General Information
-
DRAMP ID
- DRAMP03104
-
Peptide Name
- Sapecin (defensins; Insects, animals)
-
Source
- Sarcophaga peregrina (Flesh fly)
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Family
- Belongs to the invertebrate defensin family (Type 1 subfamily)
-
Gene
- Not found
-
Sequence
- ATCDLLSGTGINHSACAAHCLLRGNRGGYCNGKAVCVCRN
-
Sequence Length
- 40
-
UniProt Entry
- P18313
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- Gram-positive bacteria: Staphylococcus aureus FDA209P (MIC=5.0 µg/ml), Staphylococcus smith (MIC=5.0 µg/ml), Micrococcus luteus FDA16 (MIC=1.2 µg/ml), Micrococcus luteus IF03333 (MIC=1.2 µg/ml), Micrococcus luteus PC11001 (MIC=10.0 µg/ml), Bacillus subtilis NRRI B-558 (MIC=39.0 µg/ml), Bacillus subtilis PC1219 (MIC=20.0 µg/ml), Mycobacterium smegmatis ATCC607 (MIC=78.0 µg/ml), Corynebacterium bouis 1810 (MIC=2.5 µg/ml), Corynebacterium michiganense (MIC=2.5 µg/ml).
- Gram-negative bacteria: Xantbmonas oryzae (MIC=20.0 µg/ml), Pseudomonas lachrymans (MIC=78.0 µg/ml), Escherichia coli NIHJ (MIC>78.0 µg/ml), Shigella sonnei JS11746 (MIC>78.0 µg/ml), Proteus vulgaris O X19 (MIC>78.0 µg/ml)
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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
- Cyclic
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- Disulfide bonds between Cys3 and Cys30; Cys16 and Cys36; Cys20 and Cys38.
-
Stereochemistry
- L
-
Structure
- Combine helix and strand structure
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- 1L4V resolved by NMR.
- 1L4V-> 
-
Predicted Structure
- There is no predicted structure for DRAMP03104.
Physicochemical Information
-
Formula
- C164H272N58O52S6
Absent Amino Acids
- EFMPQW
Common Amino Acids
- CG
Mass
- 4080.68
PI
- 8.69
Basic Residues
- 6
Acidic Residues
- 1
Hydrophobic Residues
- 12
Net Charge
- +5
-
Boman Index
- -51.94
Hydrophobicity
- 0.103
Aliphatic Index
- 75.75
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 1865
Absorbance 280nm
- 47.82
Polar Residues
- 21
DRAMP03104
Comments Information
Function
- Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin is cytotoxic to Gram-positive bacteria, and to a lesser extent against Gram-negative bacteria.
Tissue specificity
- Hemocytes and fat body. Induction
PTM
- Contains three disulfide bonds 3-30; 16-36; 20-38.
Literature Information
- ·Literature 1
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Title
- Molecular cloning of cDNA for sapecin and unique expression of the sapecin gene during the development of Sarcophaga peregrina.
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Pubmed ID
- 3182836
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Reference
- J Biol Chem. 1988 Nov 15;263(32):17117-17121.
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Author
- Matsuyama K, Natori S.
- ·Literature 2
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Title
- Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina.
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Pubmed ID
- 3182836
-
Reference
- J Biol Chem. 1988 Nov 15;263(32):17112-17116.
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Author
- Matsuyama K, Natori S.
- ·Literature 3
-
Title
- Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).
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Pubmed ID
- 2358424
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Reference
- J Biochem. 1990 Apr;107(4):514-518.
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Author
- Kuzuhara T, Nakajima Y, Matsuyama K, Natori S.