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Protein

Alpha-bungarotoxin isoform A31

Gene
N/A
Organism
Bungarus multicinctus (Many-banded krait)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 µM).2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Protein family/group databases

TCDBi1.C.74.1.2. the snake cytotoxin (sct) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-bungarotoxin isoform A31
Short name:
Alpha-BTX A31
Short name:
Alpha-Bgt(A31)
Short name:
BGTX A31
Alternative name(s):
Long neurotoxin 1
OrganismiBungarus multicinctus (Many-banded krait)
Taxonomic identifieri8616 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.3 mg/kg by subcutaneous injection.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 212 PublicationsAdd BLAST21
ChainiPRO_000003540622 – 95Alpha-bungarotoxin isoform A31Add BLAST74

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 44
Disulfide bondi37 ↔ 65
Disulfide bondi50 ↔ 54
Disulfide bondi69 ↔ 80
Disulfide bondi81 ↔ 86

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Interactioni

Subunit structurei

Monomer in solution, homodimer in crystal state.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Chrna7Q059414EBI-7516391,EBI-79422From a different organism.

Protein-protein interaction databases

IntActiP60615. 4 interactors.
MINTiMINT-5223718.

Chemistry databases

BindingDBiP60615.

Structurei

Secondary structure

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Beta strandi29 – 31Combined sources3
Beta strandi33 – 36Combined sources4
Beta strandi38 – 42Combined sources5
Beta strandi43 – 49Combined sources7
Beta strandi51 – 53Combined sources3
Helixi54 – 57Combined sources4
Beta strandi59 – 68Combined sources10
Beta strandi71 – 75Combined sources5
Beta strandi77 – 81Combined sources5
Beta strandi83 – 85Combined sources3
Beta strandi91 – 93Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABTNMR-A22-95[»]
1BXPNMR-A22-95[»]
1HAANMR-A22-95[»]
1HAJNMR-A22-95[»]
1HC9X-ray1.80B22-95[»]
1HOYNMR-A22-95[»]
1IDGNMR-A22-95[»]
1IDHNMR-A22-95[»]
1IDINMR-A22-95[»]
1IDLNMR-A22-95[»]
1IK8NMR-A22-95[»]
1IKCNMR-A22-95[»]
1JBDNMR-A22-95[»]
1KC4NMR-A22-95[»]
1KFHNMR-A22-95[»]
1KL8NMR-A22-95[»]
1L4WNMR-A22-95[»]
1LJZNMR-A22-95[»]
1LK1model-C/F22-95[»]
1RGJNMR-A22-95[»]
2ABXX-ray2.50A/B22-95[»]
2BTXNMR-A22-95[»]
ProteinModelPortaliP60615.
SMRiP60615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60615.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

CDDicd00206. snake_toxin. 1 hit.
InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLTLVV VTIVCLDLGY TIVCHTTATS PISAVTCPPG ENLCYRKMWC
60 70 80 90
DAFCSSRGKV VELGCAATCP SKKPYEEVTC CSTDKCNPHP KQRPG
Length:95
Mass (Da):10,285
Last modified:March 15, 2004 - v1
Checksum:i589B26743ABBA5E4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48M → V in AAC83985 (PubMed:9837992).Curated1
Sequence conflicti53F → S in AAC83996 (PubMed:9837992).Curated1
Sequence conflicti56S → N in AAC83986 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83982 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83983 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83984 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83985 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83986 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83987 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83988 (PubMed:9837992).Curated1
Sequence conflicti57R → K in AAC83989 (PubMed:9837992).Curated1
Sequence conflicti68T → P in AAC83996 (PubMed:9837992).Curated1
Sequence conflicti70P → S in AAC83987 (PubMed:9837992).Curated1
Sequence conflicti72K → E in AAC83996 (PubMed:9837992).Curated1
Sequence conflicti72K → E in AAC83997 (PubMed:9837992).Curated1
Sequence conflicti73K → R in AAC83988 (PubMed:9837992).Curated1
Sequence conflicti79T → S in AAC83996 (PubMed:9837992).Curated1
Sequence conflicti79T → S in AAC83997 (PubMed:9837992).Curated1
Sequence conflicti85K → Q in AAC83990 (PubMed:9837992).Curated1
Sequence conflicti87N → H in AAC83990 (PubMed:9837992).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056400 mRNA. Translation: AAC83981.1.
AF056401 Genomic DNA. Translation: AAC83982.1.
AF056402 mRNA. Translation: AAC83983.1.
AF056403 mRNA. Translation: AAC83984.1.
AF056404 mRNA. Translation: AAC83985.1.
AF056405 mRNA. Translation: AAC83986.1.
AF056406 mRNA. Translation: AAC83987.1.
AF056407 mRNA. Translation: AAC83988.1.
AF056408 mRNA. Translation: AAC83989.1.
AF056409 mRNA. Translation: AAC83990.1.
AF056410 mRNA. Translation: AAC83991.1.
AF056411 mRNA. Translation: AAC83992.1.
AF056412 mRNA. Translation: AAC83993.1.
AF056413 mRNA. Translation: AAC83994.1.
AF056415 mRNA. Translation: AAC83996.1.
AF056416 mRNA. Translation: AAC83997.1.
Y17694 Genomic DNA. Translation: CAB51844.1.
Y17058 mRNA. Translation: CAB51842.1.
X91990 mRNA. Translation: CAA63045.1.
PIRiA31519. N2KF1U.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056400 mRNA. Translation: AAC83981.1.
AF056401 Genomic DNA. Translation: AAC83982.1.
AF056402 mRNA. Translation: AAC83983.1.
AF056403 mRNA. Translation: AAC83984.1.
AF056404 mRNA. Translation: AAC83985.1.
AF056405 mRNA. Translation: AAC83986.1.
AF056406 mRNA. Translation: AAC83987.1.
AF056407 mRNA. Translation: AAC83988.1.
AF056408 mRNA. Translation: AAC83989.1.
AF056409 mRNA. Translation: AAC83990.1.
AF056410 mRNA. Translation: AAC83991.1.
AF056411 mRNA. Translation: AAC83992.1.
AF056412 mRNA. Translation: AAC83993.1.
AF056413 mRNA. Translation: AAC83994.1.
AF056415 mRNA. Translation: AAC83996.1.
AF056416 mRNA. Translation: AAC83997.1.
Y17694 Genomic DNA. Translation: CAB51844.1.
Y17058 mRNA. Translation: CAB51842.1.
X91990 mRNA. Translation: CAA63045.1.
PIRiA31519. N2KF1U.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABTNMR-A22-95[»]
1BXPNMR-A22-95[»]
1HAANMR-A22-95[»]
1HAJNMR-A22-95[»]
1HC9X-ray1.80B22-95[»]
1HOYNMR-A22-95[»]
1IDGNMR-A22-95[»]
1IDHNMR-A22-95[»]
1IDINMR-A22-95[»]
1IDLNMR-A22-95[»]
1IK8NMR-A22-95[»]
1IKCNMR-A22-95[»]
1JBDNMR-A22-95[»]
1KC4NMR-A22-95[»]
1KFHNMR-A22-95[»]
1KL8NMR-A22-95[»]
1L4WNMR-A22-95[»]
1LJZNMR-A22-95[»]
1LK1model-C/F22-95[»]
1RGJNMR-A22-95[»]
2ABXX-ray2.50A/B22-95[»]
2BTXNMR-A22-95[»]
ProteinModelPortaliP60615.
SMRiP60615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP60615. 4 interactors.
MINTiMINT-5223718.

Chemistry databases

BindingDBiP60615.

Protein family/group databases

TCDBi1.C.74.1.2. the snake cytotoxin (sct) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553.

Miscellaneous databases

EvolutionaryTraceiP60615.

Family and domain databases

CDDicd00206. snake_toxin. 1 hit.
InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei3L21A_BUNMU
AccessioniPrimary (citable) accession number: P60615
Secondary accession number(s): P01378
, Q9PRI6, Q9YGD1, Q9YI06, Q9YI07, Q9YI09, Q9YI10, Q9YI11, Q9YI12, Q9YI13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 15, 2004
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:9837992 indicates that a number of mRNA with sequence conflict(s) are produced by RNA editing. This seems not to be the case as discussed in PubMed:10497260.Curated

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.