UniProt functional annotation for P61914



	UniProt functional annotation for P61914

UniProt code: P61914.

Organism: Actinia equina (Beadlet anemone).

Taxonomy: Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; Actiniidae; Actinia.

Function: Pore-forming protein that 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) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.

Subunit: Tetramer in the presence of a lipidic interface. Monomer, in soluble state.

Subcellular location: Secreted. Nematocyst. Target cell membrane. Note=Forms an alpha-helical membrane channel in the prey.

Domain: The N-terminal region, before the pore is formed, is bound to the lipid membrane. It partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore. {ECO:0000269|PubMed:10429196}.

Toxic dose: LD(50) is 35 ug/kg by intravenous injection into mice. {ECO:0000269|PubMed:2903587}.

Similarity: Belongs to the actinoporin family. Sea anemone subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Actinia equina (Beadlet anemone).
Taxonomy:		Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; Actiniidae; Actinia.



Function:		Pore-forming protein that 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) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.


Subunit:		Tetramer in the presence of a lipidic interface. Monomer, in soluble state.
Subcellular location:		Secreted. Nematocyst. Target cell membrane. Note=Forms an alpha-helical membrane channel in the prey.
Domain:		The N-terminal region, before the pore is formed, is bound to the lipid membrane. It partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore. {ECO:0000269\|PubMed:10429196}.
Toxic dose:		LD(50) is 35 ug/kg by intravenous injection into mice. {ECO:0000269\|PubMed:2903587}.
Similarity:		Belongs to the actinoporin family. Sea anemone subfamily. {ECO:0000305}.