ID   KAX6F_HEMLE             Reviewed;          35 AA.
AC   P85528;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.15 {ECO:0000303|PubMed:18699777};
DE   AltName: Full=Hemitoxin {ECO:0000303|PubMed:18699777};
OS   Hemiscorpius lepturus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae.
OX   NCBI_TaxID=520031;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TOXIC DOSE, MASS
RP   SPECTROMETRY, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=18699777; DOI=10.1111/j.1742-4658.2008.06607.x;
RA   Srairi-Abid N., Shahbazzadeh D., Chatti I., Mlayah-Bellalouna S.,
RA   Mejdoub H., Borchani L., Benkhalifa R., Akbari A., El Ayeb M.;
RT   "Hemitoxin, the first potassium channel toxin from the venom of the Iranian
RT   scorpion Hemiscorpius lepturus.";
RL   FEBS J. 275:4641-4650(2008).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels rKv1.1/KCNA1
CC       (IC(50)=13 nM), rKv1.2/KCNA2 (IC(50)=16 nM) and rKv1.3/KCNA3 (IC(50)=2
CC       nM). {ECO:0000269|PubMed:18699777}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18699777}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18699777}.
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=3899.24; Mass_error=0.67; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18699777};
CC   -!- TOXIC DOSE: LD(50) is 15 ug/kg by intracerebroventricular injection
CC       into C57BL mice. {ECO:0000269|PubMed:18699777}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85528; -.
DR   SMR; P85528; -.
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; IDA:UniProtKB.
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   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;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..35
FT                   /note="Potassium channel toxin alpha-KTx 6.15"
FT                   /evidence="ECO:0000269|PubMed:18699777"
FT                   /id="PRO_0000341448"
FT   SITE            23
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   SITE            32
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000269|PubMed:18699777"
FT   DISULFID        9..29
FT                   /evidence="ECO:0000269|PubMed:18699777"
FT   DISULFID        13..31
FT                   /evidence="ECO:0000269|PubMed:18699777"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000269|PubMed:18699777"
SQ   SEQUENCE   35 AA;  3906 MW;  7BF0C33C1232F457 CRC64;
     IKCTLSKDCY SPCKKETGCP RAKCINRNCK CYGCS