ID   SIX3B_LEIHE             Reviewed;          85 AA.
AC   P0C5I4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Beta-insect depressant toxin Lqh-dprIT3b;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TOXIC
RP   DOSE.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15966742; DOI=10.1021/bi050235t;
RA   Strugatsky D., Zilberberg N., Stankiewicz M., Ilan N., Turkov M., Cohen L.,
RA   Pelhate M., Gilles N., Gordon D., Gurevitz M.;
RT   "Genetic polymorphism and expression of a highly potent scorpion depressant
RT   toxin enable refinement of the effects on insect Na channels and illuminate
RT   the key role of Asn-58.";
RL   Biochemistry 44:9179-9187(2005).
CC   -!- FUNCTION: Depressant insect beta-toxins cause a transient contraction
CC       paralysis followed by a slow flaccid paralysis. They bind voltage-
CC       independently at site-4 of sodium channels (Nav) and block action
CC       potentials, primarily by depolarizing the axonal membrane and
CC       suppressing the sodium current. This depressant toxin is active only on
CC       insects. It is found in a relatively small amount in the venom, and its
CC       activity on insects is 10-fold higher compared to other known
CC       depressant toxins. {ECO:0000269|PubMed:15966742}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   -!- TOXIC DOSE: PD(50) is 3-5 ng/100 mg of body weight of Sarcophaga larvae
CC       for both contraction and flaccid paralysis.
CC       {ECO:0000269|PubMed:15966742}.
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; P0C5I4; -.
DR   SMR; P0C5I4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   CDD; cd00107; Knot1; 1.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR018218; Scorpion_toxinL.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   PRINTS; PR00285; SCORPNTOXIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT   CHAIN           22..82
FT                   /note="Beta-insect depressant toxin Lqh-dprIT3b"
FT                   /id="PRO_0000307612"
FT   DOMAIN          22..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   SITE            79
FT                   /note="Important for toxicity"
FT   MOD_RES         82
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        46..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   85 AA;  9203 MW;  CBB84208419C37A1 CRC64;
     MKLLLLLTIS ASMLIEGLVN ADGYIRGGDG CKVSCVINHV FCDNECKAAG GSYGYCWGWG
     LACWCEGLPA DREWDYETNT CGGKK