ID   KA263_MESGB             Reviewed;          57 AA.
AC   A0A059UI21;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Potassium channel toxin alpha-KTx 26.3 {ECO:0000303|PubMed:24746279};
DE   AltName: Full=Toxin Mgib2 {ECO:0000303|PubMed:24746279};
DE   Flags: Precursor;
OS   Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=123226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=24746279; DOI=10.1186/1471-2164-15-295;
RA   Diego-Garcia E., Caliskan F., Tytgat J.;
RT   "The Mediterranean scorpion Mesobuthus gibbosus (Scorpiones, Buthidae):
RT   transcriptome analysis and organization of the genome encoding chlorotoxin-
RT   like peptides.";
RL   BMC Genomics 15:295-295(2014).
CC   -!- FUNCTION: Recombinant toxin that reversibly inhibits the potassium
CC       current of mKv1.3/KCNA3 channel stably expressed in COS7 cells
CC       (IC(50)=150 nM). {ECO:0000250|UniProtKB:A7KJJ7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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 26 subfamily. {ECO:0000305}.
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DR   EMBL; KF770809; AHZ63118.1; -; mRNA.
DR   AlphaFoldDB; A0A059UI21; -.
DR   SMR; A0A059UI21; -.
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; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..24
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433147"
FT   CHAIN           25..57
FT                   /note="Potassium channel toxin alpha-KTx 26.3"
FT                   /id="PRO_0000433148"
FT   SITE            47
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000305"
FT   SITE            56
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000305"
FT   DISULFID        30..48
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        34..53
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        38..55
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
SQ   SEQUENCE   57 AA;  6261 MW;  922E43477483E19E CRC64;
     MSGLSVFILI ALVLSVIIDV LNNSKVEAAC KENCRQYCQA KGARNGKCIN SNCKCYY