ID   NA1C1_BUNCN             Reviewed;          48 AA.
AC   P82803;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Delta-actitoxin-Bcg1a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Bcg1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Cangitoxin {ECO:0000303|PubMed:15626370};
DE            Short=CGTX;
DE            Short=CGX {ECO:0000303|PubMed:15626370};
OS   Bunodosoma cangicum (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Bunodosoma.
OX   NCBI_TaxID=138296;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Nematoblast;
RX   PubMed=15626370; DOI=10.1016/j.toxicon.2004.10.011;
RA   Cunha R.B., Santana A.N.C., Amaral P.C., Carvalho M.D., Carvalho D.M.,
RA   Cavalheiro E.A., Maigret B., Ricart C.A.O., Cardi B.A., Sousa M.V.,
RA   Carvalho K.M.;
RT   "Primary structure, behavioral and electroencephalographic effects of an
RT   epileptogenic peptide from the sea anemone Bunodosoma cangicum.";
RL   Toxicon 45:207-217(2005).
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: Binds specifically to voltage-gated sodium channels (Nav),
CC       thereby delaying their inactivation during signal transduction. Thus it
CC       strongly stimulates mammalian cardiac muscle contraction.
CC       {ECO:0000269|PubMed:15626370}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15626370}.
CC       Nematocyst {ECO:0000305|PubMed:15626370}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P82803; -.
DR   SMR; P82803; -.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Nematocyst; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..48
FT                   /note="Delta-actitoxin-Bcg1a"
FT                   /evidence="ECO:0000269|PubMed:15626370"
FT                   /id="PRO_0000221520"
FT   DISULFID        4..45
FT                   /evidence="ECO:0000250|UniProtKB:P01530"
FT   DISULFID        6..35
FT                   /evidence="ECO:0000250|UniProtKB:P01530"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000250|UniProtKB:P01530"
SQ   SEQUENCE   48 AA;  4963 MW;  E88810EB85E1F456 CRC64;
     GVACRCDSDG PTVRGNSLSG TLWLTGGCPS GWHNCRGSGP FIGYCCKK