ID   3S1ED_LATSE             Reviewed;          83 AA.
AC   Q9YGX1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Short neurotoxin OKI-Ed;
DE   Flags: Precursor;
OS   Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda
OS   semifasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=9427847; DOI=10.1016/s0079-6603(08)61036-3;
RA   Ohno M., Menez R., Ogawa T., Danse J.M., Shimohigashi Y., Fromen C.,
RA   Ducancel F., Zinn-Justin S., Le Du M.H., Boulain J.-C., Tamiya T.,
RA   Menez A.;
RT   "Molecular evolution of snake toxins: is the functional diversity of snake
RT   toxins associated with a mechanism of accelerated evolution?";
RL   Prog. Nucleic Acid Res. Mol. Biol. 59:307-364(1998).
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}.
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DR   EMBL; AB017928; BAA75748.1; -; mRNA.
DR   AlphaFoldDB; Q9YGX1; -.
DR   SMR; Q9YGX1; -.
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..83
FT                   /note="Short neurotoxin OKI-Ed"
FT                   /id="PRO_0000316171"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        38..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        64..75
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        76..81
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ   SEQUENCE   83 AA;  9394 MW;  232E65AE389F0700 CRC64;
     MKTLLLTLVV VTIVCLDLGY TRRCFNQQSS EPQTNKSCPP GENSCYRKQW RDHRGTIIER
     GCGCPTVKPG IKLRCCESED CNN