General Information
-
DRAMP ID
- DRAMP03220
-
Peptide Name
- M-oxotoxin-Ot2c (Oxyopinin-2c, Oxki2c; spiders, Arthropods, animals)
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Source
- Oxyopes takobius (Lynx spider) (Oxyopes foliiformis)
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Family
- Belongs to the oxyopinin-2 family
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Gene
- Not found
-
Sequence
- GKLSGISKVLRAIAKFFKGVGKARKQFKEASDLDKNQ
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Sequence Length
- 37
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UniProt Entry
- P83250
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Insecticidal
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Target Organism
- No MICs found in DRAMP database
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Hemolytic Activity
-
- [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells
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Cytotoxicity
-
- Not included yet
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Binding Target
- Cell membrane
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
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Stereochemistry
- Not included yet
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Structure
- Alpha helix
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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 DRAMP03220.
Physicochemical Information
-
Formula
- C183H308N54O50
Absent Amino Acids
- CHMPTWY
Common Amino Acids
- K
Mass
- 4064.79
PI
- 10.46
Basic Residues
- 10
Acidic Residues
- 3
Hydrophobic Residues
- 14
Net Charge
- +7
-
Boman Index
- -73.79
Hydrophobicity
- -0.562
Aliphatic Index
- 79.19
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 8
DRAMP03220
Comments Information
Function
- Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides.
Literature Information
- ·Literature 1
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Title
- Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins.
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Pubmed ID
- 11976325
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Reference
- J Biol Chem. 2002 Jun 28;277(26):23627-23637.
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Author
- Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T.