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Protein

Gamma-bungarotoxin

Gene
N/A
Organism
Bungarus multicinctus (Many-banded krait)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits M2 muscarinic acetylcholine receptor (CHRM2)-blocking activity, but has a weak binding activity toward nicotinic AChR. Moreover, it inhibits collagen-induced platelet aggregation.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cell adhesion impairing toxin, G-protein coupled acetylcholine receptor impairing toxin, G-protein coupled receptor impairing toxin, Hemostasis impairing toxin, Neurotoxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-bungarotoxin
Alternative name(s):
Long neurotoxin homolog NTL2I
OrganismiBungarus multicinctus (Many-banded krait)
Taxonomic identifieri8616 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.15 mg/kg by intravenous injection into mice.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 8968Gamma-bungarotoxinPRO_0000035425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 451 Publication
Disulfide bondi27 ↔ 321 Publication
Disulfide bondi38 ↔ 661 Publication
Disulfide bondi70 ↔ 811 Publication
Disulfide bondi82 ↔ 871 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Beta strandi45 – 484Combined sources
Beta strandi54 – 563Combined sources
Beta strandi63 – 664Combined sources
Beta strandi68 – 725Combined sources
Beta strandi75 – 773Combined sources
Beta strandi82 – 865Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MR6NMR-A22-89[»]
ProteinModelPortaliQ9YGJ0.
SMRiQ9YGJ0. Positions 22-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YGJ0.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 563Cell attachment sitePROSITE-ProRule annotation

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9YGJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLTLVV VTIVCLDLGY TMQCKTCSFY TCPNSETCPD GKNICVKRSW
60 70 80
TAVRGDGPKR EIRRECAATC PPSKLGLTVF CCTTDNCNH
Length:89
Mass (Da):9,826
Last modified:May 1, 1999 - v1
Checksum:i368E86E7BA19D49C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → E in AAD41806 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006135 mRNA. Translation: CAA06885.1.
AF142324 mRNA. Translation: AAD41806.1.
AJ416991 Genomic DNA. Translation: CAD01082.1.
PIRiA59187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006135 mRNA. Translation: CAA06885.1.
AF142324 mRNA. Translation: AAD41806.1.
AJ416991 Genomic DNA. Translation: CAD01082.1.
PIRiA59187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MR6NMR-A22-89[»]
ProteinModelPortaliQ9YGJ0.
SMRiQ9YGJ0. Positions 22-89.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553.

Miscellaneous databases

EvolutionaryTraceiQ9YGJ0.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and sequence analysis of six neurotoxin-like proteins from Chinese continental banded krait."
    Qian Y.-C., Fan C.-Y., Gong Y., Yang S.-L.
    Biochem. Mol. Biol. Int. 46:821-828(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. Cai Q., He Z., Gong Y., Yang S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  3. "Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) gamma-bungarotoxin."
    Chang L.-S., Chung C., Wu B.-N., Yang C.-C.
    J. Protein Chem. 21:223-229(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Tissue: Liver.
  4. "Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus."
    Aird S.D., Womble G.C., Yates J.R. III, Griffin P.R.
    Toxicon 37:609-625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-89, LETHAL DOSE, SUBCELLULAR LOCATION.
    Tissue: Venom.
  5. "Solution structure of gamma-bungarotoxin: the functional significance of amino acid residues flanking the RGD motif in integrin binding."
    Shiu J.-H., Chen C.-Y., Chang L.-S., Chen Y.-C., Chen Y.-C., Lo Y.-H., Liu Y.-C., Chuang W.-J.
    Proteins 57:839-849(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-89, DISULFIDE BOND.

Entry informationi

Entry namei3NO5I_BUNMU
AccessioniPrimary (citable) accession number: Q9YGJ0
Secondary accession number(s): Q9W796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 1999
Last modified: October 14, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.