General Information

    • DRAMP ID

    • DRAMP03564

    • Peptide Name

    • Human hepcidin-20 (Hepc20; one chain of Hepcidin; Human, mammals, animals)

    • Source

    • Homo sapiens (Human)

    • Family

    • Not found

    • Gene

    • HAMP

    • Sequence

    • ICIFCCGCCHRSKCGMCCKT

    • Sequence Length

    • 20

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacterium: Escherichia coli;
      • Gram-positive bacteria: Staphylococcus aureus, S. epidermidis, group B Streptococcus.
      • Fungi: Candida albicans, Aspergillus fumigatus, Aspergillus niger.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

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

    • Beta strand

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03564 helical wheel diagram

    • PDB ID

    • 1M4E resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03564.

Physicochemical Information

    • Formula

    • C85H143N27O23S9

    • Absent Amino Acids

    • ADELNPQVWY

    • Common Amino Acids

    • C

    • Mass

    • 2199.78

    • PI

    • 8.53

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 3

    • Net Charge

    • +4

    • Boman Index

    • -9.36

    • Hydrophobicity

    • 0.795

    • Aliphatic Index

    • 39

    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 500

    • Absorbance 280nm

    • 26.32

    • Polar Residues

    • 12

DRAMP03564

DRAMP03564 chydropathy plot

Comments Information

    • Function

    • Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa.

    • Tissue specificity

    • Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine.

    • PTM

    • Contains four disulfide bonds 2-18; 5-17; 6-14; 8-9.

Literature Information

  • ·Literature 1

    • Title

    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver.

    • Reference

    • J Biol Chem. 2001 Mar 16;276(11):7806-7810.

    • Author

    • Park CH, Valore EV, Waring AJ, Ganz T.
  • ·Literature 2

    • Title

    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.

    • Reference

    • J Biol Chem. 2002 Oct 4;277(40):37597-37603.

    • Author

    • Hunter HN, Fulton DB, Ganz T, Vogel HJ.
  • ·Literature 3

    • Title

    • LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. ref2) Hepcidin, a rinary antimicrobial peptide synthesized in the liver.

    • Reference

    • FEBS Lett. 2000 Sep 1;480(2-3):147-150.

    • Author

    • Krause A et al Adermann K.