ID   KXA3_MESEU              Reviewed;          60 AA.
AC   E4VP04;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Potassium channel toxin MeuTXKalpha3 {ECO:0000303|PubMed:20889474};
DE   Flags: Precursor;
OS   Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PRO-59.
RC   TISSUE=Venom gland;
RX   PubMed=20889474; DOI=10.1074/mcp.m110.002832;
RA   Zhu S., Peigneur S., Gao B., Luo L., Jin D., Zhao Y., Tytgat J.;
RT   "Molecular diversity and functional evolution of scorpion potassium channel
RT   toxins.";
RL   Mol. Cell. Proteomics 10:M110.002832-M110.002832(2011).
CC   -!- FUNCTION: May block voltage-gated potassium channels (Kv).
CC       {ECO:0000305|PubMed:20889474}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20889474}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20889474}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. {ECO:0000305}.
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DR   EMBL; EF442052; ABR20117.1; -; mRNA.
DR   EMBL; EF442053; ABR20118.1; -; mRNA.
DR   AlphaFoldDB; E4VP04; -.
DR   SMR; E4VP04; -.
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   Amidation; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..59
FT                   /note="Potassium channel toxin MeuTXKalpha3"
FT                   /evidence="ECO:0000305|PubMed:20889474"
FT                   /id="PRO_5007653880"
FT   SITE            49
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000305|PubMed:20889474"
FT   SITE            58
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000305|PubMed:20889474"
FT   MOD_RES         59
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000305|PubMed:20889474"
FT   DISULFID        32..50
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        37..55
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        41..57
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
SQ   SEQUENCE   60 AA;  6822 MW;  AA41B2114AD324C4 CRC64;
     MKNYCGIITL FLAIISATGV FCVDFPNKGG KCDRKECRKT CKKLNYRGKC FPNYCRCFPG