ID   NA12_BUNGR              Reviewed;          48 AA.
AC   P0C1F4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Delta-actitoxin-Bgr2a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Bgr2a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Bg II {ECO:0000303|PubMed:7911468};
DE            Short=BgII {ECO:0000303|PubMed:11704639};
DE   AltName: Full=Neurotoxin Bg-2;
OS   Bunodosoma granuliferum (Red warty sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Bunodosoma.
OX   NCBI_TaxID=31164;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND TOXIC DOSE.
RX   PubMed=7911468; DOI=10.1016/s0021-9258(19)89460-7;
RA   Loret E.P., del Valle R.M., Mansuelle P., Sampieri F., Rochat H.;
RT   "Positively charged amino acid residues located similarly in sea anemone
RT   and scorpion toxins.";
RL   J. Biol. Chem. 269:16785-16788(1994).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=11704639; DOI=10.1038/sj.bjp.0704361;
RA   Goudet C., Ferrer T., Galan L., Artiles A., Batista C.V.F., Possani L.D.,
RA   Alvarez J., Aneiros A., Tytgat J.;
RT   "Characterization of two Bunodosoma granulifera toxins active on cardiac
RT   sodium channels.";
RL   Br. J. Pharmacol. 134:1195-1206(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=12459477; DOI=10.1016/s0014-5793(02)03653-0;
RA   Bosmans F., Aneiros A., Tytgat J.;
RT   "The sea anemone Bunodosoma granulifera contains surprisingly efficacious
RT   and potent insect-selective toxins.";
RL   FEBS Lett. 532:131-134(2002).
RN   [4]
RP   FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=22015268; DOI=10.1016/j.peptides.2011.10.011;
RA   Rodriguez A.A., Cassoli J.S., Sa F., Dong Z.Q., de Freitas J.C.,
RA   Pimenta A.M., de Lima M.E., Konno K., Lee S.M., Garateix A.,
RA   Zaharenko A.J.;
RT   "Peptide fingerprinting of the neurotoxic fractions isolated from the
RT   secretions of sea anemones Stichodactyla helianthus and Bunodosoma
RT   granulifera. New members of the APETx-like family identified by a 454
RT   pyrosequencing approach.";
RL   Peptides 34:26-38(2012).
RN   [5]
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 voltage-dependently at site 3 of sodium channels (Nav)
CC       and inhibits the inactivation of the activated channels, thereby
CC       blocking neuronal transmission. Possesses the highest efficacy for the
CC       insect sodium channel para/tipE (EC(50)=5.5 nM) (PubMed:12459477), and
CC       has effect on Nav1.2/SCN2A (in complex with SCN1B), Nav1.4/SCN4A (in
CC       complex with SCN1B) and Nav1.5/SCN5A (in complex with SCN1B)
CC       (PubMed:12459477). Also interacts with sodium channels in cardiac cells
CC       (PubMed:11704639). Shows lethality to crabs (PubMed:22015268).
CC       {ECO:0000269|PubMed:11704639, ECO:0000269|PubMed:12459477,
CC       ECO:0000269|PubMed:22015268, ECO:0000269|PubMed:7911468}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=5072.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11704639};
CC   -!- MASS SPECTROMETRY: Mass=5069.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22015268};
CC   -!- TOXIC DOSE: LD(50) is 0.4 ug/kg by intracerebroventricular injection
CC       into mice. {ECO:0000269|PubMed:7911468}.
CC   -!- MISCELLANEOUS: Has no effect on voltage-gated sodium channel
CC       Nav1.8/SCN10A (in complex with SCN1B).
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; P0C1F4; -.
DR   SMR; P0C1F4; -.
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..48
FT                   /note="Delta-actitoxin-Bgr2a"
FT                   /evidence="ECO:0000269|PubMed:11704639,
FT                   ECO:0000269|PubMed:7911468"
FT                   /id="PRO_0000236030"
FT   SITE            16
FT                   /note="Important for toxicity"
FT   DISULFID        4..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   48 AA;  5078 MW;  84C250EC829A50FA CRC64;
     GASCRCDSDG PTSRGNTLTG TLWLIGRCPS GWHNCRGSGP FIGYCCKQ