P00630 (PA2_APIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 EC=3.1.1.4 Alternative name(s): Allergen Api m I Phosphatidylcholine 2-acylhydrolase Allergen=Api m 1
Organism	Apis mellifera (Honeybee)
Taxonomic identifier	7460 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

Protein attributes

Sequence length	167 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.
Post-translational modification	N-glycosylated; contains mannose, N-acetylglucosamine and fucose alphal-6 and/or alphal-3 linked to the innermost N-acetylglucosamine. Ref.7
Allergenic properties	Causes an allergic reaction in human.
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.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from direct assay Ref.8. Source: UniProtKB phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Propeptide

19 – 33

15

PRO_0000022982

Chain

34 – 167

134

Phospholipase A2 Ref.8

PRO_0000022983

Sites

Active site

67

1

Active site

97

1

Metal binding

41

1

Calcium; via carbonyl oxygen

Metal binding

43

1

Calcium; via carbonyl oxygen

Metal binding

45

1

Calcium; via carbonyl oxygen

Metal binding

68

1

Calcium

Amino acid modifications

Glycosylation

46

1

N-linked (GlcNAc...)

CAR_000001

Disulfide bond

42 ↔ 64

Ref.6 Ref.8

Disulfide bond

63 ↔ 103

Ref.6 Ref.8

Disulfide bond

70 ↔ 96

Ref.6 Ref.8

Disulfide bond

94 ↔ 128

Ref.6 Ref.8

Disulfide bond

138 ↔ 146

Ref.6 Ref.8

Experimental info

Sequence conflict

72

1

D → N AA sequence Ref.4

Sequence conflict

85

1

N → D AA sequence Ref.4

Sequence conflict

89 – 90

2

Missing AA sequence Ref.4

Sequence conflict

95 – 99

5

DCDDK → NNND AA sequence Ref.4

Sequence conflict

102 – 104

3

Missing AA sequence Ref.4

Sequence conflict

125

1

D → N AA sequence Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

167

Helix Strand Turn

Details...

Beta strand

40 – 45

6

Helix

58 – 68

11

Beta strand

71 – 74

4

Beta strand

87 – 89

3

Beta strand

91 – 93

3

Helix

94 – 105

12

Helix

110 – 122

13

Beta strand

128 – 133

6

Beta strand

135 – 137

3

Beta strand

158 – 162

5

Sequences

	Sequence		Length	Mass (Da)
	P00630 [UniParc]. Last modified October 25, 2002. Version 3. Checksum: 88D5086A0E47DCC1	FASTA	167	19,058
	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

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]	"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: 20403370] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-60, 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: 4614976] [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: 8504812] [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: 2274788] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF438408 mRNA. Translation: AAL30844.1.
EF373554 Genomic DNA. Translation: ABQ28728.1.
X16709 mRNA. Translation: CAA34681.1.

PIR

PSHBA. S05650.

RefSeq

NP_001011614.1. NM_001011614.1.

UniGene

Ame.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1POC	X-ray	2.00	A	34-167	[»]

ProteinModelPortal

P00630.

SMR

P00630. Positions 34-167.

ModBase

Search...

Protein family/group databases

Allergome

2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3088. Api m 1.0101.
45. Api m 1.

PTM databases

GlycoSuiteDB

P00630.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

GB13351-RA; GB13351-PA; GB13351.

GeneID

406141.

KEGG

ame:406141.

Organism-specific databases

CTD

406141.

Phylogenomic databases

InParanoid

P00630.

OMA

RWQFYDL.

OrthoDB

EOG466T37.

PhylomeDB

P00630.

Enzyme and pathway databases

BRENDA

3.1.1.4. 387.

Family and domain databases

InterPro

IPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_A2_euk.
[Graphical view]

Gene3D

G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.

PANTHER

PTHR12253. Phospholipase_A2_met. 1 hit.

Pfam

PF05826. Phospholip_A2_2. 1 hit.
[Graphical view]

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

SUPFAM

SSF48619. PhospholipaseA2. 1 hit.

PROSITE

PS00119. PA2_ASP. False negative.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PA2_APIME

Accession

Primary (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:	October 19, 2011
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)