SCL7_LEIHE
ID SCL7_LEIHE Reviewed; 66 AA.
AC P59357;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Alpha-like toxin Lqh7;
DE AltName: Full=Lqh VII;
DE Short=LqhVII;
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, 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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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: 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 28.7 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; P59357; -.
DR SMR; P59357; -.
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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..66
FT /note="Alpha-like toxin Lqh7"
FT /id="PRO_0000066787"
FT DOMAIN 2..66
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 23..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 27..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 66 AA; 6830 MW; C48422A6CF8F69AD CRC64;
VRDGYIAKPE NCAHHCFPGS SGCDTLCKEN GGTGGHCGFK VGHGTACWCN ALPDKVGIIV
DGVKCH