ID   SCU1_MESMA              Reviewed;          66 AA.
AC   E7CAU3;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Neurotoxin BmK AGP-SYPU1 {ECO:0000303|PubMed:20945457};
DE   Flags: Precursor; Fragment;
GN   Name=AGP-SYPU1 {ECO:0000312|EMBL:ADR83605.1};
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] {ECO:0000305, ECO:0000312|EMBL:ADR83605.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:20945457};
RX   PubMed=20945457; DOI=10.1002/bmc.1519;
RA   Wang Y., Wang L., Cui Y., Song Y.B., Liu Y.F., Zhang R., Wu C.F.,
RA   Zhang J.H.;
RT   "Purification, characterization and functional expression of a new peptide
RT   with an analgesic effect from Chinese scorpion Buthus martensii Karsch (BmK
RT   AGP-SYPU1).";
RL   Biomed. Chromatogr. 25:801-807(2011).
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 (By similarity). This toxin has
CC       a strong analgesic effect when administered to mice by intraperitoneal
CC       injection. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20945457}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20945457}.
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=7545.4131; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20945457};
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Alpha subfamily. {ECO:0000255}.
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DR   EMBL; GU726488; ADR83605.1; -; mRNA.
DR   AlphaFoldDB; E7CAU3; -.
DR   SMR; E7CAU3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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   GO; GO:0044465; P:modulation of sensory perception of pain in another organism; IDA:UniProtKB.
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 AGP-SYPU1"
FT                   /evidence="ECO:0000269|PubMed:20945457"
FT                   /id="PRO_0000413469"
FT   PROPEP          65..66
FT                   /note="Removed by a carboxypeptidase"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GQW3"
FT                   /id="PRO_0000413470"
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         1
FT                   /evidence="ECO:0000312|EMBL:ADR83605.1"
SQ   SEQUENCE   66 AA;  7539 MW;  B8B90AFA9A09E020 CRC64;
     GRDAYIAQNY NCVYHCFRDD YCNGLCTENG ADSGYCYLAG KYGHACWCIN LPDDKPIRIP
     GKCHRR