ID   3S1A_HYDTO              Reviewed;          60 AA.
AC   P0CG02;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Toxin aagardi;
OS   Hydrophis torquatus (West Coast black-headed sea snake) (Chitulia
OS   torquata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX   NCBI_TaxID=747462;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND TOXIC DOSE.
RC   STRAIN=Subsp. aagaardi; TISSUE=Venom;
RX   DOI=10.3390/toxins1020162;
RA   Nagamizu M., Komori Y., Uchiya K.-I., Nikai T., Tu A.T.;
RT   "Isolation and chemical characterization of a toxin isolated from the venom
RT   of the sea snake, Hydrophis torquatus aagardi.";
RL   Toxins 1:162-172(2009).
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|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6591.1; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- TOXIC DOSE: LD(50) is 36 ng/kg by intravenous injection into mice.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CG02; -.
DR   SMR; P0CG02; -.
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; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..60
FT                   /note="Toxin aagardi"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000394533"
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