3S1CB_NAJNA
ID 3S1CB_NAJNA Reviewed; 83 AA.
AC Q9PTT0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cobrotoxin homolog;
DE AltName: Full=Short neurotoxin;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Qin C., Zhiyong H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR OF 22-83, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8443154; DOI=10.1021/bi00060a002;
RA Yu C., Bhaskaran R., Chuang L.-C., Yang C.-C.;
RT "Solution conformation of cobrotoxin: a nuclear magnetic resonance and
RT hybrid distance geometry-dynamical simulated annealing study.";
RL Biochemistry 32:2131-2136(1993).
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:8443154}.
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; AF068052; AAF21774.1; -; mRNA.
DR PDB; 1COD; NMR; -; A=22-83.
DR PDBsum; 1COD; -.
DR AlphaFoldDB; Q9PTT0; -.
DR BMRB; Q9PTT0; -.
DR SMR; Q9PTT0; -.
DR EvolutionaryTrace; Q9PTT0; -.
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; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8443154"
FT CHAIN 22..83
FT /note="Cobrotoxin homolog"
FT /evidence="ECO:0000269|PubMed:8443154"
FT /id="PRO_0000035455"
FT SITE 54
FT /note="May be critical for toxicity"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="May be critical for toxicity"
FT /evidence="ECO:0000250"
FT DISULFID 24..45
FT /evidence="ECO:0000269|PubMed:8443154,
FT ECO:0000312|PDB:1COD"
FT DISULFID 38..62
FT /evidence="ECO:0000269|PubMed:8443154,
FT ECO:0000312|PDB:1COD"
FT DISULFID 64..75
FT /evidence="ECO:0000269|PubMed:8443154,
FT ECO:0000312|PDB:1COD"
FT DISULFID 76..81
FT /evidence="ECO:0000269|PubMed:8443154,
FT ECO:0000312|PDB:1COD"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1COD"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1COD"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1COD"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1COD"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1COD"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1COD"
SQ SEQUENCE 83 AA; 9262 MW; 4DDC0DDC387BD0F2 CRC64;
METLLLTLLV VTIVCLDLGY TLECHNQQSS QTPTTTGCSG GETNCYKKRW RDHRGYRTER
GCGCPSVKNG IEINCCTTDR CNN