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Reviewed, UniProtKB/Swiss-Prot P00617 (PA21B_BUNMU)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phospholipase A2, beta bungarotoxin A1 chain
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismBungarus multicinctus (Many-banded krait)
Taxonomic identifier8616 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

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Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion By similarity.

Subunit structure

Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. The A1 chain is found in beta-1 and beta-2 bungarotoxins. Ref.9

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 0.019 mg/kg by intraperitoneal injection in beta-1 bungarotoxin and 0.028 mg/kg in beta-2.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 278 Ref.4 Ref.5
PRO_0000022835
Chain28 – 147120Phospholipase A2, beta bungarotoxin A1 chain
PRO_0000022836

Sites

Active site751 By similarity
Active site1211 By similarity
Metal binding551Calcium; via carbonyl oxygen
Metal binding571Calcium; via carbonyl oxygen
Metal binding591Calcium; via carbonyl oxygen
Metal binding761Calcium

Amino acid modifications

Disulfide bond42Interchain (with a B chain) Ref.9
Disulfide bond54 ↔ 146 Ref.9
Disulfide bond56 ↔ 72 Ref.9
Disulfide bond71 ↔ 127 Ref.9
Disulfide bond78 ↔ 120 Ref.9
Disulfide bond88 ↔ 113 Ref.9
Disulfide bond106 ↔ 118 Ref.9

Natural variations

Natural variant1161I → V in 20% of the molecules.

Experimental info

Mutagenesis421C → S: Loss of PA2 activity. No loss in Ca(2+)-binding ability. Weak loss in folding. Ref.3
Sequence conflict101S → L in CAB62164. Ref.2
Sequence conflict93 – 942QS → SQ Ref.4
Sequence conflict93 – 942QS → SQ Ref.5
Sequence conflict1141G → A Ref.9
Sequence conflict130 – 1323NSE → QSD Ref.4
Sequence conflict130 – 1323NSE → QSD Ref.5

Secondary structure

1 ....................... 147
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00617-1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 12109A187E20C7F6

FASTA14716,220
        10         20         30         40         50         60 
MNPAHLLVLS AVCVSLLGAA NIPPHPLNLI NFMEMIRYTI PCEKTWGEYA DYGCYCGAGG 

        70         80         90        100        110        120 
SGRPIDALDR CCYVHDNCYG DAEKKHKCNP KTQSYSYKLT KRTIICYGAA GTCGRIVCDC 

       130        140 
DRTAALCFGN SEYIEGHKNI DTARFCQ

« Hide

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References

[1]"Genomic organization of the genes encoding the A chains of beta-bungarotoxins."
Chang L.-S., Chu Y.P.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"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 10-147.
Tissue: Liver.
[3]"Expression of A chain and B chain of beta-bungarotoxin from taiwan banded krait: the functional implication of the interchain disulfide bond between A chain and B chain."
Wu P.-F., Chang L.-S.
J. Protein Chem. 20:413-421(2001) [PubMed: 11732693] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-147, MUTAGENESIS OF CYS-42.
Tissue: Venom gland.
[4]"Amino acid sequences of the two polypeptide chains in beta1-bungarotoxin from the venom of Bungarus multicinctus."
Kondo K., Narita K., Lee C.-Y.
J. Biochem. 83:101-115(1978) [PubMed: 624701] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-147.
Tissue: Venom.
[5]"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 28-147, SEQUENCE REVISION TO 112-114 AND 136.
[6]"Characterization of phospholipase A activity of beta1-bungarotoxin from Bungarus multicinctus venom. II. Identification of the histidine residue of beta1-bungarotoxin modified by p-bromophenacyl bromide."
Kondo K., Toda H., Narita K.
J. Biochem. 84:1301-1308(1978) [PubMed: 730754] [Abstract]
Cited for: CHARACTERIZATION OF PHOSPHOLIPASE A2 ACTIVITY.
[7]"Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes."
Abe T., Alema S., Miledi R.
Eur. J. Biochem. 80:1-12(1977) [PubMed: 303565] [Abstract]
Cited for: CHARACTERIZATION OF PRESYNAPTIC NEUROTOXINS.
[8]"What does beta-bungarotoxin do at the neuromuscular junction?"
Rowan E.G.
Toxicon 39:107-118(2001) [PubMed: 10936627] [Abstract]
Cited for: REVIEW.
[9]"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) OF 28-147, METAL-BINDING SITES, DISULFIDE BONDS.
Tissue: Venom.

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Cross-references

Sequence databases

AJ431711 mRNA. Translation: CAD24466.1.
AJ251360 Genomic DNA. Translation: CAB62164.1.
AJ242011 mRNA. Translation: CAB62383.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BUNX-ray2.45A28-147[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP00617.

Enzyme and pathway databases

BRENDA3.1.1.4. 81621.

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePA21B_BUNMU
AccessionPrimary (citable) accession number: P00617
Secondary accession number(s): Q8QFN8, Q9PU95, Q9PU98
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 19, 2002
Last modified: June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents