ID   SCX2_MESMA              Reviewed;          64 AA.
AC   P59360;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Neurotoxin BmK-II;
DE            Short=BmK II;
DE            Short=BmKII;
DE   AltName: Full=BmK2;
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   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   TISSUE=Venom;
RX   PubMed=8896191; DOI=10.1016/0041-0101(96)00065-7;
RA   Ji Y.-H., Mansuelle P., Terakawa S., Kopeyan C., Yanaihara N., Hsu K.,
RA   Rochat H.;
RT   "Two neurotoxins (BmK I and BmK II) from the venom of the scorpion Buthus
RT   martensi Karsch: purification, amino acid sequences and assessment of
RT   specific activity.";
RL   Toxicon 34:987-1001(1996).
CC   -!- FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation
CC       of the activated channels, thereby blocking neuronal transmission. This
CC       toxin is active against mammals and insects. BmK-II is 6-fold less
CC       toxic than BmK-I.
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   AlphaFoldDB; P59360; -.
DR   SMR; P59360; -.
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..64
FT                   /note="Neurotoxin BmK-II"
FT                   /id="PRO_0000066748"
FT   DOMAIN          2..64
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   64 AA;  7226 MW;  85DF73330778A864 CRC64;
     VRDAYIAKPH NCVYECARNE YCNDLCTKDG AKSGYCQWVG KYGNGCWCIE LPDNVPIRIP
     GNCH