Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chain

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

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 (Kv).1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Presynaptic neurotoxin, Toxin, Voltage-gated potassium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chain
Alternative name(s):
Beta-2-bungarotoxin
OrganismiBungarus multicinctus (Many-banded krait)
Taxonomic identifieri8616 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24242 PublicationsAdd
BLAST
Chaini25 – 8561Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chainPRO_0000016864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 81PROSITE-ProRule annotation1 Publication
Disulfide bondi40 ↔ 64PROSITE-ProRule annotation1 Publication
Disulfide bondi56 ↔ 77PROSITE-ProRule annotation1 Publication
Disulfide bondi79 – 79Interchain (with an A chain)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors.1 Publication

Protein-protein interaction databases

MINTiMINT-1515216.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni29 – 324Combined sources
Beta strandi40 – 423Combined sources
Beta strandi44 – 507Combined sources
Helixi51 – 533Combined sources
Beta strandi55 – 617Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 733Combined sources
Helixi74 – 818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUNX-ray2.45B25-85[»]
ProteinModelPortaliP00989.
SMRiP00989. Positions 25-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00989.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 8151BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the venom Kunitz-type family.Curated
Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00989-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGGLLLLL GLLTLCAELT PVSSRKRHPD CDKPPDTKIC QTVVRAFYYK
60 70 80
PSAKRCVQFR YGGCNGNGNH FKSDHLCRCE CLEYR
Length:85
Mass (Da):9,568
Last modified:July 15, 1998 - v2
Checksum:iFE95A59AF92BF2AA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441Missing AA sequence (PubMed:7096304).Curated
Sequence conflicti65 – 706NGNGNH → DGDHGN AA sequence (PubMed:7096304).Curated
Sequence conflicti82 – 832LE → EL AA sequence (PubMed:7096304).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12101 mRNA. Translation: CAA72810.1.
AM050151 Genomic DNA. Translation: CAJ18318.1.
AJ251224 Genomic DNA. Translation: CAB62504.1.
PIRiA44550. TIKFB2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12101 mRNA. Translation: CAA72810.1.
AM050151 Genomic DNA. Translation: CAJ18318.1.
AJ251224 Genomic DNA. Translation: CAB62504.1.
PIRiA44550. TIKFB2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUNX-ray2.45B25-85[»]
ProteinModelPortaliP00989.
SMRiP00989. Positions 25-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1515216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00989.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiVKTH2_BUNMU
AccessioniPrimary (citable) accession number: P00989
Secondary accession number(s): O42299
, Q1RPT1, Q9PRV8, Q9PTA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: May 11, 2016
This is version 112 of the entry and version 2 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.