ID   VSTX3_PARSR             Reviewed;          34 AA.
AC   P0DL74;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Voltage sensor toxin 3 {ECO:0000303|PubMed:24211312};
DE            Short=VSTX3 {ECO:0000303|PubMed:24211312};
DE   AltName: Full=Beta/kappa-theraphotoxin-Gr4a {ECO:0000250|UniProtKB:P0C2P5};
DE            Short=Beta/kappa-TRTX-Gr4a {ECO:0000250|UniProtKB:P0C2P5};
OS   Paraphysa scrofa (Chilean copper tarantula) (Phrixotrichus auratus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Paraphysa.
OX   NCBI_TaxID=269635;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=24211312; DOI=10.1016/j.toxicon.2013.10.029;
RA   Cherki R.S., Kolb E., Langut Y., Tsveyer L., Bajayo N., Meir A.;
RT   "Two tarantula venom peptides as potent and differential Na(V) channels
RT   blockers.";
RL   Toxicon 77:58-67(2014).
CC   -!- FUNCTION: Potent voltage-gated sodium channel blocker (IC(50)=190 nM
CC       and 210 nM on human and rat Nav1.3/SCN3A respectively, 430 nM on human
CC       Nav1.7/SCN9A, 770 nM and 290 nM on human and rat Nav1.8/SCN10A
CC       respectively) (PubMed:24211312). Binds the voltage-sensor domain of the
CC       potassium channel KvAP (from Aeropyrum pernix) and weakly inhibits this
CC       channel (By similarity). {ECO:0000250|UniProtKB:P0C2P5,
CC       ECO:0000269|PubMed:24211312}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24211312}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24211312}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=4168.0; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:24211312};
CC   -!- MISCELLANEOUS: Shows only a very weak inhibition on human Nav1.5/SCN5A.
CC       {ECO:0000269|PubMed:24211312}.
CC   -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC       to that of VSTX3 from Grammostola rosea (AC P0C2P5). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 61 (VSTX3)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL74; -.
DR   SMR; P0DL74; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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   InterPro; IPR013140; Huwentoxin_CS1.
DR   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..34
FT                   /note="Voltage sensor toxin 3"
FT                   /evidence="ECO:0000269|PubMed:24211312"
FT                   /id="PRO_0000442000"
FT   DISULFID        2..17
FT                   /evidence="ECO:0000250|UniProtKB:P0DL72"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250|UniProtKB:P0DL72"
FT   DISULFID        16..29
FT                   /evidence="ECO:0000250|UniProtKB:P0DL72"
SQ   SEQUENCE   34 AA;  4178 MW;  BE2D51E87DF93738 CRC64;
     DCLGWFKGCD PDNDKCCEGY KCNRRDKWCK YKLW