ID   KBX11_MESEU             Reviewed;          91 AA.
AC   A9XE60;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Potassium channel toxin MeuTXK-beta-1;
DE            Short=MeuTXKbeta1;
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], PROTEIN SEQUENCE OF 20-23, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20045493; DOI=10.1016/j.bbapap.2009.12.017;
RA   Zhu S., Gao B., Aumelas A., Del Carmen Rodriguez M., Lanz-Mendoza H.,
RA   Peigneur S., Diego-Garcia E., Martin-Eauclaire M.-F., Tytgat J.,
RA   Possani L.D.;
RT   "MeuTXKbeta1, a scorpion venom-derived two-domain potassium channel toxin-
RT   like peptide with cytolytic activity.";
RL   Biochim. Biophys. Acta 1804:872-883(2010).
CC   -!- FUNCTION: Has a low affinity binding to potassium channels of rat brain
CC       synaptosomes. Displays weak antibacterial activity against
CC       Stenotrophomonas sp. Strongly inhibits the development of the
CC       Plasmodium berghei ookinetes. Displays slight hemolytic effect on mouse
CC       erythrocytes. Induces cytolysis on Xenopus oocytes at high
CC       concentrations. Is not toxic on mice and on the insect Tenebrio
CC       molitor. {ECO:0000269|PubMed:20045493}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=8256.81; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20045493};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; EF190325; ABP35519.1; -; mRNA.
DR   AlphaFoldDB; A9XE60; -.
DR   BMRB; A9XE60; -.
DR   SMR; A9XE60; -.
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   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; 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   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Hemolysis; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:20045493"
FT   CHAIN           20..91
FT                   /note="Potassium channel toxin MeuTXK-beta-1"
FT                   /id="PRO_0000394022"
FT   DOMAIN          54..91
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        57..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        64..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        68..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   91 AA;  10338 MW;  C2879665D440C682 CRC64;
     MQRNLVVLLF LGMVALSSCG FREKHFQRFV KYAVPESTLR TVLQTVVHKV GKTQFGCPAY
     QGYCDDHCQD IEKKEGFCHG FKCKCGIPMG F