3S11_NAJPA
ID 3S11_NAJPA Reviewed; 61 AA.
AC P01426;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Short neurotoxin 1;
DE AltName: Full=Neurotoxin alpha;
DE Short=Toxin alpha {ECO:0000303|PubMed:9305882};
OS Naja pallida (Red spitting cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8658;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Eaker D.L., Porath J.;
RT "The amino acid sequence of a neurotoxin from Naja nigricollis venom.";
RL Jpn. J. Microbiol. 11:353-355(1967).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9305882; DOI=10.1074/jbc.272.39.24279;
RA Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P.,
RA Bertrand D., Menez A.;
RT "Only snake curaremimetic toxins with a fifth disulfide bond have high
RT affinity for the neuronal alpha7 nicotinic receptor.";
RL J. Biol. Chem. 272:24279-24286(1997).
RN [3]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=1332755; DOI=10.1021/bi00161a011;
RA Zinn-Justin S., Roumestand C., Gilquin B., Bontems F., Menez A., Toma F.;
RT "Three-dimensional solution structure of a curaremimetic toxin from Naja
RT nigricollis venom: a proton NMR and molecular modeling study.";
RL Biochemistry 31:11335-11347(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=12538890; DOI=10.1110/ps.0227703;
RA Gilquin B., Bourgoin M., Menez R., Le Du M.-H., Servent D., Zinn-Justin S.,
RA Menez A.;
RT "Motions and structural variability within toxins: implication for their
RT use as scaffolds for protein engineering.";
RL Protein Sci. 12:266-277(2003).
CC -!- FUNCTION: Binds with high affinity to muscular nicotinic acetylcholine
CC receptors (nAChRs) (tested on Torpedo marmorata AChR, Kd=0.07 nM) and
CC with low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric
CC receptor, Kd=3 uM) and inhibit acetylcholine from binding to the
CC receptor, thereby impairing neuromuscular transmission
CC (PubMed:9305882). Produces peripheral paralysis by blocking
CC neuromuscular transmission at the postsynaptic site.
CC {ECO:0000269|PubMed:9305882}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- TOXIC DOSE: LD(50) is 0.036 mg/kg by subcutaneous injection.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The venom of this snake was originally thought to be that of
CC N.nigricollis. {ECO:0000305}.
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DR PIR; A01695; N1NJ1B.
DR PDB; 1IQ9; X-ray; 1.80 A; A=1-61.
DR PDB; 1NEA; NMR; -; A=1-61.
DR PDB; 3NDS; X-ray; 1.20 A; A=1-61.
DR PDBsum; 1IQ9; -.
DR PDBsum; 1NEA; -.
DR PDBsum; 3NDS; -.
DR AlphaFoldDB; P01426; -.
DR SMR; P01426; -.
DR EvolutionaryTrace; P01426; -.
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 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..61
FT /note="Short neurotoxin 1"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000093608"
FT DISULFID 3..23
FT /evidence="ECO:0000269|PubMed:12538890,
FT ECO:0000269|PubMed:1332755, ECO:0000312|PDB:1IQ9,
FT ECO:0000312|PDB:1NEA, ECO:0000312|PDB:3NDS"
FT DISULFID 17..40
FT /evidence="ECO:0000269|PubMed:12538890,
FT ECO:0000269|PubMed:1332755, ECO:0000312|PDB:1IQ9,
FT ECO:0000312|PDB:1NEA, ECO:0000312|PDB:3NDS"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:12538890,
FT ECO:0000269|PubMed:1332755, ECO:0000312|PDB:1IQ9,
FT ECO:0000312|PDB:1NEA, ECO:0000312|PDB:3NDS"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:12538890,
FT ECO:0000269|PubMed:1332755, ECO:0000312|PDB:1IQ9,
FT ECO:0000312|PDB:1NEA, ECO:0000312|PDB:3NDS"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3NDS"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3NDS"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3NDS"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3NDS"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:3NDS"
SQ SEQUENCE 61 AA; 6795 MW; 751D80011221C3C1 CRC64;
LECHNQQSSQ PPTTKTCPGE TNCYKKVWRD HRGTIIERGC GCPTVKPGIK LNCCTTDKCN
N
