ID   SIX1D_LEIHE             Reviewed;          88 AA.
AC   P68724;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Beta-insect excitatory toxin LqhIT1d;
DE   AltName: Full=Insect neurotoxin 1d;
DE   AltName: Full=Lqh IT1-d;
DE            Short=LqhIT1-d;
DE   AltName: Full=Lqh-xtrITd;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9929387; DOI=10.1007/pl00006457;
RA   Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M.;
RT   "Dynamic diversification from a putative common ancestor of scorpion toxins
RT   affecting sodium, potassium, and chloride channels.";
RL   J. Mol. Evol. 48:187-196(1999).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
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: Excitatory insect toxins induce a spastic paralysis. They
CC       bind voltage-independently at site-4 of sodium channels (Nav) and shift
CC       the voltage of activation toward more negative potentials thereby
CC       affecting sodium channel activation and promoting spontaneous and
CC       repetitive firing (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9929387}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9929387}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P68724; -.
DR   SMR; P68724; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..88
FT                   /note="Beta-insect excitatory toxin LqhIT1d"
FT                   /evidence="ECO:0000305|PubMed:9929387"
FT                   /id="PRO_0000035192"
FT   DOMAIN          20..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        34..55
FT                   /evidence="ECO:0000250|UniProtKB:P56637"
FT   DISULFID        40..60
FT                   /evidence="ECO:0000250|UniProtKB:P56637"
FT   DISULFID        44..62
FT                   /evidence="ECO:0000250|UniProtKB:P56637"
FT   DISULFID        56..82
FT                   /evidence="ECO:0000250|UniProtKB:P56637"
SQ   SEQUENCE   88 AA;  9993 MW;  EAED1FEB6180608E CRC64;
     MKFFLLFLVV LPIMGVLGKK NGFAVDSNGK APECFFDHYC NSECTKVYYA EKGYCCTLSC
     YCVGLDDDKK VLDISDTRKK LCDFTLFN