[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; DOI=10.1074/jbc.M206647200; PubMed=12167627 [NCBI, ExPASy, EBI, Israel, Japan] Moreira L.A., Ito J., Ghosh A., Devenport M., Zieler H., Abraham E.G., Crisanti A., Nolan T., Catteruccia F., Jacobs-Lorena M.; "Bee venom phospholipase inhibits malaria parasite development in transgenic mosquitoes."; J. Biol. Chem. 277:40839-40843(2002).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Venom gland; DOI=10.1016/j.gene.2007.03.007; PubMed=17466468 [NCBI, ExPASy, EBI, Israel, Japan] Valdez-Cruz N.A., Segovia L., Corona M., Possani L.D.; "Sequence analysis and phylogenetic relationship of genes encoding heterodimeric phospholipases A2 from the venom of the scorpion Anuroctonus phaiodactylus."; Gene 396:149-158(2007).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 6-167. TISSUE=Venom gland; PubMed=2776767 [NCBI, ExPASy, EBI, Israel, Japan] Kuchler K., Gmachl M., Sippl M.J., Kreil G.; "Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes."; Eur. J. Biochem. 184:249-254(1989).
[4]	PROTEIN SEQUENCE OF 34-167. TISSUE=Venom; PubMed=4448181 [NCBI, ExPASy, EBI, Israel, Japan] Shipolini R.A., Callewaert G.L., Cottrell R.C., Vernon C.A.; "The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom."; Eur. J. Biochem. 48:465-476(1974).
[5]	DISULFIDE BONDS. PubMed=4614976 [NCBI, ExPASy, EBI, Israel, Japan] Shipolini R.A., Doonan S., Vernon C.A.; "The disulphide bridges of phospholipase A2 from bee venom."; Eur. J. Biochem. 48:477-483(1974).
[6]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=2274788 [NCBI, ExPASy, EBI, Israel, Japan] Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.; "Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue."; Science 250:1563-1566(1990).

Comments

FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion per subunit.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
ALLERGEN: Causes an allergic reaction in human.
SIMILARITY: Belongs to the phospholipase A2 family.

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

AF438408; AAL30844.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF373554; ABQ28728.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X16709; CAA34681.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S05650; PSHBA.

NP_001011614.1; -.

3D structure databases

PDB

1POC; X-ray; 2.00 A; A=34-167.

[ExPASy / RCSB / EBI]

1POC; -.

PTM databases

P00630; -.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
IPR008774; Phospholipase_A2_met.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.90.10; Phospholipase_A2; 1.

PANTHER

PTHR12253; Phospholipase_A2_met; 1.

Pfam

PF05826; Phospholip_A2_2; 1.
Pfam graphical view of domain structure.

SMART

SM00085; PA2c; 1.
SMART graphical view of domain structure.

PROSITE

PS00119; PA2_ASP; FALSE_NEG.
PS00118; PA2_HIS; 1.

Genome annotation databases

Ensembl

ENSAPMG00000005403; Apis mellifera. [Contig view]

GeneID

406141; -.

Other

LinkHub

P00630; -.

UniRef

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

Keywords

3D-structure; Allergen; Calcium; Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`PROPEP`	`19 33`	`15`		`PRO_0000022982`
`CHAIN`	`34 167`	`134`	`Phospholipase A2.`	`PRO_0000022983`
`ACT_SITE`	`67 67`
`ACT_SITE`	`97 97`
`METAL`	`41 41`		`Calcium; via carbonyl oxygen.`
`METAL`	`43 43`		`Calcium; via carbonyl oxygen.`
`METAL`	`45 45`		`Calcium; via carbonyl oxygen.`
`METAL`	`68 68`		`Calcium.`
`CARBOHYD`	`46 46`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000001`
`DISULFID`	`42 64`
`DISULFID`	`63 103`
`DISULFID`	`70 96`
`DISULFID`	`94 128`
`DISULFID`	`138 146`
`CONFLICT`	`72 72`		`D -> N (in Ref. 4; AA sequence).`
`CONFLICT`	`85 85`		`N -> D (in Ref. 4; AA sequence).`
`CONFLICT`	`89 90`		`Missing (in Ref. 4; AA sequence).`
`CONFLICT`	`95 99`		`DCDDK -> NNND (in Ref. 4; AA sequence).`
`CONFLICT`	`102 104`		`Missing (in Ref. 4; AA sequence).`
`CONFLICT`	`125 125`		`D -> N (in Ref. 4; AA sequence).`
`STRAND`	`40 45`	`6`
`HELIX`	`58 68`	`11`
`STRAND`	`71 74`	`4`
`STRAND`	`87 89`	`3`
`STRAND`	`91 93`	`3`
`HELIX`	`94 105`	`12`
`HELIX`	`110 122`	`13`
`STRAND`	`128 133`	`6`
`STRAND`	`135 137`	`3`
`STRAND`	`158 162`	`5`

Sequence information

Length: 167 AA [This is the length of the unprocessed precursor]

Molecular weight: 19058 Da [This is the MW of the unprocessed precursor]

CRC64: 88D5086A0E47DCC1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQVVLGSLFL LLLSTSHGWQ IRDRIGDNEL EERIIYPGTL WCGHGNKSSG PNELGRFKHT 

        70         80         90        100        110        120 
DACCRTHDMC PDVMSAGESK HGLTNTASHT RLSCDCDDKF YDCLKNSADT ISSYFVGKMY 

       130        140        150        160 
FNLIDTKCYK LEHPVTGCGE RTEGRCLHYT VDKSKPKVYQ WFDLRKY

P00630 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