ID   SCXA_MESEU              Reviewed;          65 AA.
AC   P01490;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Alpha-toxin BeM10;
DE   AltName: Full=Neurotoxin M10;
OS   Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34648;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Grishin E.V., Soldatov N.M., Soldatova L.N., Ovchinnikov Y.A.;
RT   "Studies of the toxins from Buthus eupeus scorpion venom.";
RL   Toxicon 17 Suppl. 1:60-60(1979).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Grishin E.V., Soldatova L.N., Shakhparonov M.I., Kazakov V.K.;
RT   "The amino acid sequence of neurotoxin M10 from the venom of the Central
RT   Asian scorpion Buthus eupeus.";
RL   Bioorg. Khim. 6:714-723(1980).
RN   [3]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=4091860;
RA   Volkova T.M., Garsia A.F., Telezhinskaia I.N., Potapenko N.A.,
RA   Grishin E.V.;
RT   "Neurotoxins from the venom of the Central Asian scorpion Buthus eupeus.";
RL   Bioorg. Khim. 11:1445-1456(1985).
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. Has paralytic activity in mice.
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. Alpha subfamily. {ECO:0000305}.
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DR   PIR; JT0019; NTSR0E.
DR   AlphaFoldDB; P01490; -.
DR   SMR; P01490; -.
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; 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..65
FT                   /note="Alpha-toxin BeM10"
FT                   /id="PRO_0000066730"
FT   DOMAIN          2..65
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   65 AA;  7373 MW;  E79FFE5DEE6CB694 CRC64;
     VRDGYIADDK DCAYFCGRNA YCDEECKKGA ESGKCWYAGQ YGNACWCYKL PDWVPIKQKV
     SGKCN