Summary: Cecropin family
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Cecropin Edit Wikipedia article
| Cecropin family | |||||||||
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| Identifiers | |||||||||
| Symbol | Cecropin | ||||||||
| Pfam | PF00272 | ||||||||
| InterPro | IPR000875 | ||||||||
| PROSITE | PDOC00241 | ||||||||
| SCOP | 1f0d | ||||||||
| SUPERFAMILY | 1f0d | ||||||||
| TCDB | 1.C.17 | ||||||||
| OPM superfamily | 160 | ||||||||
| OPM protein | 1d9j | ||||||||
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Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, from 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, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related. Cecropin P1, an intestinal antibacterial peptide from Sus scrofa (Pig), also belongs to this family. Cecropin family also consists Cecropin A and Cecropin B.
Cecropin is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.[6] At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.[7]
[edit] References
- ^ Cecropins at the US National Library of Medicine Medical Subject Headings (MeSH)
- ^ 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): 8973â83, doi:10.1074/jbc.M806778200, PMC 2659254, PMID 19176529, http://www.jbc.org/cgi/pmidlookup?view=long&pmid=19176529.
- ^ Boman HG, Hultmark D (1987), "Cell-free immunity in insects", Annu. Rev. Microbiol. 41: 103â126, doi:10.1146/annurev.mi.41.100187.000535, PMID 3318666.
- ^ Boman HG (1991), "Antibacterial peptides: key components needed in immunity", Cell 65 (2): 205â207, doi:10.1016/0092-8674(91)90154-Q, PMID 2015623.
- ^ 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): 23â31, doi:10.1111/j.1432-1033.1991.tb16252.x, PMID 1915368.
- ^ 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>]
- ^ Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Cecropin family Provide feedback
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External database links
| PANDIT: | PF00272 |
| PROSITE: | PDOC00241 |
| Pseudofam: | PF00272 |
| SCOP: | 1f0d |
| SYSTERS: | Cecropin |
| Transporter classification: | 1.C.17 |
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. Cecropin P1, an intestinal antibacterial peptide from Sus scrofa (Pig), also belongs to this family.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | extracellular region (GO:0005576) |
Domain organisation
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Alignments
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| Seed (28) |
Full (182) |
Representative proteomes | NCBI (210) |
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| RP15 (15) |
RP35 (26) |
RP55 (47) |
RP75 (56) |
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| PP/heatmap | 1 | |||||||
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| Seed (28) |
Full (182) |
Representative proteomes | NCBI (210) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (15) |
RP35 (26) |
RP55 (47) |
RP75 (56) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
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.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | cecropin; |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 28 |
| Number in full: | 182 |
| Average length of the domain: | 30.50 aa |
| Average identity of full alignment: | 49 % |
| Average coverage of the sequence by the domain: | 49.92 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 30 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| 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 10 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence