ID   KA131_TITOB             Reviewed;          23 AA.
AC   P83243;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Potassium channel toxin alpha-KTx 13.1;
DE   AltName: Full=Toxin Tc1;
DE   AltName: Full=Toxin To1;
OS   Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=1221240 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11113450; DOI=10.1016/s0014-5793(00)02253-5;
RA   Batista C.V.F., Gomez-Lagunas F., Lucas S., Possani L.D.;
RT   "Tc1, from Tityus cambridgei, is the first member of a new subfamily of
RT   scorpion toxin that blocks K(+)-channels.";
RL   FEBS Lett. 486:117-120(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15025998; DOI=10.1016/j.jchromb.2003.09.002;
RA   Batista C.V.F., del Pozo L., Zamudio F.Z., Contreras S., Becerril B.,
RA   Wanke E., Possani L.D.;
RT   "Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and
RT   the role of prolines on mass spectrometry analysis of toxins.";
RL   J. Chromatogr. B 803:55-66(2004).
RN   [3]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=11790849; DOI=10.1110/ps.33402;
RA   Wang I., Wu S.H., Chang H.K., Shieh R.C., Yu H.M., Chen C.;
RT   "Solution structure of a K(+)-channel blocker from the scorpion Tityus
RT   cambridgei.";
RL   Protein Sci. 11:390-400(2002).
CC   -!- FUNCTION: Blocks reversibly Shaker B potassium channels. Also displaces
CC       binding of noxiustoxin to mouse brain synaptosome membranes.
CC       {ECO:0000269|PubMed:11113450}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15025998,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15025998, ECO:0000305}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC   -!- MASS SPECTROMETRY: Mass=2446.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11113450};
CC   -!- MASS SPECTROMETRY: Mass=2446.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15025998};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 13 subfamily. {ECO:0000305}.
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DR   PDB; 1JLZ; NMR; -; A=1-23.
DR   PDBsum; 1JLZ; -.
DR   AlphaFoldDB; P83243; -.
DR   SMR; P83243; -.
DR   EvolutionaryTrace; P83243; -.
DR   GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044361; P:negative regulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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 13.1"
FT                   /id="PRO_0000044919"
FT   REGION          13..20
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="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   DISULFID        2..15
FT                   /evidence="ECO:0000269|PubMed:11790849"
FT   DISULFID        5..20
FT                   /evidence="ECO:0000269|PubMed:11790849"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000269|PubMed:11790849"
FT   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:1JLZ"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:1JLZ"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:1JLZ"
SQ   SEQUENCE   23 AA;  2454 MW;  D59BFADBC9F31700 CRC64;
     ACGSCRKKCK GSGKCINGRC KCY