General Information

    • DRAMP ID

    • DRAMP03469

    • Peptide Name

    • Serine protease inhibitor Cvsi-1 (molluscs, animals)

    • Source

    • Crassostrea virginica (Eastern oyster)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • MDVVRTLILCVCLFGLTFA

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antiparasitic

    • Target Organism

    • Subtilisin A and Prochlorococcus marinus.

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03469 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP03469.

Physicochemical Information

    • Formula

    • C97H160N22O24S3

    • Absent Amino Acids

    • EHKNPQSWY

    • Common Amino Acids

    • L

    • Mass

    • 2114.65

    • PI

    • 5.58

    • Basic Residues

    • 1

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 11

    • Net Charge

    • 0

    • Boman Index

    • 21.56

    • Hydrophobicity

    • 1.937

    • Aliphatic Index

    • 153.68

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 6.94

    • Polar Residues

    • 5

DRAMP03469

DRAMP03469 chydropathy plot

Comments Information

    • Function

    • Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A, perkinsin and trypsin with dissociation constants of 0.29 nM, 13.7 nM and 17.7 nM respectively. Not active against thermolysin, papain or pepsin. Has antiparasitic activity against the protozoan P. marinus.

    • Tissue specificity

    • Detected in hemolymph (at protein level). In oysters collected in the summer the expression level is highest in the digestive gland with low levels of expression in gill, mantle, labial palp, style-sac midgut, gonad, heart, and hemocyte. In winter expression levels are higher in all tissues with highest expression levels observed in the digestive gland. Within the digestive gland expression is limited to the basophil cells of the digestive diverticula.

Literature Information

  • ·Literature 1

    • Title

    • A novel slow-tight binding serine protease inhibitor from eastern oyster (Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus.

    • Reference

    • Comp Biochem Physiol B Biochem Mol Biol. 2006 Sep;145(1):16-26.

    • Author

    • Xue QG, Waldrop GL, Schey KL, Itoh N, Ogawa M, Cooper RK, Losso JN, La Peyre JF.
  • ·Literature 2

    • Title

    • Serine protease inhibitor cvSI-1 potential role in the eastern oyster host defense against the protozoan parasite Perkinsus marinus.

    • Reference

    • Dev Comp Immunol. 2010 Jan;34(1):84-92.

    • Author

    • La Peyre JF, Xue QG, Itoh N, Li Y, Cooper RK.