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UniProtKB/Swiss-Prot entry P00618


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PA22_BUNMU
Primary accession number P00618
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1990 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 72)
Name and origin of the protein
Protein name Phospholipase A2, beta bungarotoxin A2 chain [Precursor]
Synonyms EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
Gene name None
From
Bungarus multicinctus (Many-banded krait) [TaxID: 8616] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
DOI=10.1093/nar/18.15.4609; PubMed=2388842 [NCBI, ExPASy, EBI, Israel, Japan]
Danse J.-M., Toussaint J.L., Kempf J.;
"Nucleotide sequence encoding beta-bungarotoxin A2-chain from the venom glands of Bungarus multicinctus.";
Nucleic Acids Res. 18:4609-4609(1990).
[2]
PROTEIN SEQUENCE OF 26-145.
TISSUE=Venom;
PubMed=7096305 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K., Toda H., Narita K., Lee C.-Y.;
"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.";
J. Biochem. 91:1531-1548(1982).
[3]
REVIEW.
DOI=10.1016/S0041-0101(00)00159-8; PubMed=10936627 [NCBI, ExPASy, EBI, Israel, Japan]
Rowan E.G.;
"What does beta-bungarotoxin do at the neuromuscular junction?";
Toxicon 39:107-118(2001).
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: 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.
  • SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X53407; CAA37483.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S10980; PSKFA2.
3D structure databases
HSSP P00617; 1BUN. [HSSP ENTRY / PDB]
SMR P00618; 26-145.
ModBase P00618.
Family and domain databases
InterPro IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
Graphical view of domain structure.
Gene3D G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER PTHR11716; Phospholipase_A2; 1.
Pfam PF00068; Phospholip_A2_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00389; PHPHLIPASEA2.
ProDom PD000303; PhospholipaseA2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00085; PA2c; 1.
SMART graphical view of domain structure.
PROSITE PS00119; PA2_ASP; 1.
PS00118; PA2_HIS; 1.
BLOCKS P00618.
Phylogenomic databases
HOVERGEN P00618; -.
Other
ProtoNet P00618.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
PROPEP   18    25  8      PRO_0000022837
CHAIN   26   145  120     Phospholipase A2, beta bungarotoxin A2 chain. PRO_0000022838
ACT_SITE   73    73        By similarity. 
ACT_SITE   119   119        By similarity. 
METAL   53    53        Calcium; via carbonyl oxygen (By similarity). 
METAL   55    55        Calcium; via carbonyl oxygen (By similarity). 
METAL   57    57        Calcium; via carbonyl oxygen (By similarity). 
METAL   74    74        Calcium (By similarity). 
DISULFID   40    40        Interchain (with a B chain) (By similarity). 
DISULFID   52   144        By similarity. 
DISULFID   54    70        By similarity. 
DISULFID   69   125        By similarity. 
DISULFID   76   118        By similarity. 
DISULFID   86   111        By similarity. 
DISULFID   104   116        By similarity. 
CONFLICT   91    92        QS -> SQ (in Ref. 2; AA sequence). 
CONFLICT   128   128        N -> Q (in Ref. 2; AA sequence). 
CONFLICT   130   130        E -> D (in Ref. 2; AA sequence). 
Sequence information
Length: 145 AA [This is the length of the unprocessed precursor] Molecular weight: 16296 Da [This is the MW of the unprocessed precursor] CRC64: 08CD9D0E84E57581 [This is a checksum on the sequence]
        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 

P00618 in FASTA format

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