ACTP2_PHYSE
ID ACTP2_PHYSE Reviewed; 226 AA.
AC P0DL56; D2YZQ4; Q8IAE2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=DELTA-alicitoxin-Pse1b;
DE Short=DELTA-ALTX-Pse1b;
DE AltName: Full=Pst-I {ECO:0000303|PubMed:20837039};
DE Flags: Precursor;
OS Phyllodiscus semoni (Night anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Nynantheae; Aliciidae; Phyllodiscus.
OX NCBI_TaxID=163701;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 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 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.
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; AB512461; BAI70365.1; -; mRNA.
DR AlphaFoldDB; P0DL56; -.
DR SMR; P0DL56; -.
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:P0DL55"
FT /id="PRO_0000433628"
FT CHAIN 48..226
FT /note="DELTA-alicitoxin-Pse1b"
FT /id="PRO_0000433629"
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"
SQ SEQUENCE 226 AA; 25167 MW; 7F50634384911137 CRC64;
MRHFVVFLYM FLALSIPTAF AKKHIVTKKG NHQDITNDNE GENAEKKSAT VAGAVIAGGE
LALKILTKIL YEIGKIDRKI AIGVDNESGL KWTALNTYYK SGASDVTLPY EVENSKALLY
TARKSKGPVA RGAVGVLAYK MSSGNTLAVM FSVPFDYNLY SNWWNVKIYD GEKKADEKMY
NELYNNNNPI KPSTWEKRDL GKDGLKLRGF MTSNGDAKLV IHIEKS
