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

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.
Mesh Terms:
Amino Acid Sequence, Animals, Aplysia, Base Sequence, Carrier Proteins, Cloning, Molecular, DNA, Complementary, Humans, Membrane Proteins, Molecular Sequence Data, Rats, Sequence Alignment, Sequence Analysis, Sequence Homology, Amino Acid, Vesicular Transport Proteins
Biochem. Biophys. Res. Commun.
Date: Jan. 08, 1999
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