ID   AEP1_MESMA              Reviewed;          85 AA.
AC   P15228; Q9Y0B8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   22-FEB-2023, entry version 95.
DE   RecName: Full=Toxin BmKAEP;
DE   AltName: Full=Anti-epilepsy peptide;
DE   AltName: Full=BmK AEP;
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], PROTEIN SEQUENCE OF 22-75, AMIDATION AT GLY-82,
RP   FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=11298767; DOI=10.1046/j.1432-1327.2001.02132.x;
RA   Wang C.-G., He X.-L., Shao F., Liu W., Ling M.-H., Wang D.-C., Chi C.-W.;
RT   "Molecular characterization of an anti-epilepsy peptide from the scorpion
RT   Buthus martensi Karsch.";
RL   Eur. J. Biochem. 268:2480-2485(2001).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 22-71, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=2930463; DOI=10.1042/bj2570509;
RA   Zhou X.-H., Yang D., Zhang J.-H., Liu C.-M., Lei K.-J.;
RT   "Purification and N-terminal partial sequence of anti-epilepsy peptide from
RT   venom of the scorpion Buthus martensii Karsch.";
RL   Biochem. J. 257:509-517(1989).
CC   -!- FUNCTION: Shows anti-epileptic activity. Shares high homology with
CC       depressant insect toxins, but shows very weak toxicity against mammals
CC       and insects and no obvious symptoms on insect larvae. May target
CC       voltage-gated sodium channel (Nav). {ECO:0000269|PubMed:11298767,
CC       ECO:0000269|PubMed:2930463}.
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   -!- MASS SPECTROMETRY: Mass=6730.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11298767};
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; AF160868; AAD43570.2; -; mRNA.
DR   PIR; S02174; S02174.
DR   AlphaFoldDB; P15228; -.
DR   SMR; P15228; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; NAS:UniProtKB.
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; Knottin, scorpion toxin-like; 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; Scorpion toxin-like; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:11298767"
FT   CHAIN           22..82
FT                   /note="Toxin BmKAEP"
FT                   /id="PRO_0000035212"
FT   DOMAIN          22..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         82
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:11298767"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        46..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        29..30
FT                   /note="NG -> DN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="W -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63..64
FT                   /note="CW -> QD (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="Q -> E (in Ref. 1; AA sequence and 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="D -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9296 MW;  CC321DADAAEEF35E CRC64;
     MKLFLLLVIS ASMLIDGLVN ADGYIRGSNG CKVSCLLGNE GCNKECRAYG ASYGYCWTWK
     LACWCQGLPD DKTWKSESNT CGGKK
//