ID   KAX1B_CENNO             Reviewed;          37 AA.
AC   P0C182;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Potassium channel toxin alpha-KTx 1.11;
DE   AltName: Full=Slotoxin {ECO:0000303|PubMed:11576530};
DE            Short=SloTx {ECO:0000303|PubMed:11576530};
OS   Centruroides noxius (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6878;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, ACTIVITY PROFILE, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11576530; DOI=10.1016/s0014-5793(01)02791-0;
RA   Garcia-Valdes J., Zamudio F.Z., Toro L., Possani L.D.;
RT   "Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels
RT   that differentiates between alpha and alpha+beta (beta1 or beta4)
RT   complexes.";
RL   FEBS Lett. 505:369-373(2001).
RN   [2]
RP   ERRATUM OF PUBMED:11576530.
RA   Garcia-Valdes J., Zamudio F.Z., Toro L., Possani L.D.;
RL   FEBS Lett. 507:122-122(2001).
CC   -!- FUNCTION: Reversibly blocks the high conductance calcium-activated
CC       potassium channels composed of only alpha subunits (KCa1.1/KCNMA1).
CC       Unreversibly blocks the high conductance calcium-activated potassium
CC       channels composed of alpha and beta1 subunits (KCNMA1 and KCNMB1).
CC       Unreversibly and weakly blocks the high conductance calcium-activated
CC       potassium channels composed of alpha and beta4 (KCNMA1 and KCNMB4).
CC       {ECO:0000269|PubMed:11576530}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11576530}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11576530}.
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=4082.82; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:11576530};
CC   -!- MISCELLANEOUS: Does not inhibit other potassium channels such as dSlo,
CC       Kv1.1/KCNA1, Kv11.1/KCNH2/ERG1, Kir2.2/KCNJ12, Shaker-IR, and voltage-
CC       independent/calcium-activated SK1/KCNN1, SK2/KCNN2 and SK3/KCNN3.
CC       {ECO:0000269|PubMed:11576530}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 01 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C182; -.
DR   SMR; P0C182; -.
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   CHAIN           1..37
FT                   /note="Potassium channel toxin alpha-KTx 1.11"
FT                   /id="PRO_0000228823"
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   37 AA;  4092 MW;  87352585F8F85028 CRC64;
     TFIDVDCTVS KECWAPCKAA FGVDRGKCMG KKCKCYV