ID   CTXL_ANDAU              Reviewed;          34 AA.
AC   P86436;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Chlorotoxin-like peptide AaCtx {ECO:0000303|PubMed:21262299};
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=21262299; DOI=10.1016/j.peptides.2011.01.015;
RA   Rjeibi I., Mabrouk K., Mosrati H., Berenguer C., Mejdoub H., Villard C.,
RA   Laffitte D., Bertin D., Ouafik L., Luis J., Elayeb M., Srairi-Abid N.;
RT   "Purification, synthesis and characterization of AaCtx, the first
RT   chlorotoxin-like peptide from Androctonus australis scorpion venom.";
RL   Peptides 32:656-663(2011).
CC   -!- FUNCTION: Toxin with unknown function in healthy organisms. On glioma
CC       cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2
CC       at the surface of glioma cells. This complex is then internalized via
CC       caveolae, thus inhibiting the chloride channels necessary for cell
CC       shrinkage and tumor propagation (By similarity). Inhibits migration and
CC       invasion of U87 glioma cells expressing CLCN3/ClC-3 voltage-gated
CC       chloride channels. {ECO:0000250|UniProtKB:Q9UAD0,
CC       ECO:0000269|PubMed:21262299}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21262299}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:21262299}.
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=3607.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21262299};
CC   -!- MISCELLANEOUS: Intracerebroventricular injection into mice does not
CC       induce neurotoxicity (up to 1 ug doses). {ECO:0000305|PubMed:21262299}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride
CC       channel inhibitor family. {ECO:0000255|PROSITE-ProRule:PRU00545}.
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DR   AlphaFoldDB; P86436; -.
DR   SMR; P86436; -.
DR   TCDB; 8.B.7.1.2; the cl(-) channel peptide inhibitor (gatx1) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017081; F:chloride 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   Chloride channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Toxin;
KW   Voltage-gated chloride channel impairing toxin.
FT   PEPTIDE         1..34
FT                   /note="Chlorotoxin-like peptide AaCtx"
FT                   /evidence="ECO:0000269|PubMed:21262299"
FT                   /id="PRO_0000397237"
FT   DISULFID        2..19
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        5..27
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        16..32
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        20..34
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
SQ   SEQUENCE   34 AA;  3598 MW;  270A957375B7E355 CRC64;
     MCIPCFTTNP NMAAKCNACC GSRRGSCRGP QCIC