3L23_NAJNA
ID 3L23_NAJNA Reviewed; 71 AA.
AC P25671;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Long neurotoxin 3;
DE AltName: Full=Toxin C {ECO:0000303|Ref.1};
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Ohta M., Sasaki T., Hayashi K.;
RT "The primary structure of toxin C from the venom of the Indian cobra (Naja
RT naja).";
RL Chem. Pharm. Bull. 29:1458-1475(1981).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=1939183; DOI=10.2210/pdb2ctx/pdb;
RA Betzel C., Lange G., Pal G.P., Wilson K.S., Maelicke A., Saenger W.;
RT "The refined crystal structure of alpha-cobratoxin from Naja naja siamensis
RT at 2.4-A resolution.";
RL J. Biol. Chem. 266:21530-21536(1991).
CC -!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and
CC neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC inhibits acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular and neuronal transmission.
CC {ECO:0000250|UniProtKB:P60615}.
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 0.10 to 0.15 mg/kg by subcutaneous injection.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR PDB; 2CTX; X-ray; 2.40 A; A=1-71.
DR PDBsum; 2CTX; -.
DR AlphaFoldDB; P25671; -.
DR SMR; P25671; -.
DR EvolutionaryTrace; P25671; -.
DR Proteomes; UP000694559; 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 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Reference proteome; Secreted; Toxin.
FT CHAIN 1..71
FT /note="Long neurotoxin 3"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000093549"
FT DISULFID 3..20
FT /evidence="ECO:0000269|PubMed:1939183,
FT ECO:0007744|PDB:2CTX"
FT DISULFID 14..41
FT /evidence="ECO:0000269|PubMed:1939183,
FT ECO:0007744|PDB:2CTX"
FT DISULFID 26..30
FT /evidence="ECO:0000269|PubMed:1939183,
FT ECO:0007744|PDB:2CTX"
FT DISULFID 45..56
FT /evidence="ECO:0000269|PubMed:1939183,
FT ECO:0007744|PDB:2CTX"
FT DISULFID 57..62
FT /evidence="ECO:0000269|PubMed:1939183,
FT ECO:0007744|PDB:2CTX"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2CTX"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2CTX"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:2CTX"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:2CTX"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:2CTX"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2CTX"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2CTX"
SQ SEQUENCE 71 AA; 7833 MW; 67A5A57A85E9AC33 CRC64;
IRCFITPDIT SKDCPNGHVC YTKTWCDAFC SIRGKRVDLG CAATCPTVKT GVDIQCCSTD
DCDPFPTRKR P