ID   TO1A_HADVN              Reviewed;          83 AA.
AC   S0F1M4;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Omega-hexatoxin-Hvn1a {ECO:0000303|PubMed:24593665};
DE   Flags: Precursor;
OS   Hadronyche venenata (Tasmanian funnel-web spider) (Atrax venenatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=1337083;
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: Inhibits insect, but not mammalian, voltage-gated calcium
CC       channels (Cav). {ECO:0000250|UniProtKB:P56207}.
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   -!- SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega
CC       toxin) subfamily. {ECO:0000303|PubMed:24593665}.
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DR   EMBL; HG001285; CDF44146.1; -; mRNA.
DR   AlphaFoldDB; S0F1M4; -.
DR   SMR; S0F1M4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   InterPro; IPR009415; Omega-atracotox.
DR   InterPro; IPR018071; Omega-atracotox_CS.
DR   Pfam; PF06357; Omega-toxin; 1.
DR   PROSITE; PS60016; OMEGA_ACTX_1; 1.
PE   3: Inferred from homology;
KW   Calcium channel impairing toxin; Cleavage on pair of basic residues;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Signal;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000430910"
FT   CHAIN           47..83
FT                   /note="Omega-hexatoxin-Hvn1a"
FT                   /id="PRO_0000430911"
FT   DISULFID        50..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..82
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  8983 MW;  A880A012531C2C5B CRC64;
     MNTATGVIAL LVLATVIGCI EAETRADLQG AFESYEGEAA EKIFRRSPTC IPSGQPCPYN
     ENCCSKSCTY KEMKTATPVQ RCD