NA13_BUNGR
ID NA13_BUNGR Reviewed; 48 AA.
AC P0C1F5;
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-Bgr2b {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Bgr2b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Bg III {ECO:0000303|PubMed:7911468};
DE Short=BgIII;
DE AltName: Full=Neurotoxin Bg-3;
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 MASS SPECTROMETRY, AND FUNCTION.
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. Has effect on SCN4A/SCN1B, and
CC SCN5A/SCN1B, has no effect on SCN2A/SCN1B, and SCN10A/SCN1B. Possesses
CC the highest efficacy for the insect sodium channel para/tipE. Also
CC interacts with sodium channels in cardiac cells. Shows lethality to
CC crabs (PubMed:22015268). {ECO:0000269|PubMed:11704639,
CC ECO:0000269|PubMed:12459477, ECO:0000269|PubMed:7911468}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=5073.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11704639};
CC -!- MASS SPECTROMETRY: Mass=5072.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22015268};
CC -!- TOXIC DOSE: LD(50) is 21 ug/kg by intracerebroventricular injection
CC into mice. {ECO:0000269|PubMed:7911468}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. Type I subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C1F5; -.
DR SMR; P0C1F5; -.
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-Bgr2b"
FT /evidence="ECO:0000269|PubMed:11704639,
FT ECO:0000269|PubMed:7911468"
FT /id="PRO_0000236031"
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; 5079 MW; 8ACCB00C829A50FA CRC64;
GASCRCDSDG PTSRGDTLTG TLWLIGRCPS GWHNCRGSGP FIGYCCKQ