ID   3S12_LATCO              Reviewed;          83 AA.
AC   P10457; Q9PRJ0; Q9PRJ7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Short neurotoxin II;
DE   Flags: Precursor;
OS   Laticauda colubrina (Yellow-lipped sea krait) (Banded sea krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Kariya Y., Araki S., Agu H., Tamiya T., Tsuchiya T.;
RT   "Classification of sea snakes in genus Laticauda by nucleotide sequences
RT   encoding short chain neurotoxins.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-83, AND SUBCELLULAR LOCATION.
RC   STRAIN=Japanese, and Philippines; TISSUE=Venom;
RA   Tamiya N., Sato A., Kim H.S., Teruuchi T., Takasaki C., Ishikawa Y.,
RA   Guinea M.L., McCoy M., Heatwole H., Cogger H.G.;
RT   "Neurotoxins of sea snakes genus Laticauda.";
RL   Toxicon 21 Suppl. 3:445-447(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|Ref.1}.
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; AB017933; BAA75753.1; -; mRNA.
DR   EMBL; AB017934; BAA75754.1; -; mRNA.
DR   EMBL; AB017935; BAA75755.1; -; mRNA.
DR   EMBL; AB017936; BAA75756.1; -; mRNA.
DR   EMBL; AB017937; BAA75757.1; -; mRNA.
DR   EMBL; AB017938; BAA75758.1; -; mRNA.
DR   EMBL; AB017939; BAA75759.1; -; mRNA.
DR   EMBL; AB017941; BAA75761.1; -; mRNA.
DR   PIR; B25866; B25866.
DR   AlphaFoldDB; P10457; -.
DR   SMR; P10457; -.
DR   PRIDE; P10457; -.
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; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           22..83
FT                   /note="Short neurotoxin II"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000035437"
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"
FT   VARIANT         13
FT                   /note="V -> M"
SQ   SEQUENCE   83 AA;  9314 MW;  45FCDA72F9B8A5B4 CRC64;
     MKTLLLTLVV VTVVCLDLGY TRRCYNQQSS QPKTTKSCPP GENSCYNKQW RDHRGSITER
     GCGCPTVKPG IKLRCCESED CNN