ID   TOK1G_HADVE             Reviewed;          76 AA.
AC   S0F207;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Omega/kappa-hexatoxin-Hv1g {ECO:0000303|PubMed:24593665};
DE   Flags: Precursor;
OS   Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=6904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24593665; DOI=10.1186/1471-2164-15-177;
RA   Pineda S.S., Sollod B.L., Wilson D., Darling A., Sunagar K., Undheim E.A.,
RA   Kely L., Antunes A., Fry B.G., King G.F.;
RT   "Diversification of a single ancestral gene into a successful toxin
RT   superfamily in highly venomous Australian funnel-web spiders.";
RL   BMC Genomics 15:177-177(2014).
CC   -!- FUNCTION: Toxin that may inhibit ion channels. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24593665}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24593665}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Several paralogs that code for the same precursor are
CC       shown in this entry, whereas other paralogs that code for the same
CC       mature protein are shown in AC S0F214, AC S0F208, and AC S0F1N5.
CC       {ECO:0000305|PubMed:24593665}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 02
CC       (omega/kappa toxin) subfamily. {ECO:0000305}.
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DR   EMBL; HG001298; CDF44159.1; -; mRNA.
DR   EMBL; HG001299; CDF44160.1; -; mRNA.
DR   EMBL; HG001300; CDF44161.1; -; mRNA.
DR   EMBL; HG001301; CDF44162.1; -; mRNA.
DR   AlphaFoldDB; S0F207; -.
DR   SMR; S0F207; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..35
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000430898"
FT   CHAIN           38..76
FT                   /note="Omega/kappa-hexatoxin-Hv1g"
FT                   /id="PRO_0000430899"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..74
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   76 AA;  8373 MW;  1A30EFB457BE6CDF CRC64;
     MNTATGFIVL LVLATVLGGI EAGESHMRKD AMGRVRRQYC VPVDQPCSLN TQPCCDDATC
     TQELNENDNT VYYCRA