ID   NA1B_BUNCN              Reviewed;          48 AA.
AC   P0C7P9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Delta-actitoxin-Bcg1b {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Bcg1b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Cangitoxin II {ECO:0000303|PubMed:18342901};
DE   AltName: Full=Cangitoxin-2 {ECO:0000305};
DE   AltName: Full=Cangitoxin-II;
DE            Short=CGTX-II {ECO:0000303|PubMed:18342901};
OS   Bunodosoma cangicum (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Bunodosoma.
OX   NCBI_TaxID=138296;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Nematoblast;
RX   PubMed=18342901; DOI=10.1016/j.toxicon.2008.01.011;
RA   Zaharenko A.J., Ferreira W.A. Jr., de Oliveira J.S., Konno K.,
RA   Richardson M., Schiavon E., Wanke E., de Freitas J.C.;
RT   "Revisiting cangitoxin, a sea anemone peptide: purification and
RT   characterization of cangitoxins II and III from the venom of Bunodosoma
RT   cangicum.";
RL   Toxicon 51:1303-1307(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=21802465; DOI=10.1016/j.peptides.2011.07.008;
RA   Zaharenko A.J., Schiavon E., Ferreira W.A. Jr., Lecchi M., de Freitas J.C.,
RA   Richardson M., Wanke E.;
RT   "Characterization of selectivity and pharmacophores of type 1 sea anemone
RT   toxins by screening seven Na(v) sodium channel isoforms.";
RL   Peptides 34:158-167(2012).
RN   [3]
RP   REVIEW.
RX   PubMed=19393679; DOI=10.1016/j.toxicon.2009.04.018;
RA   Wanke E., Zaharenko A.J., Redaelli E., Schiavon E.;
RT   "Actions of sea anemone type 1 neurotoxins on voltage-gated sodium channel
RT   isoforms.";
RL   Toxicon 54:1102-1111(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: Binds to the sodium channels Nav1.1/SCN1A (EC(50)=165 nM),
CC       Nav1.5/SCN5A (EC(50)=103 nM) and Nav1.6/SCN8A (EC(50)=133 nM), thereby
CC       delaying their inactivation (PubMed:18342901, PubMed:21802465). Also
CC       inhibits Nav1.2/SCN2A, Nav1.3/SCN3A, and Nav1.4/SCN4A, but to a lesser
CC       extent (PubMed:21802465). Inhibits Nav1.5 differently from isoforms
CC       Nav1.1 and Nav1.6. In Nav1.5 the effect consists in a right-shift of
CC       inactivation; whereas in both Nav1.1 and Nav1.6 the effect consists in
CC       an incomplete inactivation (PubMed:21802465).
CC       {ECO:0000269|PubMed:18342901}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18342901}.
CC       Nematocyst {ECO:0000269|PubMed:18342901}.
CC   -!- MASS SPECTROMETRY: Mass=4958.09; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18342901};
CC   -!- MISCELLANEOUS: Does not show activity on Nav1.7/SCN9A.
CC       {ECO:0000269|PubMed:21802465}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C7P9; -.
DR   SMR; P0C7P9; -.
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-Bcg1b"
FT                   /evidence="ECO:0000269|PubMed:18342901"
FT                   /id="PRO_0000342623"
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;  4964 MW;  E686F00B85E1F456 CRC64;
     GVACRCDSDG PTVRGDSLSG TLWLTGGCPS GWHNCRGSGP FIGYCCKK