ID   KA111_PARVI             Reviewed;          37 AA.
AC   P60164;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Potassium channel toxin alpha-KTx 11.1 {ECO:0000303|PubMed:10542442, ECO:0000303|PubMed:14561751};
DE   AltName: Full=Parabutoxin-1 {ECO:0000303|PubMed:10542442, ECO:0000303|PubMed:14561751};
DE            Short=PBTx1 {ECO:0000303|PubMed:10542442, ECO:0000303|PubMed:14561751};
OS   Parabuthus villosus (Black hairy thick-tailed scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Parabuthus.
OX   NCBI_TaxID=252780;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, REVIEW, AND NOMENCLATURE.
RC   TISSUE=Venom;
RX   PubMed=10542442; DOI=10.1016/s0165-6147(99)01398-x;
RA   Tytgat J., Chandy K.G., Garcia M.L., Gutman G.A., Martin-Eauclaire M.-F.,
RA   van der Walt J.J., Possani L.D.;
RT   "A unified nomenclature for short-chain peptides isolated from scorpion
RT   venoms: alpha-KTx molecular subfamilies.";
RL   Trends Pharmacol. Sci. 20:444-447(1999).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF THR-24 AND VAL-26.
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).
RN   [3]
RP   FUNCTION ON KV7.1/KCNQ1 CHANNELS.
RX   PubMed=22511981; DOI=10.1371/journal.pone.0035154;
RA   Chen Z.Y., Zeng D.Y., Hu Y.T., He Y.W., Pan N., Ding J.P., Cao Z.J.,
RA   Liu M.L., Li W.X., Yi H., Jiang L., Wu Y.L.;
RT   "Structural and functional diversity of acidic scorpion potassium channel
RT   toxins.";
RL   PLoS ONE 7:E35154-E35154(2012).
CC   -!- FUNCTION: Binds and inhibits voltage-sensitive potassium channels.
CC       Inhibits the vertebrate potassium channels Kv1.1/KCNA1, Kv1.2/KCNA2 and
CC       Kv1.3/KCNA3 with low affinity. Also weakly inhibits Kv7.1/KCNQ1 (10 uM
CC       of the toxin inhibits currents by 21.43%) (PubMed:22511981).
CC       {ECO:0000269|PubMed:14561751, ECO:0000269|PubMed:22511981}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10542442}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:10542442}.
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   AlphaFoldDB; P60164; -.
DR   SMR; P60164; -.
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..37
FT                   /note="Potassium channel toxin alpha-KTx 11.1"
FT                   /evidence="ECO:0000269|PubMed:10542442"
FT                   /id="PRO_0000044915"
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"
FT   MUTAGEN         24
FT                   /note="T->F: Increased affinity towards Kv1.1, Kv1.2 and
FT                   Kv1.3 channels."
FT                   /evidence="ECO:0000269|PubMed:14561751"
FT   MUTAGEN         26
FT                   /note="V->K: Increased affinity towards Kv1.1, Kv1.2 and
FT                   Kv1.3 channels."
FT                   /evidence="ECO:0000269|PubMed:14561751"
SQ   SEQUENCE   37 AA;  4096 MW;  61C4CB1ADF1D51D2 CRC64;
     DEEPKESCSD EMCVIYCKGE EYSTGVCDGP QKCKCSD