[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; Paramasivam M., Srinivasan A., Singh T.P.; "Bungarus caeruleus mRNA for phospholipase A2, beta bungarotoxin A2 chain complete coding region."; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
TISSUE SPECIFICITY: Expressed by the venom gland.
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

AY081147; AAL87004.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00617; 1BUN. [HSSP ENTRY / PDB]

SMR

Q8QFW3; 28-147.

ModBase

Q8QFW3.

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:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from InterPro).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006644;	Biological process: phospholipid metabolic process (inferred from electronic annotation from InterPro).
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.

ProtoNet

Q8QFW3.

Phylogenomic databases

HOVERGEN

Q8QFW3; -.

Other

UniRef

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

Keywords

Calcium; 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`	`By similarity.`	`PRO_0000022825`
`CHAIN`	`28 147`	`120`	`Phospholipase A2, beta bungarotoxin A2 chain.`	`PRO_0000022826`
`ACT_SITE`	`75 75`		`By similarity.`
`ACT_SITE`	`121 121`		`By similarity.`
`METAL`	`55 55`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`57 57`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`59 59`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`76 76`		`Calcium (By similarity).`
`DISULFID`	`42 42`		`Interchain (with a B chain) (By similarity).`
`DISULFID`	`54 146`		`By similarity.`
`DISULFID`	`56 72`		`By similarity.`
`DISULFID`	`71 127`		`By similarity.`
`DISULFID`	`78 120`		`By similarity.`
`DISULFID`	`88 113`		`By similarity.`
`DISULFID`	`106 118`		`By similarity.`

Sequence information

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

Molecular weight: 16120 Da [This is the MW of the unprocessed precursor]

CRC64: 3B72A0EEE323EADF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPAHLLVLS AVCVSLLGAA NIPPYPLNLI NFMEMIRYTI PCDKTWGHYA DYGCYCGAGG 

        70         80         90        100        110        120 
SGTPVDALDR CCYVHDNCYG VAENKHKCNP KTQSCSYKLT KRTIICYGAA GTCGRIVCDC 

       130        140 
DRTAALCFGD SEYIGAHKNI DTKRHCQ

Q8QFW3 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