ID   SCAA2_MESMA             Reviewed;          65 AA.
AC   G4V3T9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Neurotoxin BmK AGAP-SYPU2;
DE   Flags: Fragment;
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 1-12, FUNCTION, BIOASSAY,
RP   MASS SPECTROMETRY, 3D-STRUCTURE MODELING, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24269605; DOI=10.1016/j.peptides.2013.10.023;
RA   Shao J.H., Cui Y., Zhao M.Y., Wu C.F., Liu Y.F., Zhang J.H.;
RT   "Purification, characterization, and bioactivity of a new analgesic-
RT   antitumor peptide from Chinese scorpion Buthus martensii Karsch.";
RL   Peptides 53:89-96(2014).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission (By similarity). Shows analgesic
CC       activity (ED(50) is 1.42 mg/kg) and antitumor activity against Ehrlich
CC       ascites tumor and fibrosarcoma models in vivo. {ECO:0000250,
CC       ECO:0000269|PubMed:24269605}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24269605}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24269605}.
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=7247.40; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24269605};
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   EMBL; GU726489; ADR83705.1; -; mRNA.
DR   AlphaFoldDB; G4V3T9; -.
DR   SMR; G4V3T9; -.
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..>65
FT                   /note="Neurotoxin BmK AGAP-SYPU2"
FT                   /id="PRO_0000428967"
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"
FT   NON_TER         65
SQ   SEQUENCE   65 AA;  7253 MW;  5DD8160CB2C2C302 CRC64;
     VKDGYIVDDK NCAYFCGRNA YCDDECEKNG AESGYCQWAG VYGNACWCYK LPDKVPIRVP
     GRCNG