General Information

    • DRAMP ID

    • DRAMP03811

    • Peptide Name

    • Pardaxin P-3 (Pardaxin Pa3)

    • Source

    • Pardachirus pavoninus (Peacock sole) (Achirus pavoninus)

    • Family

    • Belongs to the pardaxin family

    • Gene

    • Not found

    • Sequence

    • GFFAFIPKIISSPLFKTLLSAVGSALSSSGEQE

    • Sequence Length

    • 33

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Cytotoxic

    • 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

    • Cell membrane

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

    • DRAMP03811 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP03811.

Physicochemical Information

    • Formula

    • C160H250N36O47

    • Absent Amino Acids

    • CDHMNRWY

    • Common Amino Acids

    • S

    • Mass

    • 3429.96

    • PI

    • 6.14

    • Basic Residues

    • 2

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 15

    • Net Charge

    • 0

    • Boman Index

    • 2.02

    • Hydrophobicity

    • 0.621

    • Aliphatic Index

    • 100.61

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 11

DRAMP03811

DRAMP03811 chydropathy plot

Comments Information

    • Function

    • Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.

    • Subunit structure

    • In aqueous solution exists as a tetramer.

    • Domain

    • Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder.

Literature Information

  • ·Literature 1

    • Title

    • Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus.

    • Reference

    • Science. 1986 Jul 18;233(4761):341-343.

    • Author

    • Thompson SA, Tachibana K, Nakanishi K, Kubota I.