ID   TX482_HYSGI             Reviewed;          41 AA.
AC   P56854;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Omega-theraphotoxin-Hg1a;
DE            Short=Omega-TRTX-Hg1a;
DE   AltName: Full=Toxin SNX-482;
DE            Short=SNX482;
OS   Hysterocrates gigas (Cameroon red baboon tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Hysterocrates.
OX   NCBI_TaxID=118972;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9799496; DOI=10.1021/bi981255g;
RA   Newcomb R., Szoke B., Palma A., Wang G., Chen X.H., Hopkins W., Cong R.,
RA   Miller J., Urge L., Tarczy-Hornoch K., Loo J.A., Dooley D.J., Nadasdi L.,
RA   Tsien R.W., Lemos J., Miljanich G.;
RT   "Selective peptide antagonist of the class E calcium channel from the venom
RT   of the tarantula Hysterocrates gigas.";
RL   Biochemistry 37:15353-15362(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=11423396; DOI=10.1016/s0006-3495(01)75681-0;
RA   Bourinet E., Stotz S.C., Spaetgens R.L., Dayanithi G., Lemos J.,
RA   Nargeot J., Zamponi G.W.;
RT   "Interaction of SNX482 with domains III and IV inhibits activation gating
RT   of alpha(1E) (Ca(V)2.3) calcium channels.";
RL   Biophys. J. 81:79-88(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=12954354; DOI=10.1016/s0014-2999(03)02084-3;
RA   Arroyo G., Aldea M., Fuentealba J., Albillos A., Garcia A.G.;
RT   "SNX482 selectively blocks P/Q Ca2+ channels and delays the inactivation of
RT   Na+ channels of chromaffin cells.";
RL   Eur. J. Pharmacol. 475:11-18(2003).
CC   -!- FUNCTION: Toxin that blocks vertebrate P/Q-type (Cav2.1/CACNA1A) and R-
CC       type (Cav2.3/CACNA1E) voltage-gated calcium channels. Also inhibits
CC       sodium channels (Nav) in bovine chromaffin cells by delaying sodium
CC       channel inactivation. {ECO:0000269|PubMed:11423396,
CC       ECO:0000269|PubMed:12954354, ECO:0000269|PubMed:9799496}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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 10 (Hwtx-1) family. 56 (SNX-482)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P56854; -.
DR   SMR; P56854; -.
DR   ArachnoServer; AS000281; omega-theraphotoxin-Hg1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011696; Huwentoxin-1.
DR   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..41
FT                   /note="Omega-theraphotoxin-Hg1a"
FT                   /id="PRO_0000087673"
FT   DISULFID        7..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000250"
FT   DISULFID        20..33
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   41 AA;  4501 MW;  C5D3CC96D3A0CFF4 CRC64;
     GVDKAGCRYM FGGCSVNDDC CPRLGCHSLF SYCAWDLTFS D