ID   3S11_HYDLA              Reviewed;          60 AA.
AC   P01437;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Short neurotoxin 1;
DE   AltName: Full=Neurotoxin A;
OS   Hydrophis lapemoides (Persian gulf sea snake) (Aturia lapemoides).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX   NCBI_TaxID=8684;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, 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).
RN   [2]
RP   FUNCTION, AND RECOMBINANT EXPRESSION.
RX   PubMed=30648553; DOI=10.1016/j.bbrc.2019.01.014;
RA   Liu Y., Zhang J., Wang R., Wu Y., Wang W., Xin X., Du M., Cao Y., Zhang H.;
RT   "Identification of novel Kv1.3 targeting venom peptides by a single round
RT   of autocrine-based selection.";
RL   Biochem. Biophys. Res. Commun. 509:954-959(2019).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission (By similarity). The recombinant protein
CC       also barely blocks voltage-gated potassium channel Kv1.3/KCNA3 (2.71%
CC       inhibition at 60 nM of toxin) (PubMed:30648553).
CC       {ECO:0000250|UniProtKB:P60775, ECO:0000269|PubMed:30648553}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6615431}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 0.09 mg/kg by intramuscular injection into mice.
CC       {ECO:0000269|PubMed:6615431}.
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   PIR; A90321; N1EY1H.
DR   AlphaFoldDB; P01437; -.
DR   SMR; P01437; -.
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:0015459; F:potassium 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; Potassium channel impairing toxin; Secreted;
KW   Toxin; Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..60
FT                   /note="Short neurotoxin 1"
FT                   /evidence="ECO:0000269|PubMed:6615431"
FT                   /id="PRO_0000093584"
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;  6777 MW;  4E4212AD1156E8B5 CRC64;
     MTCCNQQSSQ PKTTTNCAES SCYKKTWRDF RGTRIERGCG CPQVKPGIKL ECCHTNECNN