3S32_PSETE
ID 3S32_PSETE Reviewed; 79 AA.
AC Q9W7K1;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Short neurotoxin 2;
DE Short=SNTX2;
DE AltName: Full=Alpha-neurotoxin 2;
DE Flags: Precursor;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom gland;
RX PubMed=10518793; DOI=10.1046/j.1432-1327.1999.00800.x;
RA Gong N.L., Armugam A., Jeyaseelan K.;
RT "Postsynaptic short-chain neurotoxins from Pseudonaja textilis: cDNA
RT cloning, expression and protein characterization.";
RL Eur. J. Biochem. 265:982-989(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=10818230; DOI=10.1016/s0014-5793(00)01549-0;
RA Gong N.L., Armugam A., Jeyaseelan K.;
RT "Molecular cloning, characterization and evolution of the genes encoding a
RT new group of short-chain alpha-neurotoxins in an Australian elapid,
RT Pseudonaja textilis.";
RL FEBS Lett. 473:303-310(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA Lavin M.F.;
RT "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT textilis.";
RL Mol. Cell. Proteomics 5:379-389(2006).
CC -!- FUNCTION: Binds with high affinity to muscle nicotinic acetylcholine
CC receptor (nAChR) and hinders acetylcholine binding to the receptor,
CC thereby impairing neuromuscular transmission. Competes with the binding
CC of alpha-bungarotoxin on muscle AChR (from Torpedo) with an IC(50) of
CC 0.30 uM. Causes muscle paralysis, spasms and increased respiration.
CC {ECO:0000269|PubMed:10518793}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 1 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:10518793}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type III alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR EMBL; AF082976; AAD40968.1; -; mRNA.
DR EMBL; AF204970; AAF75221.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9W7K1; -.
DR SMR; Q9W7K1; -.
DR Proteomes; UP000472273; 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 SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
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..79
FT /note="Short neurotoxin 2"
FT /id="PRO_0000035462"
FT DISULFID 24..41
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 34..59
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 63..71
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 72..77
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 79 AA; 8596 MW; 2FA1B458375215BD CRC64;
MKTLLLTLVM VTIMCLDLGY TLTCYKGYHD TVVCKPHETI CYRYLIPATH GNAIPARGCG
TSCPGGNHPV CCSTDLCNK
