General Information
-
DRAMP ID
- DRAMP03073
-
Peptide Name
- Sapecin-C (Sapecin C; defensins; Insects, animals)
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Source
- Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina)
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Family
- Belongs to the invertebrate defensin family (Type 1 subfamily)
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Gene
- Not found
-
Sequence
- ATCDLLSGIGVQHSACALHCVFRGNRGGYCTGKGICVCRN
-
Sequence Length
- 40
-
UniProt Entry
- P31530
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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-negative bacteria: Escherichia coli, Proteus mirabilis, Klebsiella Pneumoniae;
- Gram-positive bacteria: Staphylococcus spps., Streptococcus spps, Bacillus megaterium, Bacillus circulans, Corynebacterium glutamicum.
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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
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
-
Nonterminal Modifications and Unusual Amino Acids
- Not included yet
-
Stereochemistry
- Not included yet
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Structure
- Bridge
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP03073.
Physicochemical Information
-
Formula
- C171H279N57O51S6
Absent Amino Acids
- EMPW
Common Amino Acids
- G
Mass
- 4141.81
PI
- 8.69
Basic Residues
- 6
Acidic Residues
- 1
Hydrophobic Residues
- 12
Net Charge
- +5
-
Boman Index
- -39.86
Hydrophobicity
- 0.283
Aliphatic Index
- 78
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 1865
Absorbance 280nm
- 47.82
Polar Residues
- 20
DRAMP03073

Comments Information
Function
- Sapecins, which are potent bactericidal proteins, are produced in response to body injury. Thus, sapecin is probably a defense protein synthesized by Sarcophaga to prevent bacterial infection through the damaged body wall. This gene was also found to be activated in the embryonic and early pupal stages, suggesting that sapecin also plays a role in the ontogenetic processes of Sarcophaga.
Literature Information
- ·Literature 1
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Title
- Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.
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Pubmed ID
- 8471044
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Reference
- Biochem J. 1993 Apr 1;291 (Pt 1):275-279.
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Author
- Yamada K, Natori S.