ID   TO1D_HADMO              Reviewed;          84 AA.
AC   P0DMQ3;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Omega-hexatoxin-Hmo1d {ECO:0000303|PubMed:24593665};
DE   Flags: Precursor;
OS   Hadronyche modesta (Victorian funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=1337084;
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}.
CC   -!- CAUTION: Signal and propeptide sequences are imported from
CC       ArachnoServer. The sequence differences may reflect different paralogs.
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DR   AlphaFoldDB; P0DMQ3; -.
DR   SMR; P0DMQ3; -.
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.
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..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000430920"
FT   CHAIN           48..84
FT                   /note="Omega-hexatoxin-Hmo1d"
FT                   /id="PRO_0000430921"
FT   DISULFID        51..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..83
FT                   /evidence="ECO:0000250"
FT   CONFLICT        19
FT                   /note="C -> F (in Ref. 1)"
FT   CONFLICT        21
FT                   /note="Q -> E (in Ref. 1)"
FT   CONFLICT        24
FT                   /note="D -> N (in Ref. 1)"
FT   CONFLICT        26
FT                   /note="M -> R (in Ref. 1)"
FT   CONFLICT        37
FT                   /note="D -> E (in Ref. 1)"
FT   CONFLICT        42
FT                   /note="K -> E (in Ref. 1)"
FT   CONFLICT        43
FT                   /note="R -> K (in Ref. 1)"
SQ   SEQUENCE   84 AA;  9021 MW;  99C76281D747F849 CRC64;
     MNTATGVIAL LVLATVIGCI QAEDTMADLQ GGFESYDGEA AKRIFRRSPV CIPSGQPCPY
     NEHCCSGSCT YKENENGNTV QRCD