ID   NA12_ANTFU              Reviewed;          48 AA.
AC   P10454;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Delta-actitoxin-Afv1b {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Afv1b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=AFT-II {ECO:0000303|PubMed:15169781, ECO:0000303|PubMed:2883740};
DE            Short=AFII;
OS   Anthopleura fuscoviridis (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anthopleura.
OX   NCBI_TaxID=6111;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC   TISSUE=Nematoblast;
RX   PubMed=2883740; DOI=10.1016/0041-0101(87)90243-1;
RA   Sunahara S., Muramoto K., Tenma K., Kamiya H.;
RT   "Amino acid sequence of two sea anemone toxins from Anthopleura
RT   fuscoviridis.";
RL   Toxicon 25:211-219(1987).
RN   [2]
RP   FUNCTION, MASS SPECTROMETRY, AND TOXIC DOSE.
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       thereby delaying their inactivation. This toxin has a great efficacy
CC       for Nav1.4/SCN4A (EC(50)=30.62 nM) and Nav1.5/SCN5A (EC(50)=62.5 nM).
CC       It is less potent on Nav1.6/SCN8A (EC(50)=about 300 nM), Nav1.1/SCN1A
CC       (EC(50)=390.55 nM), Nav1.3/SCN3A (EC(50)=459.36 nM) and Nav1.2/SCN2A
CC       (EC(50)=1998.00 nM) (when measured as the increase in the slow
CC       component). {ECO:0000269|PubMed:15169781}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Nematocyst.
CC   -!- MASS SPECTROMETRY: Mass=4941; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15169781};
CC   -!- TOXIC DOSE: LD(50) is 450 ug/kg by intraperitoneal injection into mice.
CC       {ECO:0000303|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; B25860; B25860.
DR   AlphaFoldDB; P10454; -.
DR   SMR; P10454; -.
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-Afv1b"
FT                   /evidence="ECO:0000269|PubMed:2883740"
FT                   /id="PRO_0000221519"
FT   DISULFID        5..45
FT                   /evidence="ECO:0000269|PubMed:2883740"
FT   DISULFID        7..35
FT                   /evidence="ECO:0000269|PubMed:2883740"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000269|PubMed:2883740"
SQ   SEQUENCE   48 AA;  4941 MW;  3CD4B66FADA1D999 CRC64;
     GGVPCLCDSD GPSVRGNTLS GIIWLAGCPS GWHNCKAHGP TIGWCCKQ