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Reviewed, UniProtKB/Swiss-Prot P00630 (PA2_APIME)

Last modified June 16, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Allergen Api m I
    Allergen=Api m 1
OrganismApis mellifera (Honeybee)
Taxonomic identifier7460 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

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Protein attributes

Sequence length167 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.

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.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the phospholipase A2 family.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding Ref.6

Inferred from direct assay. Source: UniProtKB

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3315 Ref.4
PRO_0000022982
Chain34 – 167134Phospholipase A2 Ref.6
PRO_0000022983

Sites

Active site671
Active site971
Metal binding411Calcium; via carbonyl oxygen
Metal binding431Calcium; via carbonyl oxygen
Metal binding451Calcium; via carbonyl oxygen
Metal binding681Calcium

Amino acid modifications

Glycosylation461N-linked (GlcNAc...)
CAR_000001
Disulfide bond42 ↔ 64 Ref.5 Ref.6
Disulfide bond63 ↔ 103 Ref.5 Ref.6
Disulfide bond70 ↔ 96 Ref.5 Ref.6
Disulfide bond94 ↔ 128 Ref.5 Ref.6
Disulfide bond138 ↔ 146 Ref.5 Ref.6

Experimental info

Sequence conflict721D → N AA sequence Ref.4
Sequence conflict851N → D AA sequence Ref.4
Sequence conflict89 – 902Missing AA sequence Ref.4
Sequence conflict95 – 995DCDDK → NNND AA sequence Ref.4
Sequence conflict102 – 1043Missing AA sequence Ref.4
Sequence conflict1251D → N AA sequence Ref.4

Secondary structure

1 .................... 167
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00630-1 [UniParc].

Last modified October 25, 2002. Version 3.
Checksum: 88D5086A0E47DCC1

FASTA16719,058
        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

« Hide

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References

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

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Cross-references

Sequence databases

AF438408 mRNA. Translation: AAL30844.1.
EF373554 Genomic DNA. Translation: ABQ28728.1.
X16709 mRNA. Translation: CAA34681.1.
PIRPSHBA. S05650.
RefSeqNP_001011614.1.
UniGeneAme.2

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1POCX-ray2.00A34-167[»]
ModBaseSearch...

PTM databases

GlycoSuiteDBP00630.

Genome annotation databases

GeneID406141.
KEGGame:406141.

Phylogenomic databases

OMAP00630. CESAFRN.

Enzyme and pathway databases

BRENDA3.1.1.4. 1025.

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
IPR008774. Phospholipase_A2_met.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR12253. Phospholipase_A2_met. 1 hit.
PfamPF05826. Phospholip_A2_2. 1 hit.
[Graphical view]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. False negative.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePA2_APIME
AccessionPrimary (citable) accession number: P00630
Secondary accession number(s): A5JGM7, Q8WPH5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2002
Last modified: June 16, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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