ID   KA262_LYCMC             Reviewed;          58 AA.
AC   D9U2B2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Potassium channel toxin alpha-KTx 26.2 {ECO:0000305};
DE   AltName: Full=Neurotoxin KTx13 {ECO:0000303|PubMed:20663230};
DE   Flags: Precursor;
OS   Lychas mucronatus (Chinese swimming scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX   NCBI_TaxID=172552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hainan; TISSUE=Venom gland;
RX   PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA   Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT   "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT   mucronatus reveals intraspecific toxic gene diversity and new venomous
RT   components.";
RL   BMC Genomics 11:452-452(2010).
CC   -!- FUNCTION: Inhibits voltage-gated potassium channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20663230}.
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; EU163859; ABY26668.1; -; mRNA.
DR   AlphaFoldDB; D9U2B2; -.
DR   SMR; D9U2B2; -.
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.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..58
FT                   /note="Potassium channel toxin alpha-KTx 26.2"
FT                   /id="PRO_0000403832"
FT   SITE            48
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000305"
FT   SITE            57
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000305"
FT   DISULFID        31..49
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        35..54
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
FT   DISULFID        39..56
FT                   /evidence="ECO:0000250|UniProtKB:P0DL65"
SQ   SEQUENCE   58 AA;  6153 MW;  AE616D72CBCD2328 CRC64;
     MKTIFVVILV LFVLSAMLAS SPDTTAEAAG CRGNCVTICR DKGKVGGKCY NGKCFCFN