General Information

    • DRAMP ID

    • DRAMP00369

    • Peptide Name

    • IWF1 (Bv-LTP1; Plant defensin)

    • Source

    • Beta vulgaris (Sugar beet)

    • Family

    • Belongs to the plant LTP family

    • Gene

    • IWF1'

    • Sequence

    • ITCGLVASKLAPCIGYLQGAPGPSAACCGGIKSLNSAAASPADRKTACTCLKSAATSIKGINYGKAASLPRQCGVSVPYAISPNTNCNAIH

    • Sequence Length

    • 91

    • Protein Existence

    • Homology

Activity Information

    • Biological Activity

    • Antimicrobial, Antifungal

    • Target Organism

      • Fungi: Cercospora beticola.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Lipid-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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP00369 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP00369.

Physicochemical Information

    • Formula

    • C383H634N112O119S8

    • Absent Amino Acids

    • EFMW

    • Common Amino Acids

    • A

    • Mass

    • 8968.41

    • PI

    • 9.18

    • Basic Residues

    • 9

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 32

    • Net Charge

    • +8

    • Boman Index

    • -44.33

    • Hydrophobicity

    • 0.241

    • Aliphatic Index

    • 82.86

    • Half Life

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

    • Extinction Coefficient Cystines

    • 4970

    • Absorbance 280nm

    • 55.22

    • Polar Residues

    • 40

DRAMP00369

DRAMP00369 chydropathy plot

Comments Information

    • Function

    • Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Also has fungicide activity.

Literature Information

  • ·Literature 1

    • Title

    • New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins.

    • Reference

    • Plant Mol Biol. 1996 Jun;31(3):539-552.

    • Author

    • Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD.