ID   KAX33_LEIHE             Reviewed;          38 AA.
AC   P46112;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.3;
DE   AltName: Full=Agitoxin-3;
DE            Short=AgTx-3;
DE            Short=AgTx3;
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=8204618; DOI=10.1021/bi00188a012;
RA   Garcia M.L., Garcia-Calvo M., Hidalgo P., Lee A., Mackinnon R.;
RT   "Purification and characterization of three inhibitors of voltage-dependent
RT   K+ channels from Leiurus quinquestriatus var. hebraeus venom.";
RL   Biochemistry 33:6834-6839(1994).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16551474; DOI=10.1016/j.toxicon.2006.01.015;
RA   Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A.,
RA   Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E.,
RA   Pimenta A.M.C.;
RT   "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering
RT   analyses to infer phylogenetic relationships in some scorpions from the
RT   Buthidae family (Scorpiones).";
RL   Toxicon 47:628-639(2006).
CC   -!- FUNCTION: Potent inhibitor of shaker potassium channels as well as the
CC       mammalian homologs of shaker.
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 03 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; C54471; C54471.
DR   AlphaFoldDB; P46112; -.
DR   BMRB; P46112; -.
DR   SMR; P46112; -.
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 3.3"
FT                   /id="PRO_0000044927"
FT   REGION          26..33
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="ECO:0000255"
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;  4107 MW;  E5945513F87B51CE CRC64;
     GVPINVPCTG SPQCIKPCKD AGMRFGKCMN RKCHCTPK