ID   NA19_ANEVI              Reviewed;          83 AA.
AC   B1NWT5;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=U-actitoxin-Avd1g {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Avd1g {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Av9 {ECO:0000303|PubMed:18222944};
DE   AltName: Full=Neurotoxin 9 {ECO:0000312|EMBL:ABW97351.1};
DE   Flags: Precursor;
OS   Anemonia viridis (Snakelocks anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=51769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18222944; DOI=10.1093/molbev/msn021;
RA   Moran Y., Weinberger H., Sullivan J.C., Reitzel A.M., Finnerty J.R.,
RA   Gurevitz M.;
RT   "Concerted evolution of sea anemone neurotoxin genes is revealed through
RT   analysis of the Nematostella vectensis genome.";
RL   Mol. Biol. Evol. 25:737-747(2008).
RN   [2]
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 during signal transduction. Thus it
CC       strongly stimulates mammalian cardiac muscle contraction.
CC       {ECO:0000250|UniProtKB:P01533}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Nematocyst {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
CC   -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC       1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC       {ECO:0000305}.
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DR   EMBL; EU124472; ABW97351.1; -; mRNA.
DR   AlphaFoldDB; B1NWT5; -.
DR   SMR; B1NWT5; -.
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   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000433689"
FT   CHAIN           35..83
FT                   /note="U-actitoxin-Avd1g"
FT                   /id="PRO_5000319679"
FT   DISULFID        40..79
FT                   /evidence="ECO:0000250|UniProtKB:P01533"
FT   DISULFID        42..70
FT                   /evidence="ECO:0000250|UniProtKB:P01533"
FT   DISULFID        63..80
FT                   /evidence="ECO:0000250|UniProtKB:P01533"
SQ   SEQUENCE   83 AA;  8838 MW;  AE3684AA695AB04A CRC64;
     MMNRLLVFLM LGAAFMLVVS AIDQDANDVN MVKRFVSASC LCASDGPTTR GNSLSGTIWL
     FGCPSGWGDC KGRAIAGTCC KRE