ID   3S11_DEMVE              Reviewed;          84 AA.
AC   A6MFK6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Short neurotoxin SNTX-1;
DE   Flags: Precursor;
OS   Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX   NCBI_TaxID=412038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17608513; DOI=10.1021/pr0701613;
RA   St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA   de Jersey J., Masci P.P., Lavin M.F.;
RT   "Diversity of toxic components from the venom of the evolutionarily
RT   distinct black whip snake, Demansia vestigiata.";
RL   J. Proteome Res. 6:3093-3107(2007).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission. {ECO:0000250|UniProtKB:P60775}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type I alpha-neurotoxin sub-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; DQ917517; ABK63546.1; -; mRNA.
DR   AlphaFoldDB; A6MFK6; -.
DR   SMR; A6MFK6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..84
FT                   /note="Short neurotoxin SNTX-1"
FT                   /id="PRO_5000254110"
FT   DISULFID        25..46
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        39..63
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        65..76
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        77..82
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   84 AA;  9317 MW;  A351C70D54F2D942 CRC64;
     MKTLLLILVV VTIVCLDLVC CSRTCCNQQS SQPKTTTVCP DGEKSCYKKS WRDHRGTRSE
     RGCGCPTVKP GVNRECCDTD ECNN