ID   CTXL2_MESEU             Reviewed;          34 AA.
AC   F1DI80;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Chlorotoxin-like peptide MeICT {ECO:0000303|PubMed:35524923};
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] {ECO:0000312|EMBL:ADY02962.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Ayat H., Ilkhanizadeh S., Ahadi A.M.;
RT   "Isolation and molecular cloning of chlorotoxin-like peptide gene 'Me CT'
RT   from Mesobuthus eupeus in Iran.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   3D-STRUCTURE MODELING, AND PROBABLE INTERACTION WITH MMP2.
RA   Mohammadi Farsani F., Ayat H., Mohammad Ahadi A.;
RT   "Molecular modeling and docking studies on the first chlorotoxin-like
RT   peptide from iranian scorpion Mesobuthus eupeus (MeICT) and Snp variants of
RT   matrix methaloproteinase-2 (MMP-2).";
RL   Iran. J. Toxicol. 9:1368-1376(2015).
RN   [3]
RP   FUNCTION, BIOASSAY, 3D-STRUCTURE MODELING, AND RECOMBINANT EXPRESSION.
RC   TISSUE=Venom gland;
RX   PubMed=35524923; DOI=10.1007/s10529-022-03254-x;
RA   Gandomkari M.S., Ayat H., Ahadi A.M.;
RT   "Recombinantly expressed MeICT, a new toxin from Mesobuthus eupeus
RT   scorpion, inhibits glioma cell proliferation and downregulates Annexin A2
RT   and FOXM1 genes.";
RL   Biotechnol. Lett. 0:0-0(2022).
CC   -!- FUNCTION: Toxin with unknown function in healthy organisms. Suppress
CC       growth and migration of glioma cells and decreases the mRNA expression
CC       of annexin A2 (ANXA2) and forkhead box protein M1 (FOXM1), two key
CC       molecules in the progression and invasion of glioma (PubMed:35524923).
CC       May affect chloride channel (By similarity). May interact with MMP2 and
CC       inhibit its catalytic activity (By similarity) (Ref.2). In vivo, is not
CC       toxic when administrated to mice at high doses (PubMed:35524923).
CC       {ECO:0000250|UniProtKB:Q9UAD0, ECO:0000269|PubMed:35524923,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:35524923}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:35524923}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P15222}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride
CC       channel inhibitor family. {ECO:0000305}.
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DR   EMBL; HQ853233; ADY02962.1; -; mRNA.
DR   SMR; F1DI80; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Chloride channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Secreted; Toxin;
KW   Voltage-gated chloride channel impairing toxin.
FT   CHAIN           1..34
FT                   /note="Chlorotoxin-like peptide MeICT"
FT                   /id="PRO_0000456335"
FT   DISULFID        2..19
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        5..26
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        16..31
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        20..33
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
SQ   SEQUENCE   34 AA;  3767 MW;  1BBC1859EF318F26 CRC64;
     MCMPCFTTDH NMAKKCNDCC GGYGKCFGPQ CLCR