ID   NDB51_MESEU             Reviewed;          88 AA.
AC   P0CH57; E4VNZ9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Potassium channel toxin MeuTXKbeta3-meucin-24 {ECO:0000303|PubMed:20889474};
DE   Contains:
DE     RecName: Full=Meucin-24 {ECO:0000303|PubMed:20097251};
DE     AltName: Full=Non-disulfide-bridged peptide 5.1 {ECO:0000303|PubMed:24184590};
DE              Short=NDBP-5.1 {ECO:0000303|PubMed:24184590};
DE   Contains:
DE     RecName: Full=Potassium channel toxin MeuTXKbeta3 {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], SYNTHESIS OF 23-46, FUNCTION OF MEUCIN-24, AND
RP   STRUCTURE BY NMR OF 23-46.
RC   TISSUE=Venom gland;
RX   PubMed=20097251; DOI=10.1016/j.biochi.2010.01.011;
RA   Gao B., Xu J., Del Carmen Rodriguez M., Lanz-Mendoza H.,
RA   Hernandez-Rivas R., Du W., Zhu S.;
RT   "Characterization of two linear cationic antimalarial peptides in the
RT   scorpion Mesobuthus eupeus.";
RL   Biochimie 92:350-359(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
RN   [3]
RP   NOMENCLATURE OF MEUCIN-24.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: MeuTXKbeta3 inhibits voltage-gated potassium channels.
CC       {ECO:0000250}.
CC   -!- FUNCTION: The synthetic meucin-24 inhibits the development of P.
CC       berghei ookinetes, kills intraerythrocytic P.falciparum, and is
CC       cytotoxic to the Drosophila S2 cell at micromolar concentrations. No
CC       antibacterial, antifungal and hemolytic activities have been found at
CC       micromolar concentrations. {ECO:0000269|PubMed:20097251}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20097251}.
CC   -!- MISCELLANEOUS: The RNA coding for this protein is silently edited.
CC   -!- MISCELLANEOUS: Meucin-24 belongs to the non-disulfide-bridged peptide
CC       (NDBP) superfamily. Antimalarial peptide (group 5) family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; EF442047; ABR20112.1; -; mRNA.
DR   PDB; 2KFE; NMR; -; A=23-46.
DR   PDBsum; 2KFE; -.
DR   AlphaFoldDB; P0CH57; -.
DR   BMRB; P0CH57; -.
DR   EvolutionaryTrace; P0CH57; -.
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; IPR029237; Long_scorpion_toxin.
DR   Pfam; PF14866; Toxin_38; 1.
DR   PROSITE; PS51862; BSPN_CSAB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; RNA editing; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..46
FT                   /note="Meucin-24"
FT                   /evidence="ECO:0000305|PubMed:20097251"
FT                   /id="PRO_0000398381"
FT   CHAIN           42..88
FT                   /note="Potassium channel toxin MeuTXKbeta3"
FT                   /evidence="ECO:0000305|PubMed:20097251"
FT                   /id="PRO_0000398382"
FT   DOMAIN          55..88
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        58..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        65..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        69..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   88 AA;  10144 MW;  C773252377F56D8E CRC64;
     MMKQQFFLFL AVIVMISSVI EAGRGREFMS NLKEKLSGVK EKMKNSWNRL TSMSEYACPV
     IEKWCEDHCQ AKNAIGRCEN TECKCLSK