ACTPA_ACTTE
ID ACTPA_ACTTE Reviewed; 20 AA.
AC P30833;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Cytolysin tenebrosin-A {ECO:0000303|PubMed:1970442};
DE AltName: Full=DELTA-actitoxin {ECO:0000305};
DE Flags: Fragment;
OS Actinia tenebrosa (Australian red waratah sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6105;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1970442; DOI=10.1016/0041-0101(90)90004-q;
RA Norton R.S., Bobek G., Ivanov J.O., Thomson M., Fiala-Beer E., Moritz R.L.,
RA Simpson R.J.;
RT "Purification and characterisation of proteins with cardiac stimulatory and
RT haemolytic activity from the anemone Actinia tenebrosa.";
RL Toxicon 28:29-41(1990).
RN [2]
RP REVIEW.
RX PubMed=19268680; DOI=10.1016/j.toxicon.2009.02.026;
RA Kristan K.C., Viero G., Dalla Serra M., Macek P., Anderluh G.;
RT "Molecular mechanism of pore formation by actinoporins.";
RL Toxicon 54:1125-1134(2009).
CC -!- FUNCTION: Pore-forming protein that forms cations-selective hydrophilic
CC pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore
CC formation is a multi-step process that involves specific recognition of
CC membrane sphingomyelin (but neither cholesterol nor
CC phosphatidylcholine) using aromatic rich region and adjacent
CC phosphocholine (POC) binding site, firm binding to the membrane (mainly
CC driven by hydrophobic interactions) accompanied by the transfer of the
CC N-terminal region to the lipid-water interface and finally pore
CC formation after oligomerization of monomers.
CC -!- SUBUNIT: Tetramer in the presence of a lipidic interface. Monomer, in
CC soluble state. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC Target cell membrane. Note=Forms an alpha-helical membrane channel in
CC the prey.
CC -!- DOMAIN: The N-terminal region, before the pore is formed, is bound to
CC the lipid membrane. It partitions into the lipid-water interface and
CC stabilizes the monomeric molecule on the membrane. Finally, it
CC traverses the bilayer, thus forming the transmembrane pore.
CC {ECO:0000250|UniProtKB:P61914}.
CC -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
CC {ECO:0000305}.
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DR PIR; A34016; A34016.
DR AlphaFoldDB; P30833; -.
DR TCDB; 1.C.38.1.3; the pore-forming equinatoxin (equinatoxin) family.
DR Proteomes; UP000515163; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Hemolysis; Ion transport; Membrane;
KW Nematocyst; Reference proteome; Secreted; Target cell membrane;
KW Target membrane; Toxin; Transmembrane; Transport.
FT CHAIN 1..>20
FT /note="Cytolysin tenebrosin-A"
FT /id="PRO_0000221530"
FT REGION 3..12
FT /note="Plays an important role in the hemolytic activity"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT REGION 11..>20
FT /note="N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT NON_TER 20
SQ SEQUENCE 20 AA; 1974 MW; FA32AC8BDAAFF5FA CRC64;
NAAVAGAVIE GATLTFEVLQ
