ID   SCL6_LEIHE              Reviewed;          64 AA.
AC   P59356;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Alpha-like toxin Lqh6;
DE   AltName: Full=Lqh VI;
DE            Short=LqhVI;
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, PHARMACOLOGICAL CHARACTERIZATION, AMIDATION AT LYS-64,
RP   AND TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=12180969; DOI=10.1046/j.1432-1033.2002.03065.x;
RA   Hamon A., Gilles N., Sautiere P., Martinage A., Kopeyan C., Ulens C.,
RA   Tytgat J., Lancelin J.-M., Gordon D.;
RT   "Characterization of scorpion alpha-like toxin group using two new toxins
RT   from the scorpion Leiurus quinquestriatus hebraeus.";
RL   Eur. J. Biochem. 269:3920-3933(2002).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels (Nav) and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission. This toxin is highly toxic to
CC       insects and mice, and inhibits the binding of alpha-toxin to cockroach
CC       neuronal membranes.
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: LD(50) is 34.3 nmol/kg to cockroaches (Blattella
CC       germanica). {ECO:0000269|PubMed:12180969}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P59356; -.
DR   SMR; P59356; -.
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   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; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
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; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..64
FT                   /note="Alpha-like toxin Lqh6"
FT                   /id="PRO_0000066786"
FT   DOMAIN          2..63
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         64
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:12180969"
FT   DISULFID        12..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        20..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        24..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   64 AA;  6803 MW;  49A54B0B6C75392E CRC64;
     VRDGYIAQPE NCVYHCIPDC DTLCKDNGGT GGHCGFKLGH GIACWCNALP DNVGIIVDGV
     KCHK