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

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

Y Nishimura  1 , M Hayashi, H Inada, T Tanaka
Affiliations

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

Y Nishimura et al. Biochem Biophys Res Commun. .

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.

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