ID   SCBTY_MESMA             Reviewed;          83 AA.
AC   M4GX67;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=BmKBT-like peptide;
DE   AltName: Full=Beta-toxin BmKBy;
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 [GENOMIC DNA / MRNA], BIOASSAY, AND TOXIC DOSE.
RX   PubMed=22705625; DOI=10.1016/j.peptides.2012.06.002;
RA   Nie Y., Zeng X.C., Luo X., Wu S., Zhang L., Cao H., Zhou J., Zhou L.;
RT   "Tremendous intron length differences of the BmKBT and a novel BmKBT-like
RT   peptide genes provide a mechanical basis for the rapid or constitutive
RT   expression of the peptides.";
RL   Peptides 37:150-156(2012).
CC   -!- FUNCTION: Sodium channel inhibitor (By similarity). Possesses potent
CC       toxicity in mice but induces only paralysis in cotton bollworm.
CC       {ECO:0000250}.
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   -!- TOXIC DOSE: LD(50) is 180 ug/kg by subcutaneous injection into mice.
CC       {ECO:0000269|PubMed:22705625}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   EMBL; JN940008; AFH68057.1; -; mRNA.
DR   EMBL; JN968973; AFR43269.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4GX67; -.
DR   SMR; M4GX67; -.
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   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..82
FT                   /note="BmKBT-like peptide"
FT                   /id="PRO_0000428820"
FT   PROPEP          83
FT                   /note="Removed by a carboxypeptidase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000428821"
FT   DOMAIN          21..81
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        41..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        45..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   83 AA;  9611 MW;  122DF9DA98B48223 CRC64;
     MKAALLLVIS TLMLIGVLTK KSGYPIQHDG CKNWCVFNHF CENICETYGG SGYCYFWKLA
     CWCDNIHNWV PTWSRETNKC RAK