General Information

    • DRAMP ID

    • DRAMP03646

    • Peptide Name

    • Cathelicidin-3 (CATH-3; Fowlicidin-3; Birds, animals)

    • Source

    • Gallus gallus (Chicken)

    • Family

    • Not found

    • Gene

    • CATHL3

    • Sequence

    • RVKRFWPLVPVAINTVAAGINLYKAIRRK

    • Sequence Length

    • 29

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

    • Target Organism

      • Gram-negative bacteria: Escherichia coli 25922 (MIC=2 µM), Salmonella typhimurium 14028 (MIC=2 µM), S. typhimurium DT104 700408 (MIC=2 µM), Salmonella enteritidis 13076 (MIC=2 µM), Klebsiella pneumoniae 13883 (MIC=1 µM);
      • Gram-positive bacteria: Listeria monocytogenes 19115 (MIC=2 µM), Staphylococcus aureus 25923 (MIC=1 µM), S. aureus (MRSA) 43300 (MIC=1 µM), S. aureus (MRSA) BAA-39 (MIC=1 µM).

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Lipopolysaccharide (LPS)-binding

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (1 helices; 9 residues)

    • Structure Description

    • NMR spectroscopy reveales that fowlicidin-3 comprises 27 amino-acid residues and adopts a predominantly alpha-helical structure extending from residue 9 to 25 with a slight kink induced by a glycine at position 17..

    • Helical Wheel Diagram

    • DRAMP03646 helical wheel diagram

    • PDB ID

    • 2HFR resolved by NMR.
  • 2HFR-> 

    • Predicted Structure

Physicochemical Information

    • Formula

    • C157H261N47O34

    • Absent Amino Acids

    • CDEHMQS

    • Common Amino Acids

    • ARV

    • Mass

    • 3351.09

    • PI

    • 12.02

    • Basic Residues

    • 7

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 15

    • Net Charge

    • +7

    • Boman Index

    • -38.07

    • Hydrophobicity

    • 0.162

    • Aliphatic Index

    • 121.03

    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 6990

    • Absorbance 280nm

    • 249.64

    • Polar Residues

    • 5

DRAMP03646

DRAMP03646 chydropathy plot

Comments Information

    • Function

    • May have antimicrobial activity and play a role in the innate immune response.

    • Tissue specificity

    • Detected in bone marrow, liver and lung.

Literature Information

  • ·Literature 1

    • Title

    • Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway.

    • Reference

    • Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15063-15068.

    • Author

    • Goitsuka R, Chen CL, Benyon L, Asano Y, Kitamura D, Cooper MD.
  • ·Literature 2

    • Title

    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity.

    • Reference

    • J Biol Chem. 2006 Feb 3;281(5):2858-2867.

    • Author

    • Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, Gilliland SE, Zhang G.
  • ·Literature 3

    • Title

    • Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities.

    • Reference

    • FEBS J. 2007 Jan;274(2):418-428.

    • Author

    • Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G.