Rat prominin, like its mouse and human orthologues, is a pentaspan membrane glycoprotein

Biochem Biophys Res Commun. 2001 Jul 27;285(4):939-44. doi: 10.1006/bbrc.2001.5271.


Mouse prominin is the first characterized member of a novel family of membrane glycoproteins. It displays a characteristic membrane topology with five transmembrane segments and two large glycosylated extracellular loops. Prominin orthologues and paralogues have been identified in human, fish, fly, and worm. Recently, a cDNA sequence encoding the rat homologue of mouse prominin has been reported [Zhu et al. (2001) Biochem. Biophys. Res. Commun. 281, 951-956]. Surprisingly, due to a single nucleotide deletion that shifts the reading frame and introduces a premature stop codon, the protein predicted from this cDNA would correspond to a C-terminally truncated form of prominin with only four transmembrane segments. Here we report evidence that is in contrast to the report of Zhu et al. (2001). We isolated a rat prominin cDNA devoid of any frameshift mutation, demonstrate that rat prominin, like the other mammalian prominins, is a full-length 120-kDa pentaspan membrane glycoprotein, and have not been able to detect any C-terminally truncated form of rat prominin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • AC133 Antigen
  • Amino Acid Sequence
  • Animals
  • Antigens, CD
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Glycoproteins
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics*
  • Mice
  • Molecular Sequence Data
  • Peptides
  • Polymerase Chain Reaction
  • Rats
  • Reading Frames
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Species Specificity


  • AC133 Antigen
  • Antigens, CD
  • DNA, Complementary
  • Glycoproteins
  • Membrane Glycoproteins
  • Peptides
  • Prom1 protein, rat

Associated data

  • GENBANK/AF386758