ID   NA11_ANTEL              Reviewed;          47 AA.
AC   P0C1F0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Delta-actitoxin-Ael1b {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Ael1b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin APE 1-1 {ECO:0000303|PubMed:11072049};
OS   Anthopleura elegantissima (Green aggregating anemone) (Actinia
OS   elegantissima).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anthopleura.
OX   NCBI_TaxID=6110;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND TOXIC DOSE.
RX   PubMed=11072049; DOI=10.1016/s0041-0101(00)00199-9;
RA   Bruhn T., Schaller C., Schulze C., Sanchez-Rodriguez J., Dannmeier C.,
RA   Ravens U., Heubach J.F., Eckhardt K., Schmidtmayer J., Schmidt H.,
RA   Aneiros A., Wachter E., Beress L.;
RT   "Isolation and characterisation of five neurotoxic and cardiotoxic
RT   polypeptides from the sea anemone Anthopleura elegantissima.";
RL   Toxicon 39:693-702(2001).
RN   [2]
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: Produces a positive inotropic effect in mammalian heart
CC       muscle. Modifies current passing through the fast sodium channel (Nav)
CC       in neuroblastoma cells, leading to delayed and incomplete inactivation.
CC       Paralyzes the shore crab (C.maenas) by tetanic contractions after
CC       intramuscular injection. {ECO:0000269|PubMed:11072049}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 10 ug/kg by intramuscular injection into crabs.
CC       {ECO:0000269|PubMed:11072049}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1F0; -.
DR   SMR; P0C1F0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR000693; Anenome_toxin.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR   PIRSF; PIRSF001905; Anenome_toxin; 1.
PE   1: Evidence at protein level;
KW   Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..47
FT                   /note="Delta-actitoxin-Ael1b"
FT                   /evidence="ECO:0000269|PubMed:11072049"
FT                   /id="PRO_0000236024"
FT   DISULFID        4..44
FT                   /evidence="ECO:0000250|UniProtKB:P10453"
FT   DISULFID        6..34
FT                   /evidence="ECO:0000250|UniProtKB:P10453"
FT   DISULFID        27..45
FT                   /evidence="ECO:0000250|UniProtKB:P10453"
SQ   SEQUENCE   47 AA;  4803 MW;  A28BAF5FB05DE53A CRC64;
     GIACLCDSDG PSVRGNTLSG TYWLAGCPSG WHNCKSSGQL IGACCKQ