TO1D_HADVE
ID TO1D_HADVE Reviewed; 37 AA.
AC P81597;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Omega-hexatoxin-Hv1d {ECO:0000305};
DE Short=Omega-HXTX-Hv1d {ECO:0000305};
DE AltName: Full=Omega-atracotoxin-Hv1d {ECO:0000303|PubMed:10491095};
DE Short=Omega-AcTx-Hv1d {ECO:0000303|PubMed:10491095};
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10491095; DOI=10.1046/j.1432-1327.1999.00646.x;
RA Wang X.-H., Smith R., Fletcher J.I., Wilson H., Wood C.J., Merlin E.H.,
RA King G.F.;
RT "Structure-function studies of omega-atracotoxin, a potent antagonist of
RT insect voltage-gated calcium channels.";
RL Eur. J. Biochem. 264:488-494(1999).
CC -!- FUNCTION: Inhibits insect, but not mammalian, voltage-gated calcium
CC channels (Cav). {ECO:0000250|UniProtKB:P56207}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10491095}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10491095}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P56207}.
CC -!- SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega
CC toxin) subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P81597; -.
DR SMR; P81597; -.
DR ArachnoServer; AS000199; omega-hexatoxin-Hv1d.
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 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.
FT PEPTIDE 1..37
FT /note="Omega-hexatoxin-Hv1d"
FT /evidence="ECO:0000269|PubMed:10491095"
FT /id="PRO_0000044991"
FT SITE 10
FT /note="Critical for insecticidal activity"
FT /evidence="ECO:0000250|UniProtKB:P56207"
FT SITE 27
FT /note="Critical for insecticidal activity"
FT /evidence="ECO:0000250|UniProtKB:P56207"
FT SITE 35
FT /note="Critical for insecticidal activity"
FT /evidence="ECO:0000250|UniProtKB:P56207"
FT DISULFID 4..18
FT /evidence="ECO:0000250|UniProtKB:P56207"
FT DISULFID 11..22
FT /evidence="ECO:0000250|UniProtKB:P56207"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P56207"
SQ SEQUENCE 37 AA; 4071 MW; A105DFFE442EEE2F CRC64;
SPTCIPSGQP CPYNENCCSK SCTYKENENG NTVQRCD