• DRAMP ID

    • DRAMP02853
    • Peptide Name

    • Cathelicidin-3 (Bactenecin-7, Bac7; PR-59; mammals, animals)
    • Source

    • Bos taurus (Bovine)
    • Family

    • Belongs to the cathelicidin family
    • Gene

    • CATHL3
    • Sequence

    • RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRP
    • Sequence Length

    • 59
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-
    • Target Organism

      • Gram-negative bacterium: Escherichia coli.
    • 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

    • DRAMP02853 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP02853.
    • Formula

    • C323H526N110O60
    • Absent Amino Acids

    • ACDEHKMNQSTVWY
    • Common Amino Acids

    • P
    • Mass

    • 6910.43
    • PI

    • 13.2
    • Basic Residues

    • 17
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 11
    • Net Charge

    • +17
    • Boman Index

    • -202.52
    • Hydrophobicity

    • -1.371
    • Aliphatic Index

    • 52.88
    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 3

DRAMP02853

DRAMP02853 chydropathy plot
    • Function

    • Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms.
    • Tissue specificity

    • Large granules of neutrophils.
    • PTM

    • Contains two disulfide bonds.
  • ·Literature 1
    • Title

    • Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils.
    • Reference

    • J Biol Chem. 1990 Nov 5;265(31):18871-18874.
    • Author

    • Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D.