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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21212 PublicationsAdd
BLAST
Chaini22 – 9574Alpha-bungarotoxin isoform A31PRO_0000035406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 interactions.
MINTiMINT-5223718.

Chemistry

BindingDBiP60615.

Structurei

Secondary structure

1
95
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi29 – 313Combined sources
Beta strandi33 – 364Combined sources
Beta strandi38 – 425Combined sources
Beta strandi43 – 497Combined sources
Beta strandi51 – 533Combined sources
Helixi54 – 574Combined sources
Beta strandi59 – 6810Combined sources
Beta strandi71 – 755Combined sources
Beta strandi77 – 815Combined sources
Beta strandi83 – 853Combined sources
Beta strandi91 – 933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-95.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481M → V in AAC83985 (PubMed:9837992).Curated
Sequence conflicti53 – 531F → S in AAC83996 (PubMed:9837992).Curated
Sequence conflicti56 – 561S → N in AAC83986 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83982 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83983 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83984 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83985 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83986 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83987 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83988 (PubMed:9837992).Curated
Sequence conflicti57 – 571R → K in AAC83989 (PubMed:9837992).Curated
Sequence conflicti68 – 681T → P in AAC83996 (PubMed:9837992).Curated
Sequence conflicti70 – 701P → S in AAC83987 (PubMed:9837992).Curated
Sequence conflicti72 – 721K → E in AAC83996 (PubMed:9837992).Curated
Sequence conflicti72 – 721K → E in AAC83997 (PubMed:9837992).Curated
Sequence conflicti73 – 731K → R in AAC83988 (PubMed:9837992).Curated
Sequence conflicti79 – 791T → S in AAC83996 (PubMed:9837992).Curated
Sequence conflicti79 – 791T → S in AAC83997 (PubMed:9837992).Curated
Sequence conflicti85 – 851K → Q in AAC83990 (PubMed:9837992).Curated
Sequence conflicti87 – 871N → H in AAC83990 (PubMed:9837992).Curated

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
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. Positions 22-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP60615. 4 interactions.
MINTiMINT-5223718.

Chemistry

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: September 7, 2016
This is version 85 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.