ID   KAX1E_MESMA             Reviewed;          59 AA.
AC   H2ETQ6;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Potassium channel toxin alpha-KTx 1.14;
DE   AltName: Full=BmKcug1 {ECO:0000303|PubMed:22230549};
DE            Short=Kcug1 {ECO:0000312|EMBL:AEX92701.1};
DE   Flags: Precursor;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=22230549; DOI=10.1016/j.peptides.2011.12.012;
RA   Zeng X.C., Zhang L., Nie Y., Luo X.;
RT   "Identification and molecular characterization of three new K(+)-channel
RT   specific toxins from the Chinese scorpion Mesobuthus martensii Karsch
RT   revealing intronic number polymorphism and alternative splicing in
RT   duplicated genes.";
RL   Peptides 34:311-323(2012).
CC   -!- FUNCTION: Potent blocker of both large-conductance calcium-activated
CC       potassium channels (KCa1.1/KCNMA1) and voltage-gated potassium channels
CC       (Kv1.3/KCNA3 and ERG1/Kv11.1/KCNH2). {ECO:0000250|UniProtKB:Q9NII5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NII5}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:Q9NII5}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 01 subfamily. {ECO:0000305}.
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DR   EMBL; JQ074233; AEX92701.1; -; mRNA.
DR   AlphaFoldDB; H2ETQ6; -.
DR   SMR; H2ETQ6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   3: Inferred from homology;
KW   Calcium-activated potassium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250|UniProtKB:Q9NII5"
FT   CHAIN           23..59
FT                   /note="Potassium channel toxin alpha-KTx 1.14"
FT                   /id="PRO_0000417433"
FT   SITE            49
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            58
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NII5"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000250|UniProtKB:Q9NII5"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000250|UniProtKB:Q9NII5"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250|UniProtKB:Q9NII5"
SQ   SEQUENCE   59 AA;  6646 MW;  1618F322E2E4BE4D CRC64;
     MKKISFLLLL AIVICSIGWT DGQFTDVRCS ASSKCWPVCK KLFGTYKGKC KNSKCRCYS