TXHP1_HETVE
ID TXHP1_HETVE Reviewed; 33 AA.
AC P58425;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Kappa-sparatoxin-Hv1a {ECO:0000305};
DE Short=Kappa-SPRTX-Hv1a {ECO:0000305};
DE AltName: Full=Heteropodatoxin-1;
DE Short=HpTX1;
DE AltName: Full=Toxin AU3/KJ5;
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 ON POTASSIUM CHANNELS, SUBCELLULAR LOCATION,
RP AMIDATION AT TRP-33, AND 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 ON CALCIUM CHANNELS, SUBCELLULAR LOCATION,
RP DISULFIDE BONDS, AND MASS 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=3910.57; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9058605};
CC -!- MASS SPECTROMETRY: Mass=3909.94; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 21 (HpTx1)
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P58425; -.
DR ArachnoServer; AS000344; kappa-sparatoxin-Hv1a.
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..33
FT /note="Kappa-sparatoxin-Hv1a"
FT /evidence="ECO:0000269|PubMed:9058605, ECO:0000269|Ref.2"
FT /id="PRO_0000045019"
FT MOD_RES 33
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:9058605"
FT DISULFID 2..17
FT /evidence="ECO:0000250|UniProtKB:P58426"
FT DISULFID 9..22
FT /evidence="ECO:0000250|UniProtKB:P58426"
FT DISULFID 16..27
FT /evidence="ECO:0000250|UniProtKB:P58426"
SQ SEQUENCE 33 AA; 3917 MW; 0CBB91832004D0EB CRC64;
DCGTIWHYCG TDQSECCEGW KCSRQLCKYV IDW
