General Information

    • DRAMP ID

    • DRAMP02374

    • Peptide Name

    • Bass hepcidin (fish, chordates, animals)

    • Source

    • Morone chrysops x Morone saxatilis (white bass x striped sea-bass)

    • Family

    • Belongs to the hepcidin family

    • Gene

    • hamp

    • Sequence

    • GCRFCCNCCPNMSGCGVCCRF

    • Sequence Length

    • 21

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-, Antifungal

    • Target Organism

      • Gram-negative bacteria: Escherichia coli ATCC 25,922,351,50 (MIC=22 µM), Escherichia coli ATCC D31K (MIC=11 µM), Klebsiella pneumoniae ATCC 10,031 (MIC=22 µM), P. shigelloides ATCC KST (MIC=11 µM), S. flexneri ATCC 12,022 (MIC=22 µM), Shigella sonnei ATCC 9290 (MIC=44 µM), Y. enterocolitica ATCC 23,715 (MIC=22 µM).
      • Fungi: Aspergillus niger (MIC=44 µM).

    • Hemolytic Activity

      • [Ref.15546886] It displays essentially no hemolytic activity toward HSB erythrocytes

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds between Cys2 and Cys19; Cys5 and Cys8; Cys6 and Cys15,Cys9 and Cys18.

    • Stereochemistry

    • L

    • Structure

    • Beta strand (2 strands; 6 residues)

    • Structure Description

    • Solution structure by NMR indicates that bass hepcidin is very similar to that of human hepcidin, including the presence of an antiparallel beta-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond.

    • Helical Wheel Diagram

    • DRAMP02374 helical wheel diagram

    • PDB ID

    • 1S6W resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP02374.

Physicochemical Information

    • Formula

    • C86H135N29O25S9

    • Absent Amino Acids

    • ADEHIKLQTWY

    • Common Amino Acids

    • C

    • Mass

    • 2263.74

    • PI

    • 8.23

    • Basic Residues

    • 2

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 3

    • Net Charge

    • +2

    • Boman Index

    • -21.11

    • Hydrophobicity

    • 0.576

    • Aliphatic Index

    • 13.81

    • Half Life

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

    • Extinction Coefficient Cystines

    • 500

    • Absorbance 280nm

    • 25

    • Polar Residues

    • 14

DRAMP02374

DRAMP02374 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 (By similarity). Synthetic bass hepcidin is active in vitro against Gram-negative pathogens and fungi but showes no activity against key Gram-positive pathogens and a single yeast strain tested.

    • Tissue specificity

    • Predominantly expressed in liver.

    • Induction

    • By bacterial challenge.

    • PTM

    • Contains four disulfide bonds 2-19; 5-8; 6-15; 9-18.

Literature Information

  • ·Literature 1

    • Title

    • Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge.

    • Reference

    • Eur J Biochem. 2002 Apr;269(8):2232-2237.

    • Author

    • Shike H, Lauth X, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Shimizu C, Bulet P, Burns JC.
  • ·Literature 2

    • Title

    • Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections.

    • Reference

    • J Biol Chem. 2005 Mar 11;280(10):9272-9282.

    • Author

    • Lauth X, Babon JJ, Stannard JA, Singh S, Nizet V, Carlberg JM, Ostland VE, Pennington MW, Norton RS, Westerman ME.