ID   3S11_HYDOR              Reviewed;          60 AA.
AC   P68413; P01438; P10461; P19005;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Short neurotoxin 1;
DE   AltName: Full=Toxin A;
OS   Hydrophis ornatus (Ornate reef seasnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX   NCBI_TaxID=8685;
RN   [1]
RP   AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=6615431; DOI=10.1042/bj2130031;
RA   Tamiya N., Maeda N., Cogger H.G.;
RT   "Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and
RT   Hydrophis lapemoides.";
RL   Biochem. J. 213:31-38(1983).
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:0000269|PubMed:6615431}.
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   -!- CAUTION: The amino acid sequence of this toxin was deduced to be
CC       identical with that of toxin Astrotia stokesi A on the basis of
CC       identity of the tryptic peptide 'map' and the amino acid composition of
CC       each peptide. {ECO:0000305}.
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DR   PIR; B90321; N1AT1F.
DR   AlphaFoldDB; P68413; -.
DR   SMR; P68413; -.
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   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   CHAIN           1..60
FT                   /note="Short neurotoxin 1"
FT                   /id="PRO_0000093579"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        17..39
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        41..52
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        53..58
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   60 AA;  6599 MW;  DE41989F9056E59A CRC64;
     MTCCNQQSSQ PKTTTNCAGN SCYKKTWSDH RGTIIERGCG CPQVKSGIKL ECCHTNECNN