Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.).
Amino acid sequence data from vicilin of pea (Pisum sativum L.) were compared with predicted sequences from complementary DNA species. The sites of potential post-translational proteolytic cleavage of vicilin precursor polypeptides were located in polar regions of the polypeptide, at acidic or amide residues. Proteolysis did not take place in precursors containing a functionally distinct sequence: neutral residue-hydrophobic residue-basic residue at the cleavage site. Differences between the genomic sequences encoding vicilin thus specify proteolytic cleavage of vicilin precursor polypeptides.
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics; D004262:DNA Restriction Enzymes; D004587:Electrophoresis, Agar Gel; D007887:Fabaceae; D009693:Nucleic Acid Hybridization; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000235:genetics / Q000378:metabolism*; D010946:Plants, Medicinal; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D055314:Seed Storage Proteins
D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D011498:Protein Precursors; D055314:Seed Storage Proteins; D004247:DNA; C015575:vicilin protein, plant; D004262:DNA Restriction Enzymes