PMID:3124102

Citation	MacKay, VL, Welch, SK, Insley, MY, Manney, TR, Holly, J, Saari, GC and Parker, ML (1988) The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin. Proc. Natl. Acad. Sci. U.S.A. 85:55-9
Abstract	Saccharomyces cerevisiae a cells secrete an extracellular protein, called "barrier" activity, that acts as an antagonist of alpha factor, the peptide mating pheromone produced by mating-type alpha cells. We report here the DNA sequence of BAR1, the structural gene for barrier activity. The deduced primary translation product of 587 amino acids has a putative signal peptide, nine potential asparagine-linked glycosylation sites, and marked sequence similarity of the first two-thirds of the protein with pepsin-like proteases. Barrier activity was abolished by in vitro mutation of an aspartic acid predicted from this sequence homology to be in the active site. Therefore, barrier protein is probably a protease that cleaves alpha factor. The sequence similarity suggests that the first two-thirds of the barrier protein is organized into two distinct structural domains like those of the pepsin-like proteases. However, the BAR1 gene product has a third carboxyl-terminal domain of unknown function; deletion of at least 166 of the 191 amino acids of this region has no significant effect on barrier activity.
Links	PubMed PMC279480
Keywords	Amino Acid Sequence; Animals; Aspartic Acid Endopeptidases; Base Sequence; Cloning, Molecular; Endopeptidases/genetics; Endopeptidases/metabolism; Fungal Proteins/genetics; Fungal Proteins/metabolism; Genes; Genes, Fungal; Genes, Mating Type, Fungal; Molecular Sequence Data; Mutation; Pepsin A/genetics; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae Proteins; Sequence Homology, Nucleic Acid
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Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
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