ID   KKX14_HETPE             Reviewed;          62 AA.
AC   P0DJ33;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Potassium channel toxin kappa-KTx 1.4 {ECO:0000303|PubMed:22305749};
DE   AltName: Full=HSP009C {ECO:0000303|PubMed:20443192};
DE   Flags: Precursor;
OS   Heterometrus petersii (Asian forest scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC   Heterometrus.
OX   NCBI_TaxID=754296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=20443192; DOI=10.1002/pmic.200900763;
RA   Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.;
RT   "Molecular diversity of toxic components from the scorpion Heterometrus
RT   petersii venom revealed by proteomic and transcriptome analysis.";
RL   Proteomics 10:2471-2485(2010).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22305749; DOI=10.1016/j.bcp.2012.01.021;
RA   Vandendriessche T., Kopljar I., Jenkins D.P., Diego-Garcia E.,
RA   Abdel-Mottaleb Y., Vermassen E., Clynen E., Schoofs L., Wulff H.,
RA   Snyders D., Tytgat J.;
RT   "Purification, molecular cloning and functional characterization of HelaTx1
RT   (Heterometrus laoticus): the first member of a new kappa-KTX subfamily.";
RL   Biochem. Pharmacol. 83:1307-1317(2012).
CC   -!- FUNCTION: Shows structural homology with WaTx suggesting that it acts
CC       as a cell-penetrating peptide (CPP) with defensive purpose that induces
CC       pain by specifically activating mammalian sensory neuron TRPA1 channels
CC       (By similarity). Has no effect on the voltage-gated potassium channels
CC       tested (By similarity). {ECO:0000250|UniProtKB:C0HLG4,
CC       ECO:0000250|UniProtKB:P83655}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20443192}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20443192}.
CC   -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized
CC       by disulfide bonds (CSalpha/alpha 2(S-S)).
CC       {ECO:0000250|UniProtKB:P82851}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor kappa-KTx family. Kappa-KTx 1 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DJ33; -.
DR   TCDB; 8.B.2.1.2; the short scorpion toxin (s-st) superfamily.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012630; Toxin_25.
DR   Pfam; PF08095; Toxin_25; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..38
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416796"
FT   PEPTIDE         40..62
FT                   /note="Potassium channel toxin kappa-KTx 1.4"
FT                   /id="PRO_0000416797"
FT   SITE            44
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:P82851"
FT   SITE            58
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:P82851"
FT   DISULFID        43..61
FT                   /evidence="ECO:0000250|UniProtKB:P82851"
FT   DISULFID        47..57
FT                   /evidence="ECO:0000250|UniProtKB:P82851"
SQ   SEQUENCE   62 AA;  6830 MW;  E00B1534402C6AF2 CRC64;
     MKSCLINVSL LILLLLPILG YASVNAESID GENDFEEERG FGCFRSCWKA GHDDKTCKSM
     CG