ID   KA133_TITPA             Reviewed;          23 AA.
AC   P84630;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Potassium channel toxin alpha-KTx 13.3;
DE   AltName: Full=Toxin Tpa1;
OS   Tityus pachyurus (Colombian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=288781;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT TYR-23.
RC   TISSUE=Venom {ECO:0000269|PubMed:16309982};
RX   PubMed=16309982; DOI=10.1016/j.bbapap.2005.08.010;
RA   Barona J., Batista C.V.F., Zamudio F.Z., Gomez-Lagunas F., Wanke E.,
RA   Otero R., Possani L.D.;
RT   "Proteomic analysis of the venom and characterization of toxins specific
RT   for Na+ - and K+ -channels from the Colombian scorpion Tityus pachyurus.";
RL   Biochim. Biophys. Acta 1764:76-84(2006).
CC   -!- FUNCTION: Reversibly blocks Shaker B potassium channels, with a
CC       dissociation constant of 200 nM. {ECO:0000269|PubMed:16309982}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16309982}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16309982}.
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=2457; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16309982};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 13 subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P84630; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin.
FT   PEPTIDE         1..23
FT                   /note="Potassium channel toxin alpha-KTx 13.3"
FT                   /id="PRO_0000239431"
FT   REGION          13..20
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="ECO:0000250|UniProtKB:P83243, ECO:0000255"
FT   SITE            14
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            23
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:16309982"
FT   DISULFID        2..15
FT                   /evidence="ECO:0000250|UniProtKB:P83243"
FT   DISULFID        5..20
FT                   /evidence="ECO:0000250|UniProtKB:P83243"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250|UniProtKB:P83243"
SQ   SEQUENCE   23 AA;  2464 MW;  D59BFAD806F31700 CRC64;
     ACGSCRKKCK GPGKCINGRC KCY