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1.C.59.1.1
CPE; has been used for suicide gene therapy for selective treatment of claudin-3-and-4-overexpressing tumors (Walther et al., 2011).  It can be used as an oncoleaking/tumor eradication agent as this pore-forming protein exerts specific and rapid toxicity towards claudin-3- and -4-overexpressing cancers (Pahle et al. 2015). The crystal structure of Clostridium perfringens enterotoxin displays features of beta-pore-forming toxins (Kitadokoro et al., 2011). The N-terminal region (nCPE) mediates the cytotoxic effect through pore formation in the plasma membrane of the mammalian host cell. The C-terminal region (cCPE) binds to the second extracellular loop of a subset of claudins, Claudin-3 and claudin-4, with high affinity (Veshnyakova et al., 2010). cCPE is not cytotoxic but is a potent modulator of tight junctions.

Accession Number:P01558
Protein Name:Heat-labile enterotoxin B chain [Precursor]
Length:319
Molecular Weight:35330.00
Species:Clostridium perfringens [1502]
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules

Cross database links:

RefSeq: YP_473394.1    YP_473485.1   
Entrez Gene ID: 3896957    3897031   
Pfam: PF03505   

Gene Ontology

GO:0005576 C:extracellular region
GO:0009405 P:pathogenesis

References (11)

[1] “The amino acid sequence of the enterotoxin from Clostridium perfringens type A.”  Richardson M.et.al.   3920076
[2] “Cloning and sequencing of the Clostridium perfringens enterotoxin gene.”  Van Damme-Jongsten M.et.al.   2802575
[3] “Cloning, nucleotide sequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli.”  Czeczulin J.R.et.al.   8335373
[4] “A complex array of Hpr consensus DNA recognition sequences proximal to the enterotoxin gene in Clostridium perfringens type A.”  Brynestad S.et.al.   8162194
[5] “The enterotoxin gene (cpe) of Clostridium perfringens can be chromosomal or plasmid-borne.”  Cornillot E.et.al.   7783636
[6] “Clostridium perfringens enterotoxin from equine isolates; its characterisation, sequence and role in foal diarrhoea.”  Netherwood T.et.al.   9593490
[7] “Organization of the plasmid cpe Locus in Clostridium perfringens type A isolates.”  Miyamoto K.et.al.   12117935
[8] “Sequence of the amino-terminal part of enterotoxin from Clostridium perfringens type A: identification of points of trypsin activation.”  Richardson M.et.al.   6303961
[9] “Cloning in Escherichia coli of the enterotoxin gene from Clostridium perfringens type A.”  Iwanejko L.A.et.al.   2557378
[10] “Expression from the Clostridium perfringens cpe promoter in C. perfringens and Bacillus subtilis.”  Melville S.B.et.al.   7960138
[11] “Molecular cloning of the 3' half of the Clostridium perfringens enterotoxin gene and demonstration that this region encodes receptor-binding activity.”  Hanna P.C.et.al.   2556374
Structure:
2QUO   2XH6   2YHJ   3AM2   3X29   3ZIW   3ZIX   4P5H   5b2g      [...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)
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FASTA formatted sequence
1:	MLSNNLNPMV FENAKEVFLI SEDLKTPINI TNSNSNLSDG LYVIDKGDGW ILGEPSVVSS 
61:	QILNPNETGT FSQSLTKSKE VSINVNFSVG FTSEFIQASV EYGFGITIGE QNTIERSVST 
121:	TAGPNEYVYY KVYATYRKYQ AIRISHGNIS DDGSIYKLTG IWLSKTSADS LGNIDQGSLI 
181:	ETGERCVLTV PSTDIEKEIL DLAAATERLN LTDALNSNPA GNLYDWRSSN SYPWTQKLNL 
241:	HLTITATGQK YRILASKIVD FNIYSNNFNN LVKLEQSLGD GVKDHYVDIS LDAGQYVLVM 
301:	KANSSYSGNY PYSILFQKF