ID   KAX38_HOTTS             Reviewed;          38 AA.
AC   P59886;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.8;
DE   AltName: Full=Charybdotoxin-like peptide Bs 6 {ECO:0000303|PubMed:10048185};
DE            Short=Bs6 {ECO:0000303|PubMed:10048185};
OS   Hottentotta tamulus sindicus (Scorpion) (Buthus sindicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=42519;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10048185; DOI=10.1016/s1095-6433(98)10140-x;
RA   Ali S.A., Stoeva S., Schuetz J., Kayed R., Abbasi A., Zaidi Z.H.,
RA   Voelter W.;
RT   "Purification and primary structure of low molecular mass peptides from
RT   scorpion (Buthus sindicus) venom.";
RL   Comp. Biochem. Physiol. 121A:323-332(1998).
CC   -!- FUNCTION: Potassium channel inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10048185}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:10048185}.
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=4121.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10048185};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 03 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P59886; -.
DR   SMR; P59886; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   PRINTS; PR00286; CHARYBDTOXIN.
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.
FT   PEPTIDE         1..38
FT                   /note="Potassium channel toxin alpha-KTx 3.8"
FT                   /evidence="ECO:0000269|PubMed:10048185"
FT                   /id="PRO_0000044900"
FT   REGION          26..33
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   38 AA;  4122 MW;  1F2505014F8D2174 CRC64;
     GVPINVKCRG SPQCIQPCRD AGMRFGKCMN GKCHCTPQ