3S11_DENPO
ID 3S11_DENPO Reviewed; 60 AA.
AC P01416;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Short neurotoxin 1;
DE AltName: Full=Neurotoxin alpha;
OS Dendroaspis polylepis polylepis (Black mamba).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8620;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=5033401; DOI=10.1016/s0021-9258(19)45135-1;
RA Strydom D.J.;
RT "Snake venom toxins. The amino acid sequences of two toxins from
RT Dendroaspis polylepis polylepis (black mamba) venom.";
RL J. Biol. Chem. 247:4029-4042(1972).
RN [2]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=2847926; DOI=10.1111/j.1432-1033.1988.tb14376.x;
RA Labhardt A.L., Hunziker-Kwik E.H., Wuethrich K.;
RT "Secondary structure determination for alpha-neurotoxin from Dendroaspis
RT polylepis polylepis based on sequence-specific 1H-nuclear-magnetic-
RT resonance assignments.";
RL Eur. J. Biochem. 177:295-305(1988).
RN [3]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=1433289; DOI=10.1016/0022-2836(92)90525-o;
RA Brown L.R., Wuethrich K.;
RT "Nuclear magnetic resonance solution structure of the alpha-neurotoxin from
RT the black mamba (Dendroaspis polylepis polylepis).";
RL J. Mol. Biol. 227:1118-1135(1992).
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|PubMed:5033401}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 0.09 mg/kg by subcutaneous injection.
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 PIR; A01686; N1EP1D.
DR PDB; 1NTX; NMR; -; A=1-60.
DR PDBsum; 1NTX; -.
DR AlphaFoldDB; P01416; -.
DR BMRB; P01416; -.
DR SMR; P01416; -.
DR EvolutionaryTrace; P01416; -.
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..60
FT /note="Short neurotoxin 1"
FT /evidence="ECO:0000269|PubMed:5033401"
FT /id="PRO_0000093574"
FT DISULFID 3..22
FT /evidence="ECO:0000269|PubMed:1433289,
FT ECO:0000269|PubMed:2847926, ECO:0000312|PDB:1NTX"
FT DISULFID 17..39
FT /evidence="ECO:0000269|PubMed:1433289,
FT ECO:0000269|PubMed:2847926, ECO:0000312|PDB:1NTX"
FT DISULFID 41..52
FT /evidence="ECO:0000269|PubMed:1433289,
FT ECO:0000269|PubMed:2847926, ECO:0000312|PDB:1NTX"
FT DISULFID 53..58
FT /evidence="ECO:0000269|PubMed:1433289,
FT ECO:0000269|PubMed:2847926, ECO:0000312|PDB:1NTX"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1NTX"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1NTX"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1NTX"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:1NTX"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1NTX"
SQ SEQUENCE 60 AA; 6915 MW; E68D6A44410645AC CRC64;
RICYNHQSTT RATTKSCEEN SCYKKYWRDH RGTIIERGCG CPKVKPGVGI HCCQSDKCNY