ID   SCX47_MESMA             Reviewed;          85 AA.
AC   P0DMH9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Alpha-toxin BmalphaTx47;
DE   Flags: Precursor;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=24577584; DOI=10.3390/toxins6030816;
RA   Li T., Xu L., Liu H., He Y., Liang S., Li W., Wu Y.;
RT   "Characterization of a novel BmalphaTX47 toxin modulating sodium channels:
RT   the crucial role of expression vectors in toxin pharmacological activity.";
RL   Toxins 6:816-829(2014).
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 expressed with the
CC       pET-14b vector has low inhibitory activity on sodium channels (11.33%
CC       on rNav1.2/SCN2A, 15.96% on mNav1.4/SCN4A and 5.04% on hNav1.5/SCN5A).
CC       When expressed with the pET-28a vector, this toxin has higher
CC       inhibitory activities (44.12% on rNav1.2/SCN2A, 25.40% on mNav1.4/SCN4A
CC       and 65.34% on hNav1.5/SCN5A). {ECO:0000269|PubMed:24577584}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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   AlphaFoldDB; P0DMH9; -.
DR   SMR; P0DMH9; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..83
FT                   /note="Alpha-toxin BmalphaTx47"
FT                   /id="PRO_0000428966"
FT   DOMAIN          21..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        41..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        45..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   85 AA;  9356 MW;  A08D6890E9BDB9AD CRC64;
     MNYLIVISFA LLLMTGVQSG RDAYIADSEN CTYTCALNPY CNDLCTKNGA KSGYCQWAGR
     YGNACWCIDL PDKVPIRISG SCRGR