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Reviewed, UniProtKB/Swiss-Prot P00618 (PA22_BUNMU)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 A2 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 length145 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 A2 chain is found in beta-3 and beta-4 bungarotoxins.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 0.066 mg/kg by intraperitoneal injection in beta-3 bungarotoxin and 0.073 mg/kg in beta-4.

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 – 1717 Potential
Propeptide18 – 258 Ref.2
PRO_0000022837
Chain26 – 145120Phospholipase A2, beta bungarotoxin A2 chain
PRO_0000022838

Sites

Active site731 By similarity
Active site1191 By similarity
Metal binding531Calcium; via carbonyl oxygen By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding741Calcium By similarity

Amino acid modifications

Disulfide bond40Interchain (with a B chain) By similarity
Disulfide bond52 ↔ 144 By similarity
Disulfide bond54 ↔ 70 By similarity
Disulfide bond69 ↔ 125 By similarity
Disulfide bond76 ↔ 118 By similarity
Disulfide bond86 ↔ 111 By similarity
Disulfide bond104 ↔ 116 By similarity

Experimental info

Sequence conflict91 – 922QS → SQ AA sequence Ref.2
Sequence conflict1281N → Q AA sequence Ref.2
Sequence conflict1301E → D AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P00618-1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 08CD9D0E84E57581

FASTA14516,296
        10         20         30         40         50         60 
MLIFLWCGAV CVSLLGAANI PPHPLNLINF MEMIRYTIPC EKTWGEYADY GCYCGAGGSG 

        70         80         90        100        110        120 
RPIDALDRCC YVHDNCYGDA EKKHKCNPKT QSYSYKLTKR TIICYGAAGT CARIVCDCDR 

       130        140 
TAALCFGNSE YIERHKNIDT KRHCR

« Hide

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References

[1]"Nucleotide sequence encoding beta-bungarotoxin A2-chain from the venom glands of Bungarus multicinctus."
Danse J.-M., Toussaint J.L., Kempf J.
Nucleic Acids Res. 18:4609-4609(1990) [PubMed: 2388842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Amino acid sequences of three beta-bungarotoxins (beta 3-, beta 4-, and beta 5-bungarotoxins) from Bungarus multicinctus venom. Amino acid substitutions in the A chains."
Kondo K., Toda H., Narita K., Lee C.-Y.
J. Biochem. 91:1531-1548(1982) [PubMed: 7096305] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-145.
Tissue: Venom.
[3]"What does beta-bungarotoxin do at the neuromuscular junction?"
Rowan E.G.
Toxicon 39:107-118(2001) [PubMed: 10936627] [Abstract]
Cited for: REVIEW.

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Cross-references

Sequence databases

X53407 mRNA. Translation: CAA37483.1.
PIRPSKFA2. S10980.

3D structure databases

HSSPHSSP built from PDB template 1BUN based on UniProtKB P00617.
SMRP00618. Positions 26-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00618.

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 namePA22_BUNMU
AccessionPrimary (citable) accession number: P00618
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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