ACTP1_SAGRO
ID ACTP1_SAGRO Reviewed; 216 AA.
AC Q86FQ0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=DELTA-sagatoxin-Srs1a {ECO:0000303|PubMed:22683676};
DE Short=DELTA-SATX-Srs1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Cytolysin Src-1 {ECO:0000305};
DE AltName: Full=Src I {ECO:0000303|PubMed:12419507};
DE Flags: Precursor;
OS Sagartia rosea (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Sagartiidae; Sagartia.
OX NCBI_TaxID=396345;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TOXIC DOSE.
RC TISSUE=Tentacle;
RX PubMed=12419507; DOI=10.1016/s0041-0101(02)00173-3;
RA Jiang X.Y., Yang W.-L., Chen H.-P., Tu H.-B., Wu W.Y., Wei J.-W., Wang J.,
RA Liu W.-H., Xu A.-L.;
RT "Cloning and characterization of an acidic cytolysin cDNA from sea anemone
RT Sagartia rosea.";
RL Toxicon 40:1563-1569(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Tentacle;
RX PubMed=14680802; DOI=10.1016/j.bbrc.2003.10.159;
RA Jiang X.Y., Chen H.-P., Yang W.-L., Liu Y., Liu W.-H., Wei J.-W., Tu H.-B.,
RA Xie X., Wang L., Xu A.-L.;
RT "Functional expression and characterization of an acidic actinoporin from
RT sea anemone Sagartia rosea.";
RL Biochem. Biophys. Res. Commun. 312:562-570(2003).
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 cytolysis and hemolysis. Pore formation
CC is a multi-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. {ECO:0000269|PubMed:14680802}.
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 Note=Forms an alpha-helical membrane channel in 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: Dose that lyses erythrocyte suspension (ED(50)) is 0.86
CC ug/ml. {ECO:0000269|PubMed:12419507}.
CC -!- MISCELLANEOUS: The partial protein sequence of PubMed:14680802
CC corresponds to the N-terminal amino acid sequence.
CC -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
CC {ECO:0000305}.
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DR EMBL; AY247033; AAP04347.1; -; mRNA.
DR AlphaFoldDB; Q86FQ0; -.
DR SMR; Q86FQ0; -.
DR TCDB; 1.C.38.1.11; the pore-forming equinatoxin (equinatoxin) family.
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; Signal; Target cell membrane; Target membrane; Toxin;
KW Transmembrane; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..38
FT /note="Cleaved by a proline-endopeptidase-like protease"
FT /id="PRO_0000239806"
FT CHAIN 39..216
FT /note="DELTA-sagatoxin-Srs1a"
FT /id="PRO_0000239807"
FT REGION 40..49
FT /note="Plays an important role in the hemolytic activity"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT REGION 48..67
FT /note="N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT REGION 142..157
FT /note="Trp-rich region, which is important for the binding
FT to lipid membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT BINDING 91
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 124
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 142
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 144
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 170
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 174
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 175
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT SITE 150
FT /note="Important in the initial contact with the lipid
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
SQ SEQUENCE 216 AA; 23944 MW; CCFCE2F374F77065 CRC64;
MSRLIVVCIV ISMICGALSL SSTKMADEKK EKDEDEKPKI SGGTVIAAGR LTLDLLKTLL
GTLGSISRKI AIGVDNETGG LITGNNVYFR SGTSDDILPH RVETGEALLY TARKTKGPVA
TGAVGVFTYY LSDGNTLAVL FSVPFDYNFY SNWWNVKIYS GKRNADYDMY HELYYDANPF
EGDDTWEYRY LGYGMRMEGY MNSPGEAILK ITVMPD
