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.CI - Copyright 1999 Academic Press.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|