ID NDB51_MESEU Reviewed; 88 AA. AC P0CH57; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 1. DT 01-APR-2015, entry version 16. DE RecName: Full=Potassium channel toxin MeuTXKbeta3; DE AltName: Full=BeL-5; DE AltName: Full=BeL-69; 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=MeuTXKbeta3; 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, RP AND 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 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. CC No antibacterial, antifungal and hemolytic activities have been CC found at micromolar concentrations. {ECO:0000269|PubMed:20097251}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}. CC -!- MISCELLANEOUS: The RNA coding for this protein is silently edited. CC -!- MISCELLANEOUS: Meucin-24 belongs to the non-disulfide-bridged CC peptide (NDBP) superfamily. Antimalarial peptide (group 5) family. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class CC 2 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 PDB; 2KFE; NMR; -; A=23-46. DR PDBsum; 2KFE; -. DR EvolutionaryTrace; P0CH57; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR InterPro; IPR029237; Long_scorpion_toxin. DR Pfam; PF14866; Toxin_38; 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; KW Toxin. FT SIGNAL 1 22 {ECO:0000255}. FT PEPTIDE 23 46 Meucin-24. {ECO:0000255}. FT /FTId=PRO_0000398381. FT CHAIN 42 88 MeuTXKbeta3. FT /FTId=PRO_0000398382. FT DISULFID 58 78 {ECO:0000250}. FT DISULFID 65 83 {ECO:0000250}. FT DISULFID 69 85 {ECO:0000250}. SQ SEQUENCE 88 AA; 10144 MW; C773252377F56D8E CRC64; MMKQQFFLFL AVIVMISSVI EAGRGREFMS NLKEKLSGVK EKMKNSWNRL TSMSEYACPV IEKWCEDHCQ AKNAIGRCEN TECKCLSK //