ID   KA113_PARGR             Reviewed;          36 AA.
AC   Q6WGI9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Potassium channel toxin alpha-KTx 11.3 {ECO:0000303|PubMed:14561751};
DE   AltName: Full=Parabutoxin-10 {ECO:0000303|PubMed:14561751};
DE            Short=PBTx10 {ECO:0000303|PubMed:14561751};
OS   Parabuthus granulatus (Granulated thick-tailed scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Parabuthus.
OX   NCBI_TaxID=242110;
RN   [1] {ECO:0000312|EMBL:AAQ23195.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=14561751; DOI=10.1074/jbc.m311029200;
RA   Huys I., Olamendi-Portugal T., Garcia-Gomez B.I., Vandenberghe I.,
RA   Van Beeumen J., Dyason K., Clynen E., Zhu S., van der Walt J.,
RA   Possani L.D., Tytgat J.;
RT   "A subfamily of acidic alpha-K(+) toxins.";
RL   J. Biol. Chem. 279:2781-2789(2004).
CC   -!- FUNCTION: Binds and inhibits voltage-sensitive potassium channels.
CC       Inhibits the vertebrate potassium channel Kv1.1/KCNA1 with low
CC       affinity. {ECO:0000269|PubMed:14561751}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14561751}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:14561751}.
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 11 subfamily. {ECO:0000305}.
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DR   EMBL; AY288306; AAQ23195.1; -; mRNA.
DR   AlphaFoldDB; Q6WGI9; -.
DR   SMR; Q6WGI9; -.
DR   TCDB; 8.B.2.2.1; the short scorpion toxin (s-st) superfamily.
DR   GO; GO:0005576; C:extracellular region; IDA: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; IPR012635; Parabutoxin.
DR   Pfam; PF08119; Toxin_31; 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   PEPTIDE         1..36
FT                   /note="Potassium channel toxin alpha-KTx 11.3"
FT                   /evidence="ECO:0000269|PubMed:14561751"
FT                   /id="PRO_0000044918"
FT   DISULFID        8..27
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        17..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   36 AA;  3937 MW;  44CA18451D56BAD8 CRC64;
     DEEPKETCSD DMCVIYCKGE EFSTGACDGP QKCKCS