ID   TOT2A_HADVE             Reviewed;          45 AA.
AC   P82852;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Omega-hexatoxin-Hv2a;
DE            Short=Omega-HXTX-Hv2a;
DE   AltName: Full=Omega-atracotoxin-Hv2a;
DE            Short=AcTx-Hv2;
DE            Short=Omega-AcTx-Hv2a;
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   PROTEIN SEQUENCE, STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=11522785; DOI=10.1074/jbc.m105206200;
RA   Wang X.-H., Connor M., Wilson D., Wilson H.I., Nicholson G.M., Smith R.,
RA   Shaw D., Mackay J.P., Alewood P.F., Christie M.J., King G.F.;
RT   "Discovery and structure of a potent and highly specific blocker of insect
RT   calcium channels.";
RL   J. Biol. Chem. 276:40306-40312(2001).
RN   [2]
RP   FUNCTION.
RX   PubMed=16330063; DOI=10.1016/j.toxicon.2005.10.011;
RA   Mukherjee A.K., Sollod B.L., Wikel S.K., King G.F.;
RT   "Orally active acaricidal peptide toxins from spider venom.";
RL   Toxicon 47:182-187(2006).
CC   -!- FUNCTION: Potent inhibitor of insect (bee brain), but not mammalian
CC       (rat trigeminal neurons), voltage-gated calcium channels (Cav). As for
CC       omega-AcTx-Hv1a, the phenotypic effect of injection of this toxin into
CC       lone star ticks (Amblyomma americanum) is curling of all eight legs
CC       into closed loops, followed by death. {ECO:0000269|PubMed:16330063}.
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.
CC   -!- SIMILARITY: Belongs to the neurotoxin 15 family. 02 (omega-actx)
CC       subfamily. {ECO:0000305}.
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DR   PDB; 1G9P; NMR; -; A=1-45.
DR   PDB; 1HP3; NMR; -; A=1-32.
DR   PDBsum; 1G9P; -.
DR   PDBsum; 1HP3; -.
DR   AlphaFoldDB; P82852; -.
DR   SMR; P82852; -.
DR   ArachnoServer; AS000204; omega-hexatoxin-Hv2a.
DR   EvolutionaryTrace; P82852; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IDA:CACAO.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013139; Omega_atracotoxin_CS2.
DR   InterPro; IPR012628; Toxin_23.
DR   Pfam; PF08093; Toxin_23; 1.
DR   PROSITE; PS60017; OMEGA_ACTX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   CHAIN           1..45
FT                   /note="Omega-hexatoxin-Hv2a"
FT                   /id="PRO_0000087669"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000269|PubMed:11522785"
FT   DISULFID        11..24
FT                   /evidence="ECO:0000269|PubMed:11522785"
FT   DISULFID        17..29
FT                   /evidence="ECO:0000269|PubMed:11522785"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:1G9P"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:1G9P"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:1G9P"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1G9P"
SQ   SEQUENCE   45 AA;  4484 MW;  D9D25DC007A129B7 CRC64;
     LLACLFGNGR CSSNRDCCEL TPVCKRGSCV SSGPGLVGGI LGGIL