ID   CTXL1_LEIHE             Reviewed;          34 AA.
AC   P85066;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Toxin GaTx1 {ECO:0000303|PubMed:17951250};
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, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT ARG-34.
RC   TISSUE=Venom;
RX   PubMed=17951250; DOI=10.1074/jbc.m708079200;
RA   Fuller M.D., Thompson C.H., Zhang Z.-R., Freeman C.S., Schay E.,
RA   Szakacs G., Bakos E., Sarkadi B., McMaster D., French R.J., Pohl J.,
RA   Kubanek J., McCarty N.A.;
RT   "State-dependent inhibition of cystic fibrosis transmembrane conductance
RT   regulator chloride channels by a novel peptide toxin.";
RL   J. Biol. Chem. 282:37545-37555(2007).
CC   -!- FUNCTION: Chloride channel ligand. Potently and reversibly inhibits
CC       CFTR chloride channels when the channels are in the interburst closed
CC       state. May also interact with chloride channels (probably ClC-3/CLCN3)
CC       and MMP2 at the surface of glioma cells. This complex may be then
CC       internalized via caveolae, thus inhibiting the chloride channels
CC       necessary for cell shrinkage and tumor propagation.
CC       {ECO:0000269|PubMed:17951250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17951250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17951250}.
CC   -!- MASS SPECTROMETRY: Mass=3674.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17951250};
CC   -!- MISCELLANEOUS: Does not inhibit ClC-1/CLCN1, ClC-2/CLCN2 or ClC-3/CLCN3
CC       voltage-gated chloride channels, GABA(C)/GABRR receptors, Shaker
CC       Kv1.1/KCNA1 potassium channels, or the multidrug resistance proteins
CC       ABCC1 (MRP1), ABCC2 (MRP2) and ABCC3 (MRP3).
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; P85066; -.
DR   SMR; P85066; -.
DR   TCDB; 8.B.7.1.1; 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   Amidation; 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   CHAIN           1..34
FT                   /note="Toxin GaTx1"
FT                   /evidence="ECO:0000269|PubMed:17951250"
FT                   /id="PRO_0000312773"
FT   MOD_RES         34
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:17951250"
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   34 AA;  3685 MW;  FB9643CA945FEC82 CRC64;
     CGPCFTTDHQ MEQKCAECCG GIGKCYGPQC LCNR