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13  structures 24  species 0  interactions 107  sequences 3  architectures

Family: Cecropin (PF00272)

Summary: Cecropin family

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Cecropin Edit Wikipedia article

Cecropin family
2IGR.pdb.png
2IGR ?
Identifiers
Symbol Cecropin
Pfam PF00272
InterPro IPR000875
PROSITE PDOC00241
SCOP 1f0d
SUPERFAMILY 1f0d
TCDB 1.C.17
OPM superfamily 160
OPM protein 1d9j

Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.

Cecropins[3][4][5] constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 31 - 37 amino acid residues active against both Gram-positive and Gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names; bactericidin, lepidopterin, sarcotoxin, etc. All of these peptides are structurally related.

Members

Members include :

Cecropin A
Peptide Sequence (KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK). Secondary structure includes two α helices.[6]:4.2 At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.[7]
Cecropin B
Peptide Sequence (KWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL). Secondary structure includes two α helices.[6]:4.2
CECD
from Aedes aegypti (Yellowfever mosquito).[8]
Papiliocin
(A lepidopteran) from Papilio xuthus[8] an Asian swallowtail butterfly.
Cecropin P1
Peptide Sequence (SWLSKTAKKLENSAKKRISEGIAIAIQGGPR). An antibacterial peptide from Ascaris suum, a parasitic nematode that resides in the pig intestine, also belongs to this family.

Derivatives

A derivative of Cecropin B is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.[9]

Some of the cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called anticancer peptides (ACPs).[6]:3 Hybrid ACPs based on Cecropin A have been studied for anticancer properties.[6]:7.1

References

  1. ^ Cecropins at the US National Library of Medicine Medical Subject Headings (MeSH)
  2. ^ Lauwers A, Twyffels L, Soin R, Wauquier C, Kruys V, Gueydan C (January 2009), "Post-transcriptional regulation of genes encoding anti-microbial peptides in Drosophila", J. Biol. Chem., 284 (13): 8973–83, doi:10.1074/jbc.M806778200, PMC 2659254Freely accessible, PMID 19176529. 
  3. ^ Boman HG, Hultmark D (1987), "Cell-free immunity in insects", Annu. Rev. Microbiol., 41: 103–126, doi:10.1146/annurev.mi.41.100187.000535, PMID 3318666. 
  4. ^ Boman HG (1991), "Antibacterial peptides: key components needed in immunity", Cell, 65 (2): 205–207, doi:10.1016/0092-8674(91)90154-Q, PMID 2015623. 
  5. ^ Boman HG, Faye I, Lee JY, Gudmundsson GH, Lidholm DA (1991), "Cell-free immunity in Cecropia. A model system for antibacterial proteins", Eur. J. Biochem., 201 (1): 23–31, doi:10.1111/j.1432-1033.1991.tb16252.x, PMID 1915368. 
  6. ^ a b c d Hoskin, D.W.; Ramamoorthy, A. (February 2008), "Studies on anticancer activities of antimicrobial peptides", Biochimica et Biophysica Acta (BBA) - Biomembranes, 1778 (2): 357–375, doi:10.1016/j.bbamem.2007.11.008, PMC 2238813Freely accessible, PMID 18078805 
  7. ^ Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567
  8. ^ a b cecropin family OPM
  9. ^ Protein Data Bank (1930), Solution structure of CB1a, a novel anticancer peptide derived from natural antimicrobial peptide cecropin B  [<http://www.rcsb.org/pdb/explore/explore.do?structureId=2IGR> <Protein Data Bank>]

Further reading

  • Hoskin 2008 (above) section 4.2

External links


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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000875

Cecropins [PUBMED:3318666, PUBMED:2015623, PUBMED:1915368] are potent antibacterial proteins that constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 35 amino acid residues active against both Gram-positive and Gram-negative bacteria. They seem to exert a lytic action on bacterial membranes. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names; bactericidin, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related.

Gene Ontology

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Domain organisation

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Alignments

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(30)
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(300)
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(381)
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(25)
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RP75
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(30)
Full
(107)
Representative proteomes UniProt
(300)
NCBI
(381)
Meta
(0)
RP15
(25)
RP35
(60)
RP55
(78)
RP75
(100)
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  Seed
(30)
Full
(107)
Representative proteomes UniProt
(300)
NCBI
(381)
Meta
(0)
RP15
(25)
RP35
(60)
RP55
(78)
RP75
(100)
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: cecropin;
Type: Family
Author: Finn RD, Bateman A
Number in seed: 30
Number in full: 107
Average length of the domain: 30.50 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 44.73 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 26.8 26.2
Noise cut-off 21.8 24.2
Model length: 30
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cecropin domain has been found. There are 13 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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