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3S1CC_NAJAT
ID   3S1CC_NAJAT             Reviewed;          82 AA.
AC   P80958; O42285; Q6S468; Q9YHU9; Q9YHV0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Cobrotoxin-b;
DE            Short=CBT-b;
DE   AltName: Full=Atratoxin-b;
DE   AltName: Full=Cobrotoxin III;
DE            Short=CBT-III;
DE   AltName: Full=Cobrotoxin IV;
DE            Short=CBT IV;
DE   AltName: Full=NT3;
DE   AltName: Full=Short neurotoxin;
DE   Flags: Precursor;
OS   Naja atra (Chinese cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-82, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Liver, and Venom;
RX   PubMed=9498573; DOI=10.1093/oxfordjournals.jbchem.a021889;
RA   Chang L.-S., Chou Y.-C., Lin S.-R., Wu B.-N., Lin J., Hong E., Sun Y.-J.,
RA   Hsiao C.-D.;
RT   "A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra)
RT   venom: purification, characterization, and gene organization.";
RL   J. Biochem. 122:1252-1259(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 67.
RC   TISSUE=Venom gland;
RA   Chu R.C., Yang C.-C.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-82.
RC   TISSUE=Venom gland;
RA   Pan H., Wu J., Yang G.Z., Wu X.F.;
RT   "Molecular cloning, sequence analysis and expression of cobrotoxin from
RT   Naja naja atra.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-82, X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS)
RP   OF 22-82, AND DISULFIDE BOND.
RC   TISSUE=Venom gland;
RX   PubMed=15252034; DOI=10.1074/jbc.m403863200;
RA   Lou X., Liu Q., Tu X., Wang J., Teng M., Niu L., Schuller D.J., Huang Q.,
RA   Hao Q.;
RT   "The atomic resolution crystal structure of atratoxin determined by single
RT   wavelength anomalous diffraction phasing.";
RL   J. Biol. Chem. 279:39094-39104(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 22-35, STRUCTURE BY NMR OF 22-82, TOXIC DOSE, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=12777767; DOI=10.1107/s0907444903005687;
RA   Lou X., Tu X., Pan G., Xu C., Fan R., Lu W., Deng W., Rao P., Teng M.,
RA   Niu L.;
RT   "Purification, N-terminal sequencing, crystallization and preliminary
RT   structural determination of atratoxin-b, a short-chain alpha-neurotoxin
RT   from Naja atra venom.";
RL   Acta Crystallogr. D 59:1038-1042(2003).
CC   -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC       inhibit acetylcholine from binding to the receptor, thereby impairing
CC       neuromuscular transmission. Produces peripheral paralysis by blocking
CC       neuromuscular transmission at the postsynaptic site. Has a lower
CC       toxicity than cobrotoxin. {ECO:0000269|PubMed:9498573}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9498573}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6950; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12777767};
CC   -!- TOXIC DOSE: LD(50) is 0.18 mg/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:12777767}.
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; Y13399; CAA73829.2; -; Genomic_DNA.
DR   EMBL; AF031472; AAB86636.1; -; mRNA.
DR   EMBL; AF088997; AAD09179.1; -; mRNA.
DR   EMBL; AF088998; AAD09180.1; -; mRNA.
DR   EMBL; AY471579; AAR33036.1; -; mRNA.
DR   PIR; JC5892; JC5892.
DR   PDB; 1ONJ; X-ray; 1.55 A; A=22-82.
DR   PDB; 1VB0; X-ray; 0.92 A; A=22-82.
DR   PDBsum; 1ONJ; -.
DR   PDBsum; 1VB0; -.
DR   AlphaFoldDB; P80958; -.
DR   SMR; P80958; -.
DR   EvolutionaryTrace; P80958; -.
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; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:12777767,
FT                   ECO:0000269|PubMed:9498573"
FT   CHAIN           22..82
FT                   /note="Cobrotoxin-b"
FT                   /evidence="ECO:0000269|PubMed:9498573"
FT                   /id="PRO_0000035456"
FT   DISULFID        24..44
FT                   /evidence="ECO:0000269|PubMed:12777767,
FT                   ECO:0000269|PubMed:15252034, ECO:0000312|PDB:1ONJ,
FT                   ECO:0000312|PDB:1VB0"
FT   DISULFID        38..61
FT                   /evidence="ECO:0000269|PubMed:12777767,
FT                   ECO:0000269|PubMed:15252034, ECO:0000312|PDB:1ONJ,
FT                   ECO:0000312|PDB:1VB0"
FT   DISULFID        63..74
FT                   /evidence="ECO:0000269|PubMed:12777767,
FT                   ECO:0000269|PubMed:15252034, ECO:0000312|PDB:1ONJ,
FT                   ECO:0000312|PDB:1VB0"
FT   DISULFID        75..80
FT                   /evidence="ECO:0000269|PubMed:12777767,
FT                   ECO:0000269|PubMed:15252034, ECO:0000312|PDB:1ONJ,
FT                   ECO:0000312|PDB:1VB0"
FT   CONFLICT        22
FT                   /note="L -> M (in Ref. 3; AAD09179/AAD09180)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="T -> A (in Ref. 3; AAD09179)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="T -> TI (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36..39
FT                   /note="KTCS -> TGCSG (in Ref. 3; AAD09180)"
FT                   /evidence="ECO:0000305"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:1VB0"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1VB0"
FT   STRAND          44..51
FT                   /evidence="ECO:0007829|PDB:1VB0"
FT   STRAND          54..62
FT                   /evidence="ECO:0007829|PDB:1VB0"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:1VB0"
FT   TURN            78..81
FT                   /evidence="ECO:0007829|PDB:1VB0"
SQ   SEQUENCE   82 AA;  9139 MW;  1FFA21189C08B6E8 CRC64;
     MKTLLLTLLV VTIVCLDLGY TLECHNQQSS QTPTTKTCSG ETNCYKKWWS DHRGTIIERG
     CGCPKVKPGV NLNCCTTDRC NN
 
 
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