ID   KA311_BUTOC             Reviewed;          39 AA.
AC   P0DL62;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Potassium channel toxin alpha-KTx 31.1 {ECO:0000303|PubMed:26079392};
DE   AltName: Full=Kbot55 {ECO:0000303|PubMed:26079392};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=26079392; DOI=10.1016/j.peptides.2015.05.015;
RA   ElFessi-Magouri R., Peigneur S., Khamessi O., Srairi-Abid N., ElAyeb M.,
RA   Mille B.G., Cuypers E., Tytgat J., Kharrat R.;
RT   "Kbot55, purified from Buthus occitanus tunetanus venom, represents the
RT   first member of a novel alpha-KTx subfamily.";
RL   Peptides 80:4-8(2016).
CC   -!- FUNCTION: Voltage-gated potassium channel inhibitor. 1 uM of the native
CC       toxin inhibits rat Kv1.2/KCNA2 (100% inhibition), and drosophila Shaker
CC       IR/Sh (100%), human Kv1.3/KCNA3 (83%), rat Kv1.1/KCNA1 (32%) and rat
CC       Kv1.6/KCNA6 (21%). {ECO:0000269|PubMed:26079392}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26079392}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26079392}.
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=4128.65; Method=MALDI; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:26079392};
CC   -!- TOXIC DOSE: LD(50) is below 5 ug/kg by intracerebroventricular
CC       injection into mice. A rapid paralysis in the lower half of the body
CC       was observed a few minutes after the injection and after 10 min the
CC       animals died.
CC   -!- MISCELLANEOUS: Does not inhibit rKv1.4/ and the sodium channel
CC       rNav1.4/. {ECO:0000269|PubMed:26079392}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 31 subfamily.
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DR   AlphaFoldDB; P0DL62; -.
DR   SMR; P0DL62; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..39
FT                   /note="Potassium channel toxin alpha-KTx 31.1"
FT                   /evidence="ECO:0000269|PubMed:26079392"
FT                   /id="PRO_0000434818"
FT   SITE            29
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..30
FT                   /evidence="ECO:0000250|UniProtKB:P13487"
FT   DISULFID        13..35
FT                   /evidence="ECO:0000250|UniProtKB:P13487"
FT   DISULFID        17..37
FT                   /evidence="ECO:0000250|UniProtKB:P13487"
SQ   SEQUENCE   39 AA;  4129 MW;  46E37017096E6E3A CRC64;
     AGSMDSCSET GVCMKACSER IRQVENDNKC PAGECICTT