title: Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.).
abstract: 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.
mesh_terms: 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
chemical_list: D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D011498:Protein Precursors; D055314:Seed Storage Proteins; D004247:DNA; C015575:vicilin protein, plant; D004262:DNA Restriction Enzymes