ID   KA241_PANIM             Reviewed;          33 AA.
AC   C0HKB2;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Potassium channel toxin alpha-KTx 24.1 {ECO:0000303|PubMed:28502745};
DE   AltName: Full=Potassium channel-blocking toxin 5 {ECO:0000303|PubMed:28502745};
DE            Short=Pi5 {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]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, PRESENCE OF DISULFIDE
RP   BONDS, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
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, Kv1.3/KCNA3 and, weakly, Shaker B.
CC       {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   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:28502745}.
CC   -!- MASS SPECTROMETRY: Mass=3334.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:28502745};
CC   -!- MISCELLANEOUS: Does not inhibit voltage-gated potassium channels Shab,
CC       Kv1.2/KCNA1 and Kv1.4/KCNA4. {ECO:0000269|PubMed:28502745}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 24 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKB2; -.
DR   SMR; C0HKB2; -.
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..33
FT                   /note="Potassium channel toxin alpha-KTx 24.1"
FT                   /evidence="ECO:0000269|PubMed:28502745"
FT                   /id="PRO_0000444165"
FT   DISULFID        4..23
FT                   /evidence="ECO:0000250|UniProtKB:P58498"
FT   DISULFID        9..28
FT                   /evidence="ECO:0000250|UniProtKB:P58498"
FT   DISULFID        13..30
FT                   /evidence="ECO:0000250|UniProtKB:P58498"
FT   DISULFID        18..33
FT                   /evidence="ECO:0000250|UniProtKB:P58498"
SQ   SEQUENCE   33 AA;  3343 MW;  5C900E6DA90DE3F6 CRC64;
     VAKCSTSECG HACQQAGCRN SGCRYGSCIC VGC