General Information
-
DRAMP ID
- DRAMP02433
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Peptide Name
- Antimicrobial peptide microplusin (Microplusin; Ticks, Arthropods, animals)
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Source
- Boophilus microplus (Cattle tick)
-
Family
- Not found
-
Gene
- Not found
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Sequence
- HHQELCTKGDDALVTELECIRLRISPETNAAFDNAVQQLNCLNRACAYRKMCATNNLEQAMSVYFTNEQIKEIHDAATACDPEAHHEHDH
-
Sequence Length
- 90
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UniProt Entry
- Q86LE5
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antifungal, Antibacterial
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Target Organism
- Micrococcus luteus (MIC=0.38-0.76 µM), Cryptococcus neoformans.
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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
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Binding Target
- Metal-binding: copper II and iron II
Structure Information
-
Linear/Cyclic
- Cyclic
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N-terminal Modification
- Free
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C-terminal Modification
- Free
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Nonterminal Modifications and Unusual Amino Acids
- Disulfide bonds between Cys6 and Cys52,Cys19 and Cys80,Cys41 and Cys46.
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Stereochemistry
- L
-
Structure
- Alpha helix
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Structure Description
- Microplusin consists of five alpha-helices: alpha1 (residues Gly-9 to Arg-21), alpha2 (residues Glu-27 to Asn-40), alpha3 (residues Arg-44 to Thr-54), alpha4 (residues Leu-57 to Tyr-64), and alpha5 (residues Asn-67 to Cys-80). The N and C termini are disordered.
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Helical Wheel Diagram
-
PDB ID
- 2KNJ resolved by NMR.
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Predicted Structure
- There is no predicted structure for DRAMP02433.
Physicochemical Information
-
Formula
- C429H671N131O143S8
Absent Amino Acids
- W
Common Amino Acids
- A
Mass
- 10208.32
PI
- 5.16
Basic Residues
- 14
Acidic Residues
- 15
Hydrophobic Residues
- 28
Net Charge
- -1
-
Boman Index
- -212
Hydrophobicity
- -0.616
Aliphatic Index
- 70.67
Half Life
-
- Mammalian:3.5 hour
- Yeast:10 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 3355
Absorbance 280nm
- 37.7
Polar Residues
- 24
DRAMP02433
Comments Information
Function
- Has bacteriostatic activity against the Gram-positive bacterium M.luteus. Has fungistatic activity against C.neoformans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus.
Tissue specificity
- Expressed in the hemocytes, fat body and ovaries.
PTM
- Contains three disulfide bonds 6-52; 19-80; 41-46.
Literature Information
- ·Literature 1
-
Title
- Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile.
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Pubmed ID
- 14642886
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Reference
- Dev Comp Immunol. 2004 Mar;28(3):191-200.
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Author
- Fogaça AC, Lorenzini DM, Kaku LM, Esteves E, Bulet P, Daffre S.
- ·Literature 2
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Title
- Structure and mode of action of microplusin, a copper II-chelating antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus) microplus.
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Pubmed ID
- 19828445
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Reference
- J Biol Chem. 2009 Dec 11;284(50):34735-34746.
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Author
- Silva FD, Rezende CA, Rossi DC, Esteves E, Dyszy FH, Schreier S, Gueiros-Filho F, Campos CB, Pires JR, Daffre S.