TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.38.1.1









Equinatoxin II (EqtII) binds sphingomyelin specifically and localizes to the Golgi apparatus (Bakrac et al., 2010).  Disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII) and sticholysin II (StII) impairs the pore formation activity (Mesa-Galloso et al. 2016).

Eukaryota
Metazoa
Equinatoxin of Actinia tenebrosa (P61915)
*1.C.38.1.2









Sticholysin I (cytolysin ST1 or STII or StiII) (Alvarez et al., 2009). Pore formation goes through a dimer intermediate and then generates the active octamer. Disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII) and sticholysin II (StII) impairs the pore formation activity (Mesa-Galloso et al. 2016).

Eukaryota
Metazoa
Sticholysin I of Stichodactyla helianthus
*1.C.38.1.3









Tenebrosin-A (fragment)
Eukaryota
Metazoa
Tenebrosin-A of Actinia tenebrosa (P30833)
*1.C.38.1.4









Actinoporin Or-A, cation-selective pore forming tetrameric toxin
Eukaryota
Metazoa
Actinoporin Or-A of Oulactis orientalis (sea anenome) (Q5I4B8)
*1.C.38.1.5









Echotoxin-2 precursor, Echt-2 hemolysin (276 aas). Pore-forming protein; forms cation-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves recognition of membrane sphingomyelin using aromatic rich regions and adjacent phosphocholine binding sites for firm binding to the membrane accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers (Kawashima et al., 2003; Shiomi et al., 2002).

Eukaryota
Metazoa
Echt-2 hemolysin of Monplex echo (a marine gastropod)
(Q76CA2)
*1.C.38.1.6









Cytolytic pore-forming tetrameric toxin (forms cation-selective pores (d = 1 nm) (Mebs et al., 1992).
Eukaryota
Metazoa
Cytolysin of Heteractis magnifica
(P39088)
*1.C.38.1.7









The plant actinoporin homologue (293aas). Function unknown.
Eukaryota
Viridiplantae
Actinoporin homologue of Physcomitrella patens (A9S8W4)
*1.C.38.1.8









Fragaceatoxin C (FraC) of the strawberry anemone (Structure solved to 1.8 Å resolution; It is a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm.) Almost identical to Equinatoxin II (1.C.38.1.1) (Mechaly et al., 2011).  Fragaceatoxin C (FraC) is an α-barrel pore-forming toxin (PFT). The crystal structures of FraC at four different stages of the lytic mechanism have been determined at 3.1Å resolution, namely the water-soluble state, the monomeric lipid-bound form, an assembly intermediate and the fully assembled transmembrane pore (Tanaka et al. 2015). The structure of the transmembrane pore exhibits a unique architecture composed of both protein and lipids, with some of the lipids lining the pore wall, acting as assembly cofactors. The pore exhibits lateral fenestrations that expose the hydrophobic core of the membrane to the aqueous environment. The incorporation of lipids from the target membrane within the structure of the pore provides a membrane-specific trigger for the activation of this haemolytic toxin.  It has been reconstituted in  planar lipid bilayers and engineered for DNA analysis.  It shows a funnel-shaped geometry that allows tight wrapping around single-stranded DNA (ssDNA), resolving between homopolymeric C, T, and A polynucleotide stretches (Wloka et al. 2016). Despite the 1.2 nm internal constriction in the FraC pore, double-stranded DNA (dsDNA) can translocate through the nanopore at high applied potentials, presumably through deformation of the alpha-helical transmembrane region. Therefore, FraC nanopores might be useful for DNA sequencing and dsDNA analysis. Pore formation goes through a dimer intermediate and then generates the active octamer. Disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII) and sticholysin II (StII) impairs the pore formation activity (Mesa-Galloso et al. 2016).

Eukaryota
Metazoa
FraC of Actine fragacea (B9W5G6)
*1.C.38.1.9









Equinatoxin 5 of 214 aas (Frazão et al. 2012).

Eukaryota
Metazoa
Equinatoxin-5 of Actinia equina
*1.C.38.1.10









Cytolysin RTX-A of 175 aas. Forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) and requires oligomerization of the toxin subunits (Frazão et al. 2012). 

Eukaryota
Metazoa
Cytolysin RTX-A of Heteactis crispa (Radianthus macrodactylus) (Leathery sea anemone)
*1.C.38.1.11









Cytolysin Src-1 of 216 aas (Frazão et al. 2012).

Eukaryota
Metazoa
Cytolysin Src-1 of Sagartia rosea (sea anemone)
*1.C.38.1.12









Fragaceatoxin C (FraC), an alpha-barrel pore-forming protein, a cytolytic actinoporin, of 152 aas (Morante et al. 2015; Rojko et al. 2015).  Pore formation goes through a dimer intermediate and then generates the active octamer. Disrupting the key hydrophobic interaction between V60 and F163 (FraC numbering scheme) in the oligomerization interface of FraC, equinatoxin II (EqtII) and sticholysin II (StII) impairs the pore formation activity (Mesa-Galloso et al. 2016).

Eukaryota
Metazoa
FraC of Callorhynchus milii
*1.C.38.1.13









Conoporin 1 of 242 aas

Eukaryota
Metazoa
Conotoxin 1 of Conus geographus (Geography cone) (Nubecula geographus)