ACTP2_ACTVL
ID ACTP2_ACTVL Reviewed; 226 AA.
AC D2YZQ3; D2YZQ6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=DELTA-thalatoxin-Avl1b {ECO:0000303|PubMed:22683676};
DE Short=DELTA-TATX-Avl1b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Cytolysin Avt-II {ECO:0000303|PubMed:20837039};
DE AltName: Full=Hemolytic toxin Avt-2 {ECO:0000305};
DE Flags: Precursor;
OS Actineria villosa (Okinawan sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Nynantheae; Aliciidae; Actineria.
OX NCBI_TaxID=227975;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Tentacle;
RX PubMed=20837039; DOI=10.1016/j.toxicon.2010.09.002;
RA Uechi G., Toma H., Arakawa T., Sato Y.;
RT "Molecular characterization on the genome structure of hemolysin toxin
RT isoforms isolated from sea anemone Actineria villosa and Phyllodiscus
RT semoni.";
RL Toxicon 56:1470-1476(2010).
RN [2]
RP ERRATUM OF PUBMED:20837039.
RA Uechi G., Toma H., Arakawa T., Sato Y.;
RL Toxicon 57:625-625(2011).
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 cations-selective hydrophilic
CC pores of around 1 nm (By similarity) and causes hemolysis
CC (PubMed:20837039). Pore formation is a multi-step process that involves
CC specific recognition of membrane sphingomyelin (but neither cholesterol
CC nor 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q5R231, ECO:0000269|PubMed:20837039}.
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 {ECO:0000250}. Note=Forms an alpha-helical
CC membrane channel in the 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; AB512460; BAI70364.1; -; mRNA.
DR EMBL; AB512463; BAI70367.1; -; Genomic_DNA.
DR AlphaFoldDB; D2YZQ3; -.
DR SMR; D2YZQ3; -.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytolysis; Hemolysis; Ion transport;
KW Membrane; Nematocyst; Secreted; Signal; Target cell membrane;
KW Target membrane; Toxin; Transmembrane; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..45
FT /evidence="ECO:0000250|UniProtKB:Q5R231"
FT /id="PRO_0000395611"
FT CHAIN 48..226
FT /note="DELTA-thalatoxin-Avl1b"
FT /id="PRO_0000395612"
FT REGION 50..59
FT /note="Plays an important role in the hemolytic activity"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT REGION 58..77
FT /note="N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT REGION 152..167
FT /note="Trp-rich region, which is important for the binding
FT to lipid membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT BINDING 101
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 134
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 152
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 154
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 180
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 184
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT SITE 160
FT /note="Important in the initial contact with the lipid
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT CONFLICT 31
FT /note="N -> T (in Ref. 1; BAI70367)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="A -> T (in Ref. 1; BAI70367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25115 MW; 7BBB221EEA408A4A CRC64;
MRHFVVFLYM FLALSIPTAF AKKHIVTKKG NHQDITNDNE GENAEKKSAA VAGAVIAGGE
LALKILTKIL DEIGKIDRKI AIGVDNESGL KWTALNTYYK SGASDVTLPY EVENSKALLY
TARKSKGPVA RGAVGVLAYK MSSGNTLAVM FSVPFDYNLY TNWWNVKIYD GEKKADEKMY
NELYNNNNPI KPSIWEKRDL GQDGLKLRGF MTSNGDAKLV IHIEKS
