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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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000003542522 – 89Gamma-bungarotoxinAdd BLAST68

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Beta strandi45 – 48Combined sources4
Beta strandi54 – 56Combined sources3
Beta strandi63 – 66Combined sources4
Beta strandi68 – 72Combined sources5
Beta strandi75 – 77Combined sources3
Beta strandi82 – 86Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9YGJ0.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi54 – 56Cell attachment sitePROSITE-ProRule annotation3

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

CDDicd00206. snake_toxin. 1 hit.
InterProiIPR003571. Snake_3FTx.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti2K → E in AAD41806 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MR6NMR-A22-89[»]
ProteinModelPortaliQ9YGJ0.
SMRiQ9YGJ0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553.

Miscellaneous databases

EvolutionaryTraceiQ9YGJ0.

Family and domain databases

CDDicd00206. snake_toxin. 1 hit.
InterProiIPR003571. Snake_3FTx.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 71 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.