3S1CB_NAJKA
ID 3S1CB_NAJKA Reviewed; 83 AA.
AC P60771; O13079; P01430; Q4PLR9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Cobrotoxin;
DE Short=CBT;
DE AltName: Full=Short neurotoxin I {ECO:0000303|PubMed:11904231};
DE Short=NT1 {ECO:0000303|PubMed:11904231};
DE Flags: Precursor;
OS Naja kaouthia (Monocled cobra) (Naja siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Yao G.-T., Wei X.-H., Yu L.-X., Wang Z.-S., Feng Y., Song H., Zhang B.-B.;
RT "Cloning and expression of neurotoxin cDNA from Naja naja kaouthia
RT lesson.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 22-83, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=12039691; DOI=10.1016/s1532-0456(02)00049-2;
RA Meng Q.-X., Wang W.-Y., Lu Q.-M., Jin Y., Wei J.-F., Zhu S.-W.,
RA Xiong Y.-L.;
RT "A novel short neurotoxin, cobrotoxin c, from monocellate cobra (Naja
RT kaouthia) venom: isolation and purification, primary and secondary
RT structure determination, and tertiary structure modeling.";
RL Comp. Biochem. Physiol. 132C:113-121(2002).
RN [3]
RP INHIBITORY CONCENTRATION.
RX PubMed=11904231; DOI=10.1016/s0167-4838(01)00326-0;
RA Cheng Y., Meng Q.-X., Wang W.-Y., Wang J.;
RT "Structure-function relationship of three neurotoxins from the venom of
RT Naja kaouthia: a comparison between the NMR-derived structure of NT2 with
RT its homologues, NT1 and NT3.";
RL Biochim. Biophys. Acta 1594:353-363(2002).
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:12039691}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 65 mg/kg by intraperitoneal injection into mice.
CC {ECO:0000269|PubMed:12039691}.
CC -!- MISCELLANEOUS: It inhibits muscle contraction with an IC(50) of 0.04
CC ug/ml. {ECO:0000305|PubMed:11904231}.
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; DQ066882; AAY63884.1; -; mRNA.
DR AlphaFoldDB; P60771; -.
DR BMRB; P60771; -.
DR SMR; P60771; -.
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 Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12039691"
FT CHAIN 22..83
FT /note="Cobrotoxin"
FT /evidence="ECO:0000269|PubMed:12039691"
FT /id="PRO_0000093591"
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:0000250|UniProtKB:P0C1Z0"
FT DISULFID 38..62
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 64..75
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT DISULFID 76..81
FT /evidence="ECO:0000250|UniProtKB:P0C1Z0"
SQ SEQUENCE 83 AA; 9262 MW; 4DD6077C92717052 CRC64;
MKTLLLTLLV VTIVCLDLGY TLECHNQQSS QTPTTTGCSG GETNCYKKRW RDHRGYRTER
GCGCPSVKNG IEINCCTTDR CNN