• DRAMP ID

    • DRAMP02969
    • Peptide Name

    • Prophenin-2 (C12, PF-2, PR-2; Pro-rich; pigs, mammals, animals)
    • Source

    • Sus scrofa (Pig)
    • Family

    • Belongs to the cathelicidin family
    • Gene

    • Not found
    • Sequence

    • AFPPPNVPGPRFPPPNVPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPPFPPPIFPGPWFPPPPPFRPPPFGPPRFP
    • Sequence Length

    • 79
    • Protein Existence

    • Transcript level
    • Biological Activity

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

      • Gram-positive bacterium: Listeria monocytogenes;
      • 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

    • DRAMP02969 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02969.
    • Formula

    • C436H589N103O85
    • Absent Amino Acids

    • CDEHKLMQSTY
    • Common Amino Acids

    • P
    • Mass

    • 8633.11
    • PI

    • 12.7
    • Basic Residues

    • 6
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 19
    • Net Charge

    • +6
    • Boman Index

    • -57.28
    • Hydrophobicity

    • -0.779
    • Aliphatic Index

    • 13.54
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 70.51
    • Polar Residues

    • 12

DRAMP02969

DRAMP02969 chydropathy plot
    • Function

    • Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria.
  • ·Literature 1
    • Title

    • Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow.
    • Reference

    • FEBS Lett. 1993 Dec 27;336(2):284-288.
    • Author

    • Pungercar J, Strukelj B, Kopitar G, Renko M, Lenarcic B, Gubensek F, Turk V.
  • ·Literature 2
    • Title

    • Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39.
    • Reference

    • FEBS Lett. 1995 Dec 4;376(3):130-134.
    • Author

    • Zhao C, Ganz T, Lehrer RI.