ID   SNAY5_LYCMC             Reviewed;          83 AA.
AC   P0CI60;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Neurotoxin LmNaTx34.5;
DE   Flags: Precursor; Fragment;
OS   Lychas mucronatus (Chinese swimming scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX   NCBI_TaxID=172552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Yunnan; TISSUE=Venom gland;
RX   PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA   Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT   "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT   mucronatus reveals intraspecific toxic gene diversity and new venomous
RT   components.";
RL   BMC Genomics 11:452-452(2010).
CC   -!- FUNCTION: Binds voltage-independently at site-4 of sodium channels
CC       (Nav) and shift the voltage of activation toward more negative
CC       potentials thereby affecting sodium channel activation and promoting
CC       spontaneous and repetitive firing. {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   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GT028833; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0CI60; -.
DR   SMR; P0CI60; -.
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   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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..83
FT                   /note="Neurotoxin LmNaTx34.5"
FT                   /id="PRO_0000403821"
FT   DOMAIN          16..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        29..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        33..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        40..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   NON_TER         1
SQ   SEQUENCE   83 AA;  9472 MW;  CC8E71E958BFBF90 CRC64;
     FILVVIALMV IEVKSDGYLM VRAGREKGCK VWCVINNTYC DKDCKLKGGS YGYCYFWKLA
     CYCEGLPESS PDIWTYEKNT CST