ID   KA165_LEIHE             Reviewed;          36 AA.
AC   P45660;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Potassium channel toxin alpha-KTx 16.5;
DE   AltName: Full=Lqh 15-1;
DE   AltName: Full=Toxin 15-1;
DE   AltName: Full=alpha-KTx 1.7;
OS   Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus
OS   hebraeus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX   NCBI_TaxID=6884;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=7533951; DOI=10.1016/0041-0101(94)90415-4;
RA   Marshall D.L., Vatanpour H., Harvey A.L., Boyot P., Pinkasfeld S.,
RA   Doljansky Y., Bouet F., Menez A.;
RT   "Neuromuscular effects of some potassium channel blocking toxins from the
RT   venom of the scorpion Leiurus quinquestriatus hebreus.";
RL   Toxicon 32:1433-1443(1994).
CC   -!- FUNCTION: Augments responses to direct muscle stimulation probably by
CC       blocking calcium-activated potassium channels.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 16 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P45660; -.
DR   SMR; P45660; -.
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   Calcium-activated potassium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin.
FT   PEPTIDE         1..36
FT                   /note="Potassium channel toxin alpha-KTx 16.5"
FT                   /id="PRO_0000044893"
FT   REGION          26..33
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="ECO:0000255"
FT   SITE            27
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            36
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   36 AA;  4144 MW;  11866427AA00C467 CRC64;
     GLIDVRCYDS RQCWIACKKV TGSTQGKCQN KQCRCY