ID   KAX34_LEIHE             Reviewed;          38 AA.
AC   P46110;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.4;
DE   AltName: Full=Agitoxin-1 {ECO:0000303|PubMed:8204618};
DE            Short=AgTx-1 {ECO:0000303|PubMed:8204618};
DE            Short=AgTx1 {ECO:0000303|PubMed:8204618};
DE   AltName: Full=Leiurotoxin II;
DE            Short=LeTx II;
DE   AltName: Full=Leiurotoxin-2;
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, FUNCTION, ACTIVITY PROFILE, AND SUBCELLULAR LOCATION.
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 the Shaker potassium channel (Ki=0.16 nM)
CC       and its mammalian homologs (Kv1.3/KCNA3 (Ki=1.7 nM), Kv1.1/KCNA1
CC       (Ki=136 nM), Kv1.6/KCNA6 (Ki=149 nM)). {ECO:0000269|PubMed:8204618}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8204618}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8204618}.
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   -!- MISCELLANEOUS: Does not block Kv2.1/KCNB1 (Ki >2000 nM).
CC       {ECO:0000269|PubMed:8204618}.
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   PIR; A54471; A54471.
DR   AlphaFoldDB; P46110; -.
DR   SMR; P46110; -.
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;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..38
FT                   /note="Potassium channel toxin alpha-KTx 3.4"
FT                   /evidence="ECO:0000269|PubMed:8204618"
FT                   /id="PRO_0000044925"
FT   DISULFID        8..28
FT                   /evidence="ECO:0000250|UniProtKB:P46111"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000250|UniProtKB:P46111"
FT   DISULFID        18..35
FT                   /evidence="ECO:0000250|UniProtKB:P46111"
SQ   SEQUENCE   38 AA;  4021 MW;  A0951113F87B51CE CRC64;
     GVPINVKCTG SPQCLKPCKD AGMRFGKCIN GKCHCTPK