Beta-bungarotoxin B2 chain precursor - Bungarus multicinctus (Many-banded krait)

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P00989 (IVBI2_BUNMU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Beta-bungarotoxin B2 chain Alternative name(s): Beta-2-bungarotoxin
Organism	Bungarus multicinctus (Many-banded krait)
Taxonomic identifier	8616 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	85 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Beta-2-bungarotoxin is a presynaptic neurotoxin of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels. Ref.1
Subunit structure	Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Contains 1 BPTI/Kunitz inhibitor domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Ionic channel inhibitor Neurotoxin Potassium channel inhibitor Presynaptic neurotoxin Toxin
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	other organism presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	potassium channel inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Ref.4 Ref.5

Chain

25 – 85

Beta-bungarotoxin B2 chain

PRO_0000016864

Regions

Domain

31 – 81

BPTI/Kunitz inhibitor

Amino acid modifications

Disulfide bond

31 ↔ 81

Disulfide bond

40 ↔ 64

Disulfide bond

56 ↔ 77

Disulfide bond

Interchain (with an A chain)

Experimental info

Sequence conflict

Missing AA sequence Ref.4

Sequence conflict

65 – 70

NGNGNH → DGDHGN AA sequence Ref.4

Sequence conflict

82 – 83

LE → EL AA sequence Ref.4

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00989 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: FE95A59AF92BF2AA
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FASTA

9,568

        10         20         30         40         50         60 
MSSGGLLLLL GLLTLCAELT PVSSRKRHPD CDKPPDTKIC QTVVRAFYYK PSAKRCVQFR 

        70         80 
YGGCNGNGNH FKSDHLCRCE CLEYR

« Hide

References

[1]	"Cloning and functional expression of B chains of beta-bungarotoxins from Bungarus multicinctus (Taiwan banded krait)." Wu P.-F., Wu S.-N., Chang C.-C., Chang L.-S. Biochem. J. 334:87-92(1998) [PubMed: 9693106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Venom gland.
[2]	"Divergence of genes encoding B chains of beta-bungarotoxins." Cheng Y.-C., Chen K.-C., Lin S.-K., Chang L.-S. Toxicon 47:322-329(2006) [PubMed: 16457863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Venom gland.
[3]	"Genetic organization of A chain and B chain of beta-bungarotoxin from Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain genes do not share a common origin." Wu P.-F., Chang L.-S. Eur. J. Biochem. 267:4668-4675(2000) [PubMed: 10903499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82. Tissue: Liver.
[4]	"Amino acid sequence of beta 2-bungarotoxin from Bungarus multicinctus venom. The amino acid substitutions in the B chains." Kondo K., Toda H., Narita K., Lee C.-Y. J. Biochem. 91:1519-1530(1982) [PubMed: 7096304] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-85. Tissue: Venom.
[5]	"The non-phospholipase A2 subunit of beta-bungarotoxin plays an important role in the phospholipase A2-independent neurotoxic effect: characterization of three isotoxins with a common phospholipase A2 subunit." Chu C.C., Chu S.T., Chen S.W., Chen Y.H. Biochem. J. 303:171-176(1994) [PubMed: 7945237] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-63.
[6]	"Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action." Kwong P.D., McDonald N.Q., Sigler P.B., Hendrickson W.A. Structure 3:1109-1119(1995) [PubMed: 8590005] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), DISULFIDES BONDS. Tissue: Venom.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y12101 mRNA. Translation: CAA72810.1.
AM050151 Genomic DNA. Translation: CAJ18318.1.
AJ251224 Genomic DNA. Translation: CAB62504.1.

PIR

TIKFB2. A44550.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BUN	X-ray	2.45	B	25-85	[»]

ProteinModelPortal

P00989.

SMR

P00989. Positions 25-85.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]

Gene3D

G3DSA:4.10.410.10. Prot_inh_Kunz-m. 1 hit.

Pfam

PF00014. Kunitz_BPTI. 1 hit.
[Graphical view]

PRINTS

PR00759. BASICPTASE.

SMART

SM00131. KU. 1 hit.
[Graphical view]

SUPFAM

SSF57362. Prot_inh_Kunz-m. 1 hit.

PROSITE

PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IVBI2_BUNMU

Accession

Primary (citable) accession number: P00989
Secondary accession number(s): O42299

Q9PTA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 15, 1998
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents