ID ACTPP_ACTEQ Reviewed; 20 AA. AC P0C1H1; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 03-MAR-2009, entry version 14. DE RecName: Full=Equinatoxin-1''; DE AltName: Full=Equinatoxin I''; DE Flags: Fragment; OS Actinia equina (European sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Nynantheae; Actiniidae; Actinia. OX NCBI_TaxID=6106; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=99341830; PubMed=10414864; DOI=10.1016/S0041-0101(99)00082-3; RA Anderluh G., Krizaj I., Strukelj B., Gubensek F., Macek P., RA Pungercar J.; RT "Equinatoxins, pore-forming proteins from the sea anemone Actinia RT equina, belong to a multigene family."; RL Toxicon 37:1391-1401(1999). RN [2] RP AMINO-ACID COMPOSITION, AND LETHAL DOSE. RX PubMed=2903587; DOI=10.1016/0041-0101(88)90183-3; RA Macek P., Lebez D.; RT "Isolation and characterization of three lethal and hemolytic toxins RT from the sea anemone Actinia equina L."; RL Toxicon 26:441-451(1988). CC -!- FUNCTION: This cardiac stimulatory and hemolytic pore-forming CC protein forms cations-selective hydrophilic pores of around 1 nm. CC Cytolytic effects include red blood cells hemolysis, platelet CC aggregation and lysis, cytotoxic and cytostatic effects on CC fibroblasts. Lethality in mammals has been ascribed to severe CC vasospasm of coronary vessels, cardiac arrhythmia, and inotropic CC effects. Pore formation proceeds by membrane binding via a surface CC rich in aromatic residues, followed by translocation of the N- CC terminal region to the membrane and, finally, across the bilayer CC to form a functional pore (By similarity). CC -!- SUBUNIT: Tetramer in the presence of a lipidic interface. Monomer, CC in soluble state (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst. Membrane (By CC similarity). Note=Forms a membrane channel in the prey (By CC similarity). CC -!- DOMAIN: The N-terminal region, before the pore is formed, is bound CC to the lipid membrane. It partitions into the lipid-water CC interface and stabilizes the monomeric molecule on the membrane. CC Finally, it traverses the bilayer, thus forming the transmembrane CC pore (By similarity). CC -!- TOXIC DOSE: LD(50) is 23 ug/kg by intravenous injection into mice. CC -!- SIMILARITY: Belongs to the sea anemone actinoporin family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-KW. DR GO; GO:0046930; C:pore complex; IEA:InterPro. DR GO; GO:0015267; F:channel activity; IEA:InterPro. DR GO; GO:0006812; P:cation transport; IEA:InterPro. DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. DR GO; GO:0019836; P:hemolysis by symbiont of host red blood cells; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0046931; P:pore complex biogenesis; IEA:InterPro. DR InterPro; IPR009104; Anemon_Cytolysin. DR Pfam; PF06369; Anemone_cytotox; 1. PE 1: Evidence at protein level; KW Cytolysis; Direct protein sequencing; Hemolysis; Ion transport; KW Membrane; Nematocyst; Porin; Secreted; Toxin; Transmembrane; KW Transport. FT PEPTIDE 1 >20 Equinatoxin-1''. FT /FTId=PRO_0000244624. FT REGION 11 ? N-terminal region (By similarity). FT NON_TER 20 20 SQ SEQUENCE 20 AA; 1960 MW; FA32B426009FF5FA CRC64; SVAVAGAVIE GATLTFNVLQ //