• DRAMP ID

    • DRAMP02994
    • Peptide Name

    • Defensin-1 (Royalisin; Insects, animals)
    • Source

    • Apis mellifera (Honeybee)
    • Family

    • Belongs to the invertebrate defensin family (Type 1 subfamily)
    • Gene

    • Not found
    • Sequence

    • VTCDLLSFKGQVNDSACAANCLSLGKAGGHCEKVGCICRKTSFKDLWDKYF
    • Sequence Length

    • 51
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • Bifidobacterium adolescentis ATCC15703, Bifidobacterium longum ATCC15707, Leuconostoc cremoris ATCC 19254, Lactobacillus spps, Staphylococcus aureus, Streptococcus spps
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • 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

    • DRAMP02994 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02994.
    • Formula

    • C240H378N66O72S6
    • Absent Amino Acids

    • MP
    • Common Amino Acids

    • CKGL
    • Mass

    • 5532.4
    • PI

    • 8.3
    • Basic Residues

    • 8
    • Acidic Residues

    • 5
    • Hydrophobic Residues

    • 17
    • Net Charge

    • +3
    • Boman Index

    • -59.74
    • Hydrophobicity

    • -0.024
    • Aliphatic Index

    • 70.78
    • Half Life

      • Mammalian:100 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 7365
    • Absorbance 280nm

    • 147.3
    • Polar Residues

    • 20

DRAMP02994

DRAMP02994 chydropathy plot
    • Function

    • Found in royal jelly and in hemolymph, potent antibacterial protein against Gram-positive bacteria at low concentration.
    • Tissue specificity

    • High expression in head, hypopharyngeal gland, and mandibular gland. Low expression in thorax and thoracic salivary gland.
    • PTM

    • Contains three disulfide bonds 3-31; 17-36; 21-38 and Phenylalanine amide at F51.
  • ·Literature 1
    • Title

    • A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin.
    • Reference

    • J Biol Chem. 1990 Jul 5;265(19):11333-11337.
    • Author

    • Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kawashima T, Kobayashi K.
  • ·Literature 2
    • Title

    • Two structurally different defensin genes, one of them encoding a novel defensin isoform, are expressed in honeybee Apis mellifera.
    • Reference

    • Insect Biochem Mol Biol. 2005 Jan;35(1):11-22.
    • Author

    • Klaudiny J, Albert S, Bachanová K, Kopernický J, Simúth J.