ACTP1_ANTAS
ID ACTP1_ANTAS Reviewed; 213 AA.
AC C5NSL2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=DELTA-actitoxin-Aas1a {ECO:0000303|PubMed:22683676};
DE Short=DELTA-AITX-Aas1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Bandaporin {ECO:0000303|Ref.1};
DE Short=Cytolysin bp-1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
OS Anthopleura asiatica (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anthopleura.
OX NCBI_TaxID=160217;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-83; 104-111; 155-160;
RP 187-193 AND 196-212, AND FUNCTION.
RA Kohno Y., Satoh H., Iguchi A., Nagai H.;
RT "Characterization of a new hemolytic protein toxin from the sea anemone
RT Anthopleura asiatica.";
RL Fish. Sci. 75:1049-1054(2009).
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).
RN [3]
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 cation-selective hydrophilic
CC pores of around 1 nm and causes hemolysis. Pore formation is a multi-
CC step process that involves specific recognition of membrane
CC sphingomyelin (but neither cholesterol nor phosphatidylcholine) using
CC aromatic rich region and adjacent phosphocholine (POC) binding site,
CC firm binding to the membrane (mainly driven by hydrophobic
CC interactions) accompanied by the transfer of the N-terminal region to
CC the lipid-water interface and finally pore formation after
CC oligomerization of monomers (By similarity). This protein shows potent
CC hemolytic activity (EC(50)=8.8 ng/ml) that is specifically inhibited by
CC sphingomyelin. Shows no phospholipase A2 activity, nor antimicrobial
CC activity against the four bacteria tested. Is lethal to crayfish
CC (Ref.1). {ECO:0000250, ECO:0000269|Ref.1}.
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 -!- TOXIC DOSE: LD(100) is 0.58 mg/kg to crayfish.
CC -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
CC {ECO:0000305}.
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DR EMBL; AB479475; BAH80315.1; -; mRNA.
DR AlphaFoldDB; C5NSL2; -.
DR SMR; C5NSL2; -.
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 Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Hemolysis; Ion transport; Membrane; Nematocyst; Secreted; Signal;
KW Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..34
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000395609"
FT CHAIN 35..213
FT /note="DELTA-actitoxin-Aas1a"
FT /id="PRO_0000395610"
FT REGION 37..46
FT /note="Plays an important role in the hemolytic activity"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT REGION 45..64
FT /note="N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT REGION 139..154
FT /note="Trp-rich region, which is important for the binding
FT to lipid membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT MOTIF 178..180
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 121
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 139
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 141
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 167
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 171
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 172
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT SITE 147
FT /note="Important in the initial contact with the lipid
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
SQ SEQUENCE 213 AA; 23316 MW; D8823A22B51198EF CRC64;
MSRLIIAFIV VTMVCSAIAL PKKKVEPLEK DEKRSLAVAG AVIEGGNLVM SVLDRILEAI
GDVNRKIAIG VENQSGKSWT AMNTYFRSGT SDVVLPHSVP SGKALLYDGQ KTRGPVATGV
VGVFAYAMSD GNTLAVMFSI PYDYNLYSNW WNVKTYSGMK RADQSMYEDL YYHASPFKGD
NGWHSRNLGY GLKCRGFMNS SGAAKLEIHV SRA
