General Information
-
DRAMP ID
- DRAMP01576
-
Peptide Name
- Caerin-4.3 (Frogs, amphibians, animals)
-
Source
- Litoria caerulea (Green tree frog)
-
Family
- Belongs to the frog skin active peptide family (Caerin subfamily)
-
Gene
- Not found
-
Sequence
- GLWQKIKNAAGDLASGIVEGIKS
-
Sequence Length
- 23
-
UniProt Entry
- P56244
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
-
Target Organism
-
- Gram-positive bacterium: Micrococcus luteus (MIC=25 µg/ml);
- Gram-negative bacterium: Escherichia coli (MIC=50 µg/ml).(Ref.2)
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
-
Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Amidation
-
Nonterminal Modifications and Unusual Amino Acids
- Free
-
Stereochemistry
- L
-
Structure
- Not found
-
Structure Description
- Not found
-
Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- Please click DRAMP01576_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C105H175N29O32
Absent Amino Acids
- CFHMPRTY
Common Amino Acids
- G
Mass
- 2355.72
PI
- 8.5
Basic Residues
- 3
Acidic Residues
- 2
Hydrophobic Residues
- 10
Net Charge
- +1
-
Boman Index
- -11
Hydrophobicity
- 0.039
Aliphatic Index
- 110.43
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 250
Polar Residues
- 7
DRAMP01576
Comments Information
Function
- Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
Tissue specificity
- Expressed by the skin parotoid and/or rostral glands.
PTM
- C-terminal amidation.
Literature Information
- ·Literature 1
-
Title
- Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.
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Pubmed ID
- 15203252
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Reference
- Peptides. 2004 Jun;25(6):1035-1054.
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Author
- Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.
- ·Literature 2
-
Title
- Peptides from Australian frogs. The structures of the caerins from Litoria caerula.
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Pubmed ID
- PubMed ID is not available
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Reference
- J. Chem. Res. 1993; 138: 910-936.
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Author
- Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.