ID   3S1B_LATLA              Reviewed;          83 AA.
AC   P10459; Q9PRJ3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Short neurotoxin B;
DE   Flags: Precursor;
OS   Laticauda laticaudata (Blue-ringed sea krait) (Blue-lipped 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=8630;
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   TISSUE=Venom;
RX   PubMed=3955004; DOI=10.1021/bi00350a019;
RA   Endo T., Nakanishi M., Furukawa S., Joubert F.J., Tamiya N., Hayashi K.;
RT   "Stopped-flow fluorescence studies on binding kinetics of neurotoxins with
RT   acetylcholine receptor.";
RL   Biochemistry 25:395-404(1986).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission.
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; AB017956; BAA75776.1; -; mRNA.
DR   EMBL; AB017959; BAA75779.1; -; mRNA.
DR   EMBL; AB017961; BAA75781.1; -; mRNA.
DR   EMBL; AB017963; BAA75783.1; -; mRNA.
DR   PIR; G25866; G25866.
DR   AlphaFoldDB; P10459; -.
DR   SMR; P10459; -.
DR   Proteomes; UP000694406; Unplaced.
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; Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:3955004"
FT   CHAIN           22..83
FT                   /note="Short neurotoxin B"
FT                   /evidence="ECO:0000269|PubMed:3955004"
FT                   /id="PRO_0000035436"
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;  9264 MW;  3F2A9DCB2A1CD638 CRC64;
     MKTLLLTLVV VTIVCLDLGY TRRCFNHPSS QPQTNKSCPP GENSCYNKQW RDHRGTITER
     GCGCPQVKSG IKLTCCQSDD CNN