ID   TXHP3_HETVE             Reviewed;          31 AA.
AC   P58427;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Kappa-sparatoxin-Hv1c {ECO:0000305};
DE            Short=Kappa-SPRTX-Hv1c {ECO:0000305};
DE   AltName: Full=Heteropodatoxin-3;
DE            Short=HpTX3;
DE   AltName: Full=Toxin AU5C/KJ7;
OS   Heteropoda venatoria (Brown huntsman spider) (Aranea venatoria).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Dionycha; Sparassidae; Heteropoda.
OX   NCBI_TaxID=152925;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT TRP-31, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=9058605;
RA   Sanguinetti M.C., Johnson J.H., Hammerland L.G., Kelbaugh P.R.,
RA   Volkmann R.A., Saccomano N.A., Mueller A.L.;
RT   "Heteropodatoxins: peptides isolated from spider venom that block Kv4.2
RT   potassium channels.";
RL   Mol. Pharmacol. 51:491-498(1997).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RA   Kelbaugh P.R., Saccomano N.A., Volkmann R.A.;
RT   "Calcium channel blocking polypeptides from Heteropoda venatoria.";
RL   Patent number US5627154, 06-MAY-1997.
CC   -!- FUNCTION: Blocks transient outward voltage-gated potassium channels in
CC       rat ventricular myocytes (thus prolonging action-potential duration)
CC       and rat Kv4.2/KCNA4 channels expressed in Xenopus oocytes. Is also a
CC       weak blocker of calcium channels in rat cerebellar granule cells.
CC       {ECO:0000269|PubMed:9058605, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9058605,
CC       ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9058605, ECO:0000305|Ref.2}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P58426}.
CC   -!- MASS SPECTROMETRY: Mass=3599.38; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9058605, ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 20 (HpTX3)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P58427; -.
DR   SMR; P58427; -.
DR   ArachnoServer; AS000346; kappa-sparatoxin-Hv1c.
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:0015459; F:potassium 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   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..31
FT                   /note="Kappa-sparatoxin-Hv1c"
FT                   /evidence="ECO:0000269|PubMed:9058605, ECO:0000269|Ref.2"
FT                   /id="PRO_0000045020"
FT   MOD_RES         31
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000269|PubMed:9058605"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:P58426"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P58426"
FT   DISULFID        15..25
FT                   /evidence="ECO:0000250|UniProtKB:P58426"
SQ   SEQUENCE   31 AA;  3606 MW;  BE2558D2E1053095 CRC64;
     ECGTLFSGCS THADCCEGFI CKLWCRYERT W