Molecular cloning of the murine cMOAT ATPase

Biochim Biophys Acta. 2000 Jul 24;1492(2-3):531-6. doi: 10.1016/s0167-4781(00)00132-9.

Abstract

cMOAT encodes an ATPase within the family of cMOAT/MRP ATPases that functions as an ATP dependent, multispecific anion transporter within the canalicular surface of hepatocytes that has pharmacologic significance. We describe here the cloning of a murine cMOAT cDNA isolated from mouse liver. The open reading frame of this cDNA incorporates 4627 nucleotides encoding 1309 amino acids with 77.5% and 86.7% identity with the human and rat encoded amino acids, respectively. Northern blotting showed that the expression of cMOAT mRNA occurs primarily in mouse liver in the form of two variants with approximately 5.6 and 7.8 kb of sequence each. cMOAT mRNA was also detected in mouse kidney at a low level but was not detected in other mouse organs or tumors except the Hep 1-6 murine hepatoma where expression was also in the form of the same two mRNA variants.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 5' Untranslated Regions
  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Animals
  • Anion Transport Proteins
  • Base Sequence
  • Blotting, Northern
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Cloning, Molecular
  • DNA, Complementary / analysis
  • Mice
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Tissue Distribution

Substances

  • 5' Untranslated Regions
  • Anion Transport Proteins
  • Carrier Proteins
  • DNA, Complementary
  • Adenosine Triphosphatases

Associated data

  • GENBANK/AF227274