• DRAMP ID

    • DRAMP01079
    • Peptide Name

    • Non-specific lipid-transfer protein (Plants)
    • Source

    • Secale cereale (Rye)
    • Family

    • Belongs to the plant LTP family
    • Gene

    • Not found
    • Sequence

    • AITCGQVSSALSPCIPYARGNGANPSAACCSGVRRIAGAVQSTADKKTACNCIKRAAGGLNAGKAADIPSKCSVSIPYAINPSVDCSTIR
    • Sequence Length

    • 90
    • Protein Existence

    • Homology
    • Biological Activity

    • Antimicrobial
    • 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

    • Lipid-binding
    • 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

    • DRAMP01079 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01079.
    • Formula

    • C372H625N117O121S8
    • Absent Amino Acids

    • EFHMW
    • Common Amino Acids

    • A
    • Mass

    • 8929.25
    • PI

    • 9.22
    • Basic Residues

    • 10
    • Acidic Residues

    • 3
    • Hydrophobic Residues

    • 31
    • Net Charge

    • +7
    • Boman Index

    • -104.63
    • Hydrophobicity

    • 0.104
    • Aliphatic Index

    • 77.22
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 3480
    • Absorbance 280nm

    • 39.1
    • Polar Residues

    • 38

DRAMP01079

DRAMP01079 chydropathy plot
    • 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 (By similarity).
  • ·Literature 1
    • Title

    • Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions.
    • Reference

    • Nat Biotechnol. 2006 Jul;24(7):852-855.
    • Author

    • Doxey AC, Yaish MW, Griffith M, McConkey BJ.