ID   KKX27_HETPE             Reviewed;          65 AA.
AC   P0DJ34;
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 2.7 {ECO:0000303|PubMed:22305749};
DE   AltName: Full=HSP053C.1 {ECO:0000303|PubMed:20443192};
DE   AltName: Full=Toxin HeTx203 {ECO:0000303|PubMed:22511981, ECO:0000303|PubMed:23573241};
DE   AltName: Full=Toxin kappa-KTx 2.6 {ECO:0000303|PubMed:22511981, ECO:0000303|PubMed:23573241};
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
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   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=22511981; DOI=10.1371/journal.pone.0035154;
RA   Chen Z.Y., Zeng D.Y., Hu Y.T., He Y.W., Pan N., Ding J.P., Cao Z.J.,
RA   Liu M.L., Li W.X., Yi H., Jiang L., Wu Y.L.;
RT   "Structural and functional diversity of acidic scorpion potassium channel
RT   toxins.";
RL   PLoS ONE 7:E35154-E35154(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=23573241; DOI=10.1371/journal.pone.0060201;
RA   Chen Z., Luo F., Feng J., Yang W., Zeng D., Zhao R., Cao Z., Liu M., Li W.,
RA   Jiang L., Wu Y.;
RT   "Genomic and structural characterization of Kunitz-type peptide LmKTT-1a
RT   highlights diversity and evolution of scorpion potassium channel toxins.";
RL   PLoS ONE 8:E60201-E60201(2013).
RN   [4]
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: Weakly inhibits the Kv7.1/KCNQ1 channel (10 uM of the toxin
CC       inhibits currents by 17.8%). {ECO:0000269|PubMed:22511981}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|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:P0C1Z3}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor kappa-KTx family. Kappa-KTx 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FD664203; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DJ34; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..39
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416798"
FT   PEPTIDE         42..64
FT                   /note="Potassium channel toxin kappa-KTx 2.7"
FT                   /id="PRO_0000416799"
FT   DISULFID        45..63
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z3"
FT   DISULFID        49..59
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z3"
SQ   SEQUENCE   65 AA;  7142 MW;  9315EB6EFC772BA1 CRC64;
     MKTSGTVYVF LLLLAFGIFT DISSACSEQM DDEDSYEVEK RGNACIEVCL QHTGNPAECD
     KACDK