ID   SCB1_LEIHE              Reviewed;          85 AA.
AC   P0C5H3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Beta-mammal/insect toxin Lqhb1;
DE   AltName: Full=Lqh-beta-1;
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], PROTEIN SEQUENCE OF 28-41, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12787033; DOI=10.1046/j.1432-1033.2003.03643.x;
RA   Gordon D., Ilan N., Zilberberg N., Gilles N., Urbach D., Cohen L.,
RA   Karbat I., Froy O., Gaathon A., Kallen R.G., Benveniste M., Gurevitz M.;
RT   "An 'Old World' scorpion beta-toxin that recognizes both insect and
RT   mammalian sodium channels.";
RL   Eur. J. Biochem. 270:2663-2670(2003).
CC   -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC       channels (Nav) and shift the voltage of activation toward more negative
CC       potentials thereby affecting sodium channel activation and promoting
CC       spontaneous and repetitive firing. Competes, with apparent high
CC       affinity, with anti-insect and anti-mammalian beta-toxins for binding
CC       to cockroach and rat brain synaptosomes, respectively. Also competes
CC       with an anti-mammalian alpha-toxin on binding to rat brain sodium
CC       channels. Has a weak effect on cardiac sodium channels and a marked
CC       effect on rat brain and skeletal muscle sodium channels.
CC       {ECO:0000269|PubMed:12787033}.
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   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. {ECO:0000305}.
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DR   AlphaFoldDB; P0C5H3; -.
DR   SMR; P0C5H3; -.
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   Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..85
FT                   /note="Beta-mammal/insect toxin Lqhb1"
FT                   /id="PRO_0000306088"
FT   DOMAIN          20..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
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;  9574 MW;  52F951FFDAD9D914 CRC64;
     MKIIIFLIVS SLMLIGVKTD NGYLLNKATG CKVWCVINNA SCNSECKLRR GNYGYCYFWK
     LACYCEGAPK SELWAYATNK CNGKL