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 11-DEC-2019, entry version 21. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF442047; ABR20112.1; -; mRNA. DR PDB; 2KFE; NMR; -; A=23-46. DR PDBsum; 2KFE; -. DR EvolutionaryTrace; P0CH57; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:GOC. 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 //