General Information

    • DRAMP ID

    • DRAMP03572

    • Peptide Name

    • Antibacterial protein FALL-39 (one chain of hCAP-18; Human, mammals, animals)

    • Source

    • Homo sapiens (Human)

    • Family

    • Belongs to the cathelicidin family

    • Gene

    • CAMP

    • Sequence

    • FALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES

    • Sequence Length

    • 39

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • 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

    • Lipopolysaccharide (LPS)-binding

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

    • Alpha helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03572 helical wheel diagram
  • 2K6O-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03572.

Physicochemical Information

    • Formula

    • C217H354N62O55

    • Absent Amino Acids

    • CHMWY

    • Common Amino Acids

    • K

    • Mass

    • 4711.58

    • PI

    • 10.61

    • Basic Residues

    • 11

    • Acidic Residues

    • 5

    • Hydrophobic Residues

    • 15

    • Net Charge

    • +6

    • Boman Index

    • -106.21

    • Hydrophobicity

    • -0.569

    • Aliphatic Index

    • 87.44

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 6

DRAMP03572

DRAMP03572 chydropathy plot

Comments Information

    • Function

    • Has antibacterial activity.

    • Tissue specificity

    • Expressed in bone marrow and testis and neutrophils.

    • PTM

    • The N-terminus is blocked.

Literature Information

  • ·Literature 1

    • Title

    • FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

    • Reference

    • Proc Natl Acad Sci U S A. 1995 Jan 3;92(1):195-199.

    • Author

    • Agerberth B, Gunne H, Odeberg J, Kogner P, Boman HG, Gudmundsson GH.
  • ·Literature 2

    • Title

    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes.

    • Reference

    • Eur J Biochem. 1996 Jun 1;238(2):325-332.

    • Author

    • Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R.