Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins

Biochem Biophys Res Commun. 1999 Jan 8;254(1):21-6. doi: 10.1006/bbrc.1998.9876.

Abstract

We have identified human and rat homologues of the VAMP-associated protein (VAP) of 33 kDa of Aplysia californica (aVAP-33), which we designated VAP-A, VAP-B, and VAP-C. Human VAP-A (hVAP-A) was found to be identical to the recently reported protein hVAP-33, with the exception of two amino acid residues. VAP-B contained a coiled-coil domain and a transmembrane domain (TMD). Human VAP-B (hVAP-B) was 46 and 60% homologous of the amino acid level to aVAP-33 and hVAP-A, respectively. Human VAP-C was a splicing variant of hVAP-B, lacking both the coiled-coil domain and the TMD. hVAP-B had VAMP-binding ability. Moreover, hVAP-A and hVAP-B associated with each other through their respective TMDs. These results suggest that complex formation by VAPs might be important in the trafficking of mammalian vesicle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aplysia
  • Base Sequence
  • Carrier Proteins / genetics*
  • Cloning, Molecular
  • DNA, Complementary / analysis
  • DNA, Complementary / genetics
  • Humans
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Rats
  • Sequence Alignment
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • DNA, Complementary
  • Membrane Proteins
  • VAPA protein, human
  • VAPB protein, human
  • Vapa protein, rat
  • Vesicular Transport Proteins

Associated data

  • GENBANK/AF086627
  • GENBANK/AF086628
  • GENBANK/AF086629
  • GENBANK/AF086630
  • GENBANK/AF086631