• DRAMP ID

    • DRAMP00910
    • Peptide Name

    • Tricyclon-A (Cyclotides; Plant defensin)
    • Source

    • Viola arvensis (European field pansy) (Field violet)
    • Family

    • Belongs to the cyclotide family
    • Gene

    • Not found
    • Sequence

    • GGTIFDCGESCFLGTCYTKGCSCGEWKLCYGTN
    • Sequence Length

    • 33
    • Protein Existence

    • Protein level
    • Biological Activity

    • Not found
    • Target Organism

    • Cytolysis
    • Hemolytic Activity

      • [Ref:15893660] It has 2% hemolytic activity at 500 μM against human red blood cells
    • Cytotoxicity

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

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • No specific N-terminal
    • C-terminal Modification

    • No specific C-terminal
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds between Cys7 and Cys21, Cys11 and Cys23, Cys16 and Cys29.
    • Stereochemistry

    • L
    • Structure

    • Beta strand (3 strands; 13 residues)
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00910 helical wheel diagram
    • PDB ID

    • 1YP8 resolved by NMR.
    • Predicted Structure

    • There is no predicted structure for DRAMP00910.
    • Formula

    • C149H219N37O49S6
    • Absent Amino Acids

    • AHMPQRV
    • Common Amino Acids

    • G
    • Mass

    • 3504.96
    • PI

    • 4.68
    • Basic Residues

    • 2
    • Acidic Residues

    • 3
    • Hydrophobic Residues

    • 6
    • Net Charge

    • -1
    • Boman Index

    • -20.13
    • Hydrophobicity

    • 0.006
    • Aliphatic Index

    • 35.45
    • Half Life

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

    • 8855
    • Absorbance 280nm

    • 276.72
    • Polar Residues

    • 22

DRAMP00910

DRAMP00910 chydropathy plot
    • Function

    • Probably participates in a plant defense mechanism. Has a weak hemolytic activity.
    • PTM

    • Contains three disulfide bonds 7-21; 11-23; 16-29. Proteolytically processed in two steps to yield first two linear precursors, and then two cyclic peptides after removal of the N-terminal repeats (NTR) and short tails.
  • ·Literature 1
    • Title

    • Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.
    • Reference

    • Structure. 2005 May;13(5):691-701.
    • Author

    • Mulvenna JP, Sando L, Craik DJ.