ACTPG_OULOR
ID ACTPG_OULOR Reviewed; 173 AA.
AC Q5I2B1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=DELTA-actitoxin-Oor1b {ECO:0000303|PubMed:22683676};
DE Short=DELTA-AITX-Oor1b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Actinoporin Or-G {ECO:0000303|PubMed:15787212, ECO:0000303|PubMed:16119454};
DE AltName: Full=Cytolysin Or-G {ECO:0000303|PubMed:15787212};
OS Oulactis orientalis (Japan anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Oulactis.
OX NCBI_TaxID=308032;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16119454;
RA Il'ina A.P., Monastyrnaia M.M., Isaeva M.P., Guzev K.V., Rasskazov V.A.,
RA Kozlovskaya E.P.;
RT "Primary structures of actinoporins from sea anemone Oulactis orientalis.";
RL Bioorg. Khim. 31:357-362(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-8.
RX PubMed=15787212;
RA Il'ina A.P., Monastyrnaia M.M., Sokotun I.N., Egorov T.A., Nazarenko I.A.,
RA Likhatskaia G.N., Kozlovskaya E.P.;
RT "Actinoporins from the Sea of Japan anemone Oulactis orientalis: isolation
RT and partial characterization.";
RL Bioorg. Khim. 31:39-48(2005).
RN [3]
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).
RN [4]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
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. Cytolytic effects include
CC red blood cells hemolysis, platelet aggregation and lysis, cytotoxic
CC and cytostatic effects on fibroblasts. Lethality in mammals has been
CC ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia,
CC and inotropic effects (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Tetramer in the presence of a lipidic interface. Monomer, in
CC soluble state (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst. Target cell membrane
CC {ECO:0000250}. Note=Forms an alpha-helical membrane channel in the
CC prey. {ECO:0000250}.
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 EMBL; AY861662; AAW47579.1; -; mRNA.
DR AlphaFoldDB; Q5I2B1; -.
DR SMR; Q5I2B1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006812; P:cation transport; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0046931; P:pore complex assembly; IEA:InterPro.
DR Gene3D; 2.60.270.20; -; 1.
DR InterPro; IPR009104; Anemon_actinoporin-like.
DR InterPro; IPR015926; Cytolysin/lectin.
DR Pfam; PF06369; Anemone_cytotox; 1.
DR SUPFAM; SSF63724; SSF63724; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Hemolysis; Ion transport; Membrane;
KW Nematocyst; Secreted; Target cell membrane; Target membrane; Toxin;
KW Transmembrane; Transport.
FT CHAIN 1..173
FT /note="DELTA-actitoxin-Oor1b"
FT /id="PRO_0000239262"
FT REGION 6..25
FT /note="N-terminal region"
FT /evidence="ECO:0000250"
FT REGION 100..115
FT /note="Trp-rich region, which is important for the binding
FT to lipid membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT BINDING 49
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250"
FT SITE 108
FT /note="Important in the initial contact with the lipid
FT membrane"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 18733 MW; 59502F48FCBAF34D CRC64;
GAIIAGAALG FNVHQTVLKA LGQVSRKIAI GVDNESGGTW TALNAYFRSG TTDVILPEFV
PNQKALLYSG QKDTGPVATG AVGVLAYYMS DGNTLGVMFS VPFDYNLYSN WWDVKVYRGR
RRADQAMYEG LLYGIPYGGD NGWHARKLGY GLKGRGFMKS SAQSILEIHV TKA
