ID   KA192_BUTOC             Reviewed;          31 AA.
AC   C0HJQ2;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Potassium channel toxin alpha-KTx 19.2 {ECO:0000303|PubMed:26398235};
DE   AltName: Full=Toxin Kbot21 {ECO:0000303|PubMed:26398235};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871 {ECO:0000303|PubMed:26398235};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC   TISSUE=Venom {ECO:0000303|PubMed:26398235};
RX   PubMed=26398235; DOI=10.1371/journal.pone.0137611;
RA   ElFessi-Magouri R., Peigneur S., Othman H., Srairi-Abid N., ElAyeb M.,
RA   Tytgat J., Kharrat R.;
RT   "Characterization of Kbot21 Reveals Novel Side Chain Interactions of
RT   Scorpion Toxins Inhibiting Voltage-Gated Potassium Channels.";
RL   PLoS ONE 10:E0137611-E0137611(2015).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY.
RA   ElFessi-Magouri R., Peigneur S., Othman H., Srairi-Abid N., ElAyeb M.,
RA   Tytgat J., Kharrat R.;
RL   Submitted (DEC-2014) to UniProtKB.
CC   -!- FUNCTION: Blocks voltage-gated potassium channels rKv1.1/KCNA1,
CC       rKv1.2/KCNA2, hKv1.3/KCNA3, rKv1.6/KCNA6 (IC(50)=75.9 nM) and, to a
CC       lesser extent, Shaker IR (with the inactivation domain removed).
CC       {ECO:0000269|PubMed:26398235}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26398235}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26398235}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26398235}.
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   -!- MASS SPECTROMETRY: Mass=3383; Mass_error=0.17; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- TOXIC DOSE: LD(50) is 1 ug/kg by intracerebro-ventricular injection in
CC       mice. {ECO:0000269|PubMed:26398235}.
CC   -!- MISCELLANEOUS: Does not block voltage-gated potassium channels
CC       rKv1.4/KCNA4 and rKv2.1/KCNB1. {ECO:0000269|PubMed:26398235}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 19 subfamily.
CC       {ECO:0000303|PubMed:26398235}.
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DR   AlphaFoldDB; C0HJQ2; -.
DR   SMR; C0HJQ2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044361; P:negative regulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..31
FT                   /note="Potassium channel toxin alpha-KTx 19.2"
FT                   /evidence="ECO:0000269|PubMed:26398235"
FT                   /id="PRO_0000440689"
FT   SITE            21
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   SITE            30
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        8..27
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        12..29
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
SQ   SEQUENCE   31 AA;  3400 MW;  7F13B190790746FF CRC64;
     AACYSSDCRV KCRAMGFSSG KCIDSKCKCY K