NA1D_BUNCN
ID NA1D_BUNCN Reviewed; 47 AA.
AC P86459; P86460;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Delta-actitoxin-Bcg1d {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Bcg1d {ECO:0000303|PubMed:22683676};
DE AltName: Full=Delta-AITX-Bcg1a {ECO:0000303|Ref.1};
DE AltName: Full=Delta-AITX-Bcg1b {ECO:0000303|Ref.1};
DE AltName: Full=Delta-actitoxin-Bcg1e {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Bcg1e {ECO:0000303|PubMed:22683676};
DE AltName: Full=Toxin Bcg 30.24 {ECO:0000303|PubMed:20483220};
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, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RA Zaharenko A.J., Schiavon E., Ferreira W.A. Jr., Freitas J.C.,
RA Richardson M., Wanke E.;
RL Submitted (FEB-2010) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
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 PROTEIN SEQUENCE OF 1-39, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20483220; DOI=10.1016/j.cbd.2008.04.002;
RA Zaharenko A.J., Ferreira W.A. Jr., Oliveira J.S., Richardson M.,
RA Pimenta D.C., Konno K., Portaro F.C., de Freitas J.C.;
RT "Proteomics of the neurotoxic fraction from the sea anemone Bunodosoma
RT cangicum venom: novel peptides belonging to new classes of toxins.";
RL Comp. Biochem. Physiol. 3D:219-225(2008).
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)=453 nM),
CC Nav1.5/SCN5A (EC(50)=440 nM) and Nav1.6/SCN8A (EC(50)=1740 nM), thereby
CC delaying their inactivation (Ref.1, PubMed:21802465). Also inhibits
CC Nav1.2/SCN2A, Nav1.3/SCN3A, and Nav1.4/SCN4A, but to a lesser extent
CC (PubMed:21802465). Toxin effect on Nav1.1 and Nav1.6 (and on Nav1.5,
CC but in a lesser extent) consists in an incomplete inactivation
CC (PubMed:21802465). {ECO:0000269|PubMed:20483220,
CC ECO:0000269|PubMed:21802465, ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20483220}.
CC Nematocyst {ECO:0000305|PubMed:20483220}.
CC -!- MASS SPECTROMETRY: Mass=4781.32; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
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:0000255}.
CC -!- CAUTION: The sequence submitted as delta-AITX-Bcg1b (AC P86460) and
CC renamed delta-AITX-Bcg1e is a deamidation product (at Asn-16 residue)
CC of delta-AITX-Bcg1a (renamed delta-AITX-Bcg1d). This product does not
CC show any activity on all Nav1 tested (Nav1.1 to Nav1.7).
CC {ECO:0000269|PubMed:21802465}.
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; P86459; -.
DR SMR; P86459; -.
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..47
FT /note="Delta-actitoxin-Bcg1d"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000392961"
FT SITE 16
FT /note="Important for toxin activity on Nav channels"
FT /evidence="ECO:0000305|PubMed:21802465"
FT DISULFID 4..44
FT /evidence="ECO:0000250|UniProtKB:P01530"
FT DISULFID 6..34
FT /evidence="ECO:0000250|UniProtKB:P01530"
FT DISULFID 27..45
FT /evidence="ECO:0000250|UniProtKB:P01530"
FT CONFLICT 16
FT /note="N -> D (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305|PubMed:21802465"
SQ SEQUENCE 47 AA; 4786 MW; 794B4D2BA4C2DA00 CRC64;
GVPCLCDSDG PSVRGNTLSG TVWVFGCPSG WHICTSDGPT IGSCCKK
