NA13_BUNCI
ID NA13_BUNCI Reviewed; 48 AA.
AC Q7M425;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Delta-actitoxin-Bcs1a {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Bcs1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Bc-III {ECO:0000303|PubMed:15169781};
DE AltName: Full=Major neurotoxin BcIII {ECO:0000303|PubMed:8105563};
OS Bunodosoma caissarum (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Bunodosoma.
OX NCBI_TaxID=31165;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Nematoblast;
RX PubMed=8105563; DOI=10.1016/0041-0101(93)90220-d;
RA Malpezzi E.L.A., de Freitas J.C., Muramoto K., Kamiya H.;
RT "Characterization of peptides in sea anemone venom collected by a novel
RT procedure.";
RL Toxicon 31:853-864(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-25, TOXIC DOSE, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=15169781; DOI=10.1074/jbc.m404344200;
RA Oliveira J.S., Redaelli E., Zaharenko A.J., Cassulini R.R., Konno K.,
RA Pimenta D.C., Freitas J.C., Clare J.J., Wanke E.;
RT "Binding specificity of sea anemone toxins to Nav 1.1-1.6 sodium channels:
RT unexpected contributions from differences in the IV/S3-S4 outer loop.";
RL J. Biol. Chem. 279:33323-33335(2004).
RN [3]
RP ERRATUM OF PUBMED:15169781.
RA Oliveira J.S., Redaelli E., Zaharenko A.J., Cassulini R.R., Konno K.,
RA Pimenta D.C., Freitas J.C., Clare J.J., Wanke E.;
RL J. Biol. Chem. 279:44229-44230(2004).
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 specifically to voltage-gated sodium channels (Nav)
CC (site 3), thereby delaying their inactivation. This toxin has moderate
CC activity on Nav1.1/SCN1A (EC(50)=about 300 nM) and Nav1.5/SCN5A
CC (EC(50)=307.00 nM). It less potent on Nav1.4/SCN4A (EC(50)=820.84 nM),
CC Nav1.6/SCN8A (EC(50)=about 900 nM), Nav1.2/SCN2A (EC(50)=1449.17 nM)
CC and Nav1.3/SCN3A (EC(50)=1458.42 nM) (when measured as the increase in
CC the slow component). {ECO:0000269|PubMed:15169781}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8105563}. Nematocyst
CC {ECO:0000269|PubMed:8105563}.
CC -!- MASS SPECTROMETRY: Mass=4976; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15169781};
CC -!- TOXIC DOSE: LD(50) is 600 ug/kg by intraperitoneal injection into mice.
CC {ECO:0000269|PubMed:15169781}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. Type I subfamily. {ECO:0000305}.
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DR PIR; A37435; A37435.
DR AlphaFoldDB; Q7M425; -.
DR SMR; Q7M425; -.
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-Bcs1a"
FT /evidence="ECO:0000269|PubMed:15169781,
FT ECO:0000269|PubMed:8105563"
FT /id="PRO_0000221521"
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; 4979 MW; A9CD00EC8296F426 CRC64;
GVACRCDSDG PTSRGNTLTG TLWLTGGCPS GWHNCRGSGP FIGYCCKK