ID   KBX1_TITST              Reviewed;          60 AA.
AC   P0C2F3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Potassium channel toxin Tst-beta-KTx;
DE            Short=TstbetaKTx;
OS   Tityus stigmurus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=50344;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17270501; DOI=10.1016/j.cbpc.2006.12.004;
RA   Batista C.V.F., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z.,
RA   Gomez-Lagunas F., Possani L.D.;
RT   "Proteomic analysis of the venom from the scorpion Tityus stigmurus:
RT   biochemical and physiological comparison with other Tityus species.";
RL   Comp. Biochem. Physiol. 146C:147-157(2007).
RN   [2]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17141373; DOI=10.1016/j.peptides.2006.06.012;
RA   Diego-Garcia E., Schwartz E.F., D'Suze G., Gonzalez S.A., Batista C.V.,
RA   Garcia B.I., Rodriguez de la Vega R.C., Possani L.D.;
RT   "Wide phylogenetic distribution of scorpine and long-chain beta-KTx-like
RT   peptides in scorpion venoms: identification of 'orphan' components.";
RL   Peptides 28:31-37(2007).
RN   [3]
RP   FUNCTION.
RX   PubMed=18030427; DOI=10.1007/s00018-007-7370-x;
RA   Diego-Garcia E., Abdel-Mottaleb Y., Schwartz E.F.,
RA   Rodriguez de la Vega R.C., Tytgat J., Possani L.D.;
RT   "Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like
RT   peptides purified from scorpion venoms.";
RL   Cell. Mol. Life Sci. 65:187-200(2008).
CC   -!- FUNCTION: Blocks potassium channels Kv1.1/KCNA1, Kv1.2/KCNA2, and
CC       Kv1.3/KCNA3. {ECO:0000269|PubMed:18030427}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=6716.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17141373, ECO:0000269|PubMed:17270501};
CC   -!- MISCELLANEOUS: This toxin does not inhibit Kv1.4/KCNA4, Kv1.5/KCNA5,
CC       Kv1.6/KCNA6, Shaker IR and Kv11.1/KCNH2 potassium channels. Does not
CC       show cytolytic activity (PubMed:18030427).
CC       {ECO:0000305|PubMed:18030427}.
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC       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   AlphaFoldDB; P0C2F3; -.
DR   SMR; P0C2F3; -.
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; IPR029237; Long_scorpion_toxin.
DR   Pfam; PF14866; Toxin_38; 1.
DR   PROSITE; PS51862; BSPN_CSAB; 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   CHAIN           1..60
FT                   /note="Potassium channel toxin Tst-beta-KTx"
FT                   /id="PRO_0000274675"
FT   DOMAIN          26..60
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        36..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        40..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   60 AA;  6723 MW;  BA0F39860AB5CD21 CRC64;
     KLVALIPNDQ LRSILKAVVH KVAKTQFGCP AYEGYCNDHC NDIERKDGEC HGFKCKCAKD