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1.C.17.1.1
Cecropin A, B and C precursor.  Cecropin A and B form pores, but cecropin P1 doesn't.  Insertion and activity are dependent on the lipids present.  Can be cation- or anion-selective, or non-selective.  The negative pole of the dipole is probably inserted into the membrane first (Efimova et al. 2014).

Accession Number:P01507
Protein Name:CECA
Length:64
Molecular Weight:6952.00
Species:Hyalophora cecropia (Cecropia moth) [7123]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules, electrolytes, water

Cross database links:

Pfam: PF00272   

Gene Ontology

GO:0005576 C:extracellular region
GO:0042742 P:defense response to bacterium
GO:0045087 P:innate immune response

References (4)

[1] “The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia.”  Gudmundsson G.H.et.al.   1711035
[2] “Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae.”  Hultmark D.et.al.   7140755
[3] “Sequence and specificity of two antibacterial proteins involved in insect immunity.”  Steiner H.et.al.   7019715
[4] “The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study.”  Holak T.A.et.al.   3207693
Structure:
1D9J   1D9L   1D9M   1D9O   1D9P   1F0D   1F0E   1F0F   1F0G   1F0H   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
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FASTA formatted sequence
1:	MNFSRIFFFV FACLTALAMV NAAPEPKWKL FKKIEKVGQN IRDGIIKAGP AVAVVGQATQ 
61:	IAKG