ID   KKX29_PANIM             Reviewed;          28 AA.
AC   C0HKB3;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Potassium channel toxin kappa-KTx 2.9 {ECO:0000303|PubMed:28502745};
DE   AltName: Full=Potassium channel-blocking toxin 6 {ECO:0000303|PubMed:28502745};
DE            Short=Pi6 {ECO:0000303|PubMed:28502745};
OS   Pandinus imperator (Emperor scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX   NCBI_TaxID=55084 {ECO:0000303|PubMed:28502745};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, PRESENCE OF DISULFIDE
RP   BONDS, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:28502745};
RX   PubMed=28502745; DOI=10.1016/j.toxicon.2017.05.011;
RA   Olamendi-Portugal T., Csoti A., Jimenez-Vargas J.M., Gomez-Lagunas F.,
RA   Panyi G., Possani L.D.;
RT   "Pi5 and Pi6, two undescribed peptides from the venom of the scorpion
RT   Pandinus imperator and their effects on K(+)-channels.";
RL   Toxicon 133:136-144(2017).
CC   -!- FUNCTION: Reversibly blocks voltage-gated potassium channels
CC       Kv1.2/KCNA2 and Kv1.3/KCNA3. {ECO:0000269|PubMed:28502745}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28502745}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:28502745}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000269|PubMed:28502745}.
CC   -!- MASS SPECTROMETRY: Mass=3126.5; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:28502745};
CC   -!- MISCELLANEOUS: Does not inhibit voltage-gated potassium channels Shaker
CC       B, Shab, Kv1.1/KCNA1 and Kv1.4/KCNA4. {ECO:0000269|PubMed:28502745}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Gamma-KTx 2 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKB3; -.
DR   SMR; C0HKB3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..28
FT                   /note="Potassium channel toxin kappa-KTx 2.9"
FT                   /evidence="ECO:0000269|PubMed:28502745"
FT                   /id="PRO_0000444166"
FT   DISULFID        4..22
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z3"
FT   DISULFID        8..18
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z3"
SQ   SEQUENCE   28 AA;  3131 MW;  69CBD5B340915A6A CRC64;
     VDACYEACMH HHMNSDDCIE ACKNPVPP