ID   KAX14_CENLM             Reviewed;          37 AA.
AC   P0C167;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=Potassium channel toxin alpha-KTx 1.4;
DE   AltName: Full=Limbatotoxin;
DE            Short=LbTx;
DE   AltName: Full=Limbatustoxin;
OS   Centruroides limbatus (Bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=244936;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Novick J., Leonard R.J., King V.F., Schmalhofer W., Kaczororowski G.J.,
RA   Garcia M.L.;
RT   "Peptides and genes coding for scorpion toxins that affect ion-channels.";
RL   Biophys. J. 59:78A-78A(1991).
CC   -!- FUNCTION: Blocks selectively the high conductance calcium-activated
CC       (maxi-K) potassium channels. {ECO:0000250|UniProtKB:P0C182}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
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 01 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   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; Knottin, scorpion toxin-like; 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; Scorpion toxin-like; 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..37
FT                   /note="Potassium channel toxin alpha-KTx 1.4"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="PRO_0000226964"
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;  4042 MW;  D24C3592CBA917A3 CRC64;
     VFIDVSCSVS KECWAPCKAA VGTDRGKCMG KKCRCYX
//