ID   CTXL_MESEU              Reviewed;          39 AA.
AC   P86401; R4H616;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Chlorotoxin-like peptide MeuClTx {ECO:0000305};
DE   AltName: Full=Chloride channel toxin-like peptide {ECO:0000303|Ref.2};
DE   Flags: Precursor; Fragment;
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].
RA   Zhu S., Gao B.;
RT   "Molecular characterization of a chloride channel toxin-like peptide from
RT   the scorpion Mesobuthus eupeus.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 4-38, FUNCTION, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND AMIDATION AT ARG-38.
RC   TISSUE=Venom;
RA   Shunyi S.Y., Gao B.;
RT   "Characterization of chloride channel toxin-like peptide from the scorpion
RT   Mesobuthus eupeus.";
RL   Submitted (NOV-2009) to UniProtKB.
CC   -!- FUNCTION: Inhibits Kv1.2/KCNA2 potassium channels. On glioma cells, may
CC       interact with chloride channels (probably Clc-3/CLCN3) and MMP2 at the
CC       surface of glioma cells. This complex may be then internalized via
CC       caveolae, thus inhibiting the chloride channels necessary for cell
CC       shrinkage and tumor propagation. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.2}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P15222}.
CC   -!- MASS SPECTROMETRY: Mass=3932; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride
CC       channel inhibitor family. {ECO:0000255|PROSITE-ProRule:PRU00545}.
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; GU187951; ADT64274.1; -; mRNA.
DR   AlphaFoldDB; P86401; -.
DR   SMR; P86401; -.
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; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR007958; Scorpion_toxinS_Cl_inh.
DR   Pfam; PF05294; Toxin_5; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51200; SHORT_SCORPION_CHLORIDE; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          <1..3
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         4..38
FT                   /note="Chlorotoxin-like peptide MeuClTx"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000401124"
FT   MOD_RES         38
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|Ref.2"
FT   DISULFID        5..22
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        8..29
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        23..36
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   NON_TER         1
SQ   SEQUENCE   39 AA;  4299 MW;  8583CBE8720B658A CRC64;
     TEAMCMPCFT TDHNMAKKCR DCCGGNGKCF GYQCLCNRG