3S13_LATLA
ID 3S13_LATLA Reviewed; 83 AA.
AC Q9YGC4; Q7T2I2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Short neurotoxin OKI-01/OKI-19;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=12957382; DOI=10.1016/s0378-1119(03)00637-1;
RA Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T.;
RT "Molecular evolution and diversification of snake toxin genes, revealed by
RT analysis of intron sequences.";
RL Gene 313:111-118(2003).
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; AB017964; BAA75784.1; -; mRNA.
DR EMBL; AB017960; BAA75780.1; -; mRNA.
DR EMBL; AB098534; BAC78206.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9YGC4; -.
DR SMR; Q9YGC4; -.
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 3: Inferred from homology;
KW Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..83
FT /note="Short neurotoxin OKI-01/OKI-19"
FT /id="PRO_0000035444"
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; 9261 MW; 3F2C2B7B2BACD5F7 CRC64;
MKTLLLTLVV VTIVCLDLGY TRRCFNHPSS QPQTNKSCPP GENSCYNKQW RDHRGTITER
GCGCPTVKPG IKLTCCQSED CNN