Primary structure of human pepsinogen C gene

T. Hayano, K. Sogawa, Y. Ichihara, Y. Fujii-Kuriyama, K. Takahashi

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    66 Citations (Scopus)

    Abstract

    The entire human pepsinogen C gene has been isolated from a cosmid genomic library. The nucleotide sequences of all the exons and the 5'- and 3'-flanking regions of the gene are presented. The organization of the gene is fundamentally compatible with those of other aspartic proteinases, allowing us to conclude that the genes of these aspartic proteinases including pepsinogen C are derived from a common ancestral gene. The predicted 388-residue amino acid sequence of human pepsinogen C consists of a signal sequence of 16-amino acid residues, an activation peptide of 43 residues, and the mature pepsin of 329 residues containing the two active-site aspartic acids. In the light of present notions about eukaryotic gene expression, possible regulatory roles of the oligonucleotide DNA sequences in the promoter region of the gene are discussed.

    Original languageEnglish
    Pages (from-to)1382-1385
    Number of pages4
    JournalJournal of Biological Chemistry
    Volume263
    Issue number3
    Publication statusPublished - 1988 Jan 1

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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