ID   CTXL_HOTTS              Reviewed;          36 AA.
AC   P59887;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Chlorotoxin-like peptide Bs 14 {ECO:0000303|PubMed:10048185};
DE            Short=Bs14 {ECO:0000303|PubMed:10048185};
OS   Hottentotta tamulus sindicus (Scorpion) (Buthus sindicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=42519;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10048185; DOI=10.1016/s1095-6433(98)10140-x;
RA   Ali S.A., Stoeva S., Schuetz J., Kayed R., Abbasi A., Zaidi Z.H.,
RA   Voelter W.;
RT   "Purification and primary structure of low molecular mass peptides from
RT   scorpion (Buthus sindicus) venom.";
RL   Comp. Biochem. Physiol. 121A:323-332(1998).
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).
CC       {ECO:0000250|UniProtKB:Q9UAD0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10048185}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:10048185}.
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=3848.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10048185};
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; P59887; -.
DR   SMR; P59887; -.
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..36
FT                   /note="Chlorotoxin-like peptide Bs 14"
FT                   /evidence="ECO:0000269|PubMed:10048185"
FT                   /id="PRO_0000044901"
FT   DISULFID        1..18
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        4..25
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        15..30
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
FT   DISULFID        19..32
FT                   /evidence="ECO:0000250|UniProtKB:P15222,
FT                   ECO:0000255|PROSITE-ProRule:PRU00545"
SQ   SEQUENCE   36 AA;  3847 MW;  536117F8E50165A0 CRC64;
     CGPCFTKDPE TEKKCATCCG GIGRCFGPQC LCNRGY