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1.C.43.1.1
Lysenin of 297 aas and 1 N-terminal TMS, a sphingomyelin-specific pore-forming toxin from earthworms; causes contraction of rat vascular smooth muscle. (Sekizawa et al., 1997; Shogomori and Kobayashi, 2007). Trp-20 is required for cation selective channel assembly (Kwiatkowska et al., 2007).  Adenosine phosphates control the activity of lysenin channels inserted into planar lipid membranes with respect to their macroscopic conductance and voltage-induced gating. Addition of ATP, ADP, or AMP decreased the macroscopic conductance of lysenin channels in a concentration-dependent manner, with ATP being the most potent inhibitor and AMP the least (Bryant et al. 2016). lysenin can specifically interact with sphingomyelin, and may confer innate immunity against parasites by attacking the membranes of the parasites to form pores (Pang et al. 2019).  Upon binding to sphingomyelin (SM)-containing membranes, lysenin undergoes a series of structural changes promoting the conversion of water-soluble monomers into oligomers, leading to its insertion into the membrane and the 2-step formation of a lytic beta-barrel pore (Kulma et al. 2019). Structural stabilization of the lysenin prepore starts at the site of  initial interaction with the lipid membrane and is transmitted to the twisted beta-sheet of the N-terminal domain (Kulma et al. 2019). 3-d structures are available (PDB# 5EC5; 3ZXD; 3ZX7). The beta pore-forming toxins (beta-PFTs) are cytotoxic proteins produced as soluble monomers, which cluster and oligomerize at the membrane of the target host cells. Their initial oligomeric state, the prepore, is not cytotoxic. The beta-PFTs undergo a large structural transition to a second oligomeric state, the pore, which pierces the membrane of the host cell and is cytotoxic. Munguira et al. 2019 described the mechanism by which the rates of formation of the transmembrane pores correlate with the local levels of crowding for the beta-PFT lysenin.

Accession Number:O18423
Protein Name:EFL1
Length:297
Molecular Weight:33441.00
Species:Eisenia foetida (Common brandling worm) (Common dung-worm) [6396]
Location1 / Topology2 / Orientation3: Secreted1
Substrate ions

Cross database links:

Gene Ontology

GO:0044218 C:other organism cell membrane
GO:0046930 C:pore complex
GO:0019835 P:cytolysis
GO:0042742 P:defense response to bacterium
GO:0019836 P:hemolysis by symbiont of host erythrocytes
GO:0006811 P:ion transport
GO:0009405 P:pathogenesis

References (6)

[1] “Molecular cloning of cDNA for lysenin, a novel protein in the earthworm Eisenia foetida that causes contraction of rat vascular smooth muscle.”  Sekizawa Y.et.al.   9210594
[2] “Lysenin, a novel sphingomyelin-specific binding protein.”  Yamaji A.et.al.   9478988
[3] “Lethal and non-lethal responses of spermatozoa from a wide variety of vertebrates and invertebrates to lysenin, a protein from the coelomic fluid of the earthworm Eisenia foetida.”  Kobayashi H.et.al.   10684578
[4] “Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin.”  Yamaji-Hasegawa A.et.al.   12676961
[5] “Recognition of sphingomyelin by lysenin and lysenin-related proteins.”  Kiyokawa E.et.al.   15274631
[6] “Exfoliation of the epidermal cells and defecation by amphibian larvae in response to coelomic fluid and lysenin from the earthworm Eisenia foetida.”  Kobayashi H.et.al.   16971770
Structure:
3ZX7   3ZXD   3ZXG   5ec5     

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)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSAKAAEGYE QIEVDVVAVW KEGYVYENRG STSVDQKITI TKGMKNVNSE TRTVTATHSI 
61:	GSTISTGDAF EIGSVEVSYS HSHEESQVSM TETEVYESKV IEHTITIPPT SKFTRWQLNA 
121:	DVGGADIEYM YLIDEVTPIG GTQSIPQVIT SRAKIIVGRQ IILGKTEIRI KHAERKEYMT 
181:	VVSRKSWPAA TLGHSKLFKF VLYEDWGGFR IKTLNTMYSG YEYAYSSDQG GIYFDQGTDN 
241:	PKQRWAINKS LPLRHGDVVT FMNKYFTRSG LCYDDGPATN VYCLDKREDK WILEVVG