[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; Chang L.-S., Chu Y.P.; "Genomic organization of the genes encoding the A chains of beta-bungarotoxins."; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-147. TISSUE=Liver; PubMed=10903499 [NCBI, ExPASy, EBI, Israel, Japan] Wu P.-F., Chang L.-S.; "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."; Eur. J. Biochem. 267:4668-4675(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 11-147, AND MUTAGENESIS OF CYS-42. TISSUE=Venom gland; DOI=10.1023/A:1012237005574; PubMed=11732693 [NCBI, ExPASy, EBI, Israel, Japan] Wu P.-F., Chang L.-S.; "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."; J. Protein Chem. 20:413-421(2001).
[4]	PROTEIN SEQUENCE OF 28-147. TISSUE=Venom; PubMed=624701 [NCBI, ExPASy, EBI, Israel, Japan] Kondo K., Narita K., Lee C.-Y.; "Amino acid sequences of the two polypeptide chains in beta1-bungarotoxin from the venom of Bungarus multicinctus."; J. Biochem. 83:101-115(1978).
[5]	PROTEIN SEQUENCE OF 28-147, AND SEQUENCE REVISION TO 112-114 AND 136. PubMed=7096304 [NCBI, ExPASy, EBI, Israel, Japan] Kondo K., Toda H., Narita K., Lee C.-Y.; "Amino acid sequence of beta 2-bungarotoxin from Bungarus multicinctus venom. The amino acid substitutions in the B chains."; J. Biochem. 91:1519-1530(1982).
[6]	CHARACTERIZATION OF PHOSPHOLIPASE A2 ACTIVITY. PubMed=730754 [NCBI, ExPASy, EBI, Israel, Japan] Kondo K., Toda H., Narita K.; "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."; J. Biochem. 84:1301-1308(1978).
[7]	CHARACTERIZATION OF PRESYNAPTIC NEUROTOXINS. PubMed=303565 [NCBI, ExPASy, EBI, Israel, Japan] Abe T., Alema S., Miledi R.; "Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes."; Eur. J. Biochem. 80:1-12(1977).
[8]	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).
[9]	X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 28-147, METAL-BINDING SITES, AND DISULFIDE BONDS. TISSUE=Venom; DOI=10.1016/S0969-2126(01)00246-5; PubMed=8590005 [NCBI, ExPASy, EBI, Israel, Japan] Kwong P.D., McDonald N.Q., Sigler P.B., Hendrickson W.A.; "Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action."; Structure 3:1109-1119(1995).

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 A1 chain is found in beta-1 and beta-2 bungarotoxins.
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.
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

AJ431711; CAD24466.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ251360; CAB62164.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ242011; CAB62383.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1BUN; X-ray; 2.45 A; A=28-147.

[ExPASy / RCSB / EBI]

PDBsum

1BUN; -.

ModBase

P00617.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0042734;	Cellular component: presynaptic membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0007268;	Biological process: synaptic transmission (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

Phylogenomic databases

HOVERGEN

P00617; -.

Other

LinkHub

P00617; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`PROPEP`	`20 27`	`8`		`PRO_0000022835`
`CHAIN`	`28 147`	`120`	`Phospholipase A2, beta bungarotoxin A1 chain.`	`PRO_0000022836`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`121 121`		`By similarity.`
`METAL`	`55 55`		`Calcium; via carbonyl oxygen.`
`METAL`	`57 57`		`Calcium; via carbonyl oxygen.`
`METAL`	`59 59`		`Calcium; via carbonyl oxygen.`
`METAL`	`76 76`		`Calcium.`
`DISULFID`	`42 42`		`Interchain (with a B chain).`
`DISULFID`	`54 146`
`DISULFID`	`56 72`
`DISULFID`	`71 127`
`DISULFID`	`78 120`
`DISULFID`	`88 113`
`DISULFID`	`106 118`
`VARIANT`	`116 116`	`1`	`I -> V (in 20% of the molecules).`
`MUTAGEN`	`42 42`		`C->S: Loss of PA2 activity. No loss in Ca(2+)-binding ability. Weak loss in folding.`
`CONFLICT`	`10 10`		`S -> L (in Ref. 2; CAB62164).`
`CONFLICT`	`93 94`		`QS -> SQ (in Ref. 4 and 5).`
`CONFLICT`	`114 114`		`G -> A (in Ref. 9).`
`CONFLICT`	`130 132`		`NSE -> QSD (in Ref. 4 and 5).`
`HELIX`	`29 37`	`9`
`HELIX`	`47 50`	`4`
`TURN`	`53 55`	`3`
`STRAND`	`56 58`	`3`
`HELIX`	`67 83`	`17`
`TURN`	`84 86`	`3`
`TURN`	`90 92`	`3`
`STRAND`	`97 100`	`4`
`STRAND`	`103 106`	`4`
`HELIX`	`113 130`	`18`
`HELIX`	`135 137`	`3`
`HELIX`	`142 145`	`4`

Sequence information

Length: 147 AA [This is the length of the unprocessed precursor]

Molecular weight: 16220 Da [This is the MW of the unprocessed precursor]

CRC64: 12109A187E20C7F6 [This is a checksum on the sequence]

        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

P00617 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools