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Protein

Phospholipase A2

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi43 – 431Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi45 – 451Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei67 – 6711 Publication
Metal bindingi68 – 681CalciumCombined sources1 Publication
Active sitei97 – 9711 Publication

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • phospholipase A2 activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 387.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2 (EC:3.1.1.4)
Short name:
bvPLA2
Alternative name(s):
Allergen Api m I
Phosphatidylcholine 2-acylhydrolase
Allergen: Api m 1
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
Proteomesi
  • UP000005203 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3088. Api m 1.0101.
45. Api m 1.

Chemistry

ChEMBLiCHEMBL4807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 33152 PublicationsPRO_0000022982Add
BLAST
Chaini34 – 167134Phospholipase A21 PublicationPRO_0000022983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 642 Publications
Glycosylationi46 – 461N-linked (GlcNAc...)1 PublicationCAR_000001
Disulfide bondi63 ↔ 1032 Publications
Disulfide bondi70 ↔ 962 Publications
Disulfide bondi94 ↔ 1282 Publications
Disulfide bondi138 ↔ 1462 Publications

Post-translational modificationi

N-glycosylated; contains mannose, N-acetylglucosamine and fucose alphal-6 and/or alphal-3 linked to the innermost N-acetylglucosamine.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP00630.

PTM databases

UniCarbKBiP00630.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Chemistry

BindingDBiP00630.

Structurei

Secondary structure

1
167
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 456Combined sources
Helixi58 – 6811Combined sources
Beta strandi71 – 744Combined sources
Beta strandi87 – 893Combined sources
Beta strandi91 – 933Combined sources
Helixi94 – 10512Combined sources
Helixi110 – 12213Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi158 – 1625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POCX-ray2.00A34-167[»]
ProteinModelPortaliP00630.
SMRiP00630. Positions 34-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00630.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J1W3. Eukaryota.
ENOG410YVBF. LUCA.
HOGENOMiHOG000143527.
InParanoidiP00630.
KOiK01047.
OMAiSWFANDA.
PhylomeDBiP00630.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PfamiPF05826. Phospholip_A2_2. 1 hit.
[Graphical view]
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVVLGSLFL LLLSTSHGWQ IRDRIGDNEL EERIIYPGTL WCGHGNKSSG
60 70 80 90 100
PNELGRFKHT DACCRTHDMC PDVMSAGESK HGLTNTASHT RLSCDCDDKF
110 120 130 140 150
YDCLKNSADT ISSYFVGKMY FNLIDTKCYK LEHPVTGCGE RTEGRCLHYT
160
VDKSKPKVYQ WFDLRKY
Length:167
Mass (Da):19,058
Last modified:October 25, 2002 - v3
Checksum:i88D5086A0E47DCC1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721D → N AA sequence (PubMed:4448181).Curated
Sequence conflicti85 – 851N → D AA sequence (PubMed:4448181).Curated
Sequence conflicti89 – 902Missing AA sequence (PubMed:4448181).Curated
Sequence conflicti95 – 995DCDDK → NNND AA sequence (PubMed:4448181).Curated
Sequence conflicti102 – 1043Missing AA sequence (PubMed:4448181).Curated
Sequence conflicti125 – 1251D → N AA sequence (PubMed:4448181).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF438408 mRNA. Translation: AAL30844.1.
EF373554 Genomic DNA. Translation: ABQ28728.1.
X16709 mRNA. Translation: CAA34681.1.
PIRiS05650. PSHBA.
RefSeqiNP_001011614.1. NM_001011614.1.
UniGeneiAme.2.

Genome annotation databases

EnsemblMetazoaiGB48228-RA; GB48228-PA; GB48228.
GeneIDi406141.
KEGGiame:406141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF438408 mRNA. Translation: AAL30844.1.
EF373554 Genomic DNA. Translation: ABQ28728.1.
X16709 mRNA. Translation: CAA34681.1.
PIRiS05650. PSHBA.
RefSeqiNP_001011614.1. NM_001011614.1.
UniGeneiAme.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POCX-ray2.00A34-167[»]
ProteinModelPortaliP00630.
SMRiP00630. Positions 34-167.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP00630.
ChEMBLiCHEMBL4807.

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3088. Api m 1.0101.
45. Api m 1.

PTM databases

UniCarbKBiP00630.

Proteomic databases

PaxDbiP00630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiGB48228-RA; GB48228-PA; GB48228.
GeneIDi406141.
KEGGiame:406141.

Organism-specific databases

CTDi406141.

Phylogenomic databases

eggNOGiENOG410J1W3. Eukaryota.
ENOG410YVBF. LUCA.
HOGENOMiHOG000143527.
InParanoidiP00630.
KOiK01047.
OMAiSWFANDA.
PhylomeDBiP00630.

Enzyme and pathway databases

BRENDAi3.1.1.4. 387.

Miscellaneous databases

EvolutionaryTraceiP00630.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PfamiPF05826. Phospholip_A2_2. 1 hit.
[Graphical view]
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-167.
    Tissue: Venom.
  5. "Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of melittin and phospholipase A(2) levels."
    Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L., Orsi R.D., Barraviera B., Pimenta D.C.
    Toxicon 56:355-362(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-60, IDENTIFICATION BY MASS SPECTROMETRY, SEASONAL VARIATION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  7. "Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2."
    Kubelka V., Altmann F., Staudacher E., Tretter V., Marz L., Hard K., Kamerling J.P., Vliegenthart J.F.
    Eur. J. Biochem. 213:1193-1204(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-167 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2_APIME
AccessioniPrimary (citable) accession number: P00630
Secondary accession number(s): A5JGM7, Q8WPH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2002
Last modified: May 11, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The secretion of this protein into venom follows a seasonal pattern. This variation is synchronized with melittin variation, i.e. their production increase in the same months.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.