| Literature DB >> 2845974 |
K Mizuno1, T Nakamura, T Ohshima, S Tanaka, H Matsuo.
Abstract
Yeast Saccharomyces cerevisiae KEX2 gene previously isolated, was characterized as the gene encoding a calcium-dependent endopeptidase required for processing of precursors of alpha-factor and killer toxin. In this study, we report the amino acid sequence of the KEX2 gene product deduced from nucleotide sequencing. Our results indicate that the KEX2 gene contains a 2,442-bp open reading frame encoding a polypeptide of 814 amino acids. The deduced amino acid sequence contains a region extensively homologous to the members of subtilisin-like serine protease family near the N-terminus. A putative membrane-spanning domain near the C-terminus was also detected. These facts indicate that the KEX2-encoded protein may function as a membrane-bound, subtilisin-like serine protease.Entities:
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Year: 1988 PMID: 2845974 DOI: 10.1016/s0006-291x(88)80832-5
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575