1 H+/organic cation antiporter with a long hydrophobic tail

Arch Biochem Biophys. 2008 Jan 15;469(2):195-9. doi: 10.1016/j.abb.2007.10.010. Epub 2007 Oct 25.


Mammalian multidrug and toxic compound extrusion 1 (MATE1) are polyspecific H+-coupled exporters of organic cations (OCs) and responsible for excretion of metabolic waste products and xenobiotics. Here, we report a novel variant of mouse MATE1, mMATE1b, that has a long carboxyl terminal hydrophobic tail homologous to other MATE1 transporter proteins. Mouse MATE1b mediates tetraethylammonium (TEA) uptake with properties similar to that of mMATE1 and is localized in renal brush border membranes. Thus, mMATE1b is a functional variant of mMATE1 and seems to be the true counterpart to other MATE1 transporters.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cations
  • Cell Line
  • Frameshift Mutation
  • Humans
  • Mice
  • Microvilli / metabolism
  • Models, Genetic
  • Molecular Sequence Data
  • Organic Cation Transport Proteins / chemistry*
  • Organic Cation Transport Proteins / genetics*
  • Organic Cation Transport Proteins / physiology
  • Protein Structure, Tertiary
  • Tetraethylammonium / pharmacokinetics
  • Xenobiotics / chemistry


  • Cations
  • MATE1 protein, mouse
  • Organic Cation Transport Proteins
  • Xenobiotics
  • Tetraethylammonium