Primary structure of human pepsinogen C gene

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

Research output: Contribution to journalArticlepeer-review

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
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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