• DRAMP ID

    • DRAMP03354
    • Peptide Name

    • Alpha-defensin-related sequence 7 (Defensin-related cryptdin 3; Rodents, mammals, animals)
    • Source

    • Mus musculus (Mouse)
    • Family

    • Belongs to the alpha-defensin family
    • Gene

    • Defa-rs7
    • Sequence

    • PRCPPCPRCSWCPRCPTCPRCNCNPK
    • Sequence Length

    • 26
    • Protein Existence

    • Transcript level
    • Biological Activity

    • Antimicrobial
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • 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

    • DRAMP03354 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03354.
    • Formula

    • C120H192N42O31S8
    • Absent Amino Acids

    • ADEFGHILMQVY
    • Common Amino Acids

    • CP
    • Mass

    • 2975.59
    • PI

    • 9.02
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 1
    • Net Charge

    • +5
    • Boman Index

    • -71.91
    • Hydrophobicity

    • -0.927
    • Aliphatic Index

    • 0
    • Half Life

      • Mammalian:>20 hour
      • Yeast:>20 hour
      • E.coli:?
    • Extinction Coefficient Cystines

    • 6000
    • Absorbance 280nm

    • 240
    • Polar Residues

    • 12

DRAMP03354

DRAMP03354 chydropathy plot
    • Function

    • Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activit.
    • Tissue specificity

    • Paneth cells of the small bowel.
  • ·Literature 1
    • Title

    • A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells.
    • Reference

    • Genomics. 1994 Nov 1;24(1):99-109.
    • Author

    • Huttner K.M, Ouellette A.J.
  • ·Literature 2
    • Title

    • Increased diversity of intestinal antimicrobial peptides by covalentdimer formation.
    • Reference

    • Nat. Immunol. 2004;5:836-843.
    • Author

    • Hornef M.W, Putsep K, Karlsson J, Refai E, Andersson M.