ID   CTXL8_LEIHE             Reviewed;          38 AA.
AC   P55966;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Toxin Lqh 8/6;
OS   Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus
OS   hebraeus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX   NCBI_TaxID=6884;
RN   [1]
RP   PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=9210487; DOI=10.1111/j.1432-1033.1997.00218.x;
RA   Adjadj E., Naudat V., Quiniou E., Wouters D., Sautiere P., Craescu C.T.;
RT   "Solution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom
RT   -- structural heterogeneity induced by proline cis/trans isomerization.";
RL   Eur. J. Biochem. 246:218-227(1997).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16551474; DOI=10.1016/j.toxicon.2006.01.015;
RA   Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A.,
RA   Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E.,
RA   Pimenta A.M.C.;
RT   "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering
RT   analyses to infer phylogenetic relationships in some scorpions from the
RT   Buthidae family (Scorpiones).";
RL   Toxicon 47:628-639(2006).
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. {ECO:0000250|UniProtKB:Q9UAD0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9210487}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9210487}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:9210487}.
CC   -!- MASS SPECTROMETRY: Mass=4165; Mass_error=0.4; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:9210487};
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; P55966; -.
DR   SMR; P55966; -.
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..38
FT                   /note="Toxin Lqh 8/6"
FT                   /evidence="ECO:0000269|PubMed:9210487"
FT                   /id="PRO_0000044942"
FT   DISULFID        2..19
FT                   /evidence="ECO:0000269|PubMed:9210487"
FT   DISULFID        5..28
FT                   /evidence="ECO:0000269|PubMed:9210487"
FT   DISULFID        16..33
FT                   /evidence="ECO:0000269|PubMed:9210487"
FT   DISULFID        20..35
FT                   /evidence="ECO:0000269|PubMed:9210487"
SQ   SEQUENCE   38 AA;  4174 MW;  2ECA352EF9ACAFCD CRC64;
     RCSPCFTTDQ QMTKKCYDCC GGKGKGKCYG PQCICAPY