P49369 (PA1_VESVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A1 EC=3.1.1.32 EC=3.1.1.4 Alternative name(s): Allergen Ves v I Allergen=Ves v 1
Organism	Vespula vulgaris (Yellow jacket) (Wasp)
Taxonomic identifier	7454 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Vespoidea › Vespidae › Vespinae › Vespula

Protein attributes

Sequence length	336 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	Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities By similarity.
Catalytic activity	Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate. Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Contains six disulfide bonds By similarity.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-acyl-2-lysophosphatidylserine acylhydrolase activity Inferred from electronic annotation. Source: EC phosphatidylcholine 1-acylhydrolase activity Inferred from electronic annotation. Source: EC phosphatidylserine 1-acylhydrolase activity Inferred from electronic annotation. Source: EC 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 – 36	36	Ref.1
	Chain	37 – 336	300	Phospholipase A1		PRO_0000017813
Sites
	Active site	173	1	Nucleophile By similarity
	Active site	201	1	Charge relay system By similarity
	Active site	265	1	Charge relay system By similarity
Experimental info
	Sequence conflict	37	1	G → F AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49369 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 65548B7F5BE56456	FASTA	336	37,676
	10 20 30 40 50 60 MEENMNLKYL LLFVYFVQVL NCCYGHGDPL SYELDRGPKC PFNSDTVSII IETRENRNRD 70 80 90 100 110 120 LYTLQTLQNH PEFKKKTITR PVVFITHGFT SSASETNFIN LAKALVDKDN YMVISIDWQT 130 140 150 160 170 180 AACTNEAAGL KYLYYPTAAR NTRLVGQYIA TITQKLVKHY KISMANIRLI GHSLGAHASG 190 200 210 220 230 240 FAGKKVQELK LGKYSEIIGL DPARPSFDSN HCSERLCETD AEYVQIIHTS NYLGTEKTLG 250 260 270 280 290 300 TVDFYMNNGK NQPGCGRFFS EVCSHSRAVI YMAECIKHEC CLIGIPKSKS SQPISSCTKQ 310 320 330 ECVCVGLNAK KYPSRGSFYV PVESTAPFCN NKGKII

References

[1]

"Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy." King T.P., Lu G., Gonzalez M., Qian N., Soldatova L. J. Allergy Clin. Immunol. 98:588-600(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-65; 165-183; 247-263 AND 273-294. Tissue: Venom and Venom gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43561 mRNA. Translation: AAB48072.1.
3D structure databases
ProteinModelPortal	P49369.
ModBase	Search...
Protein family/group databases
Allergome	3520. Ves v 1.0101. 668. Ves v 1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002334. Dol/Ves_allerg. IPR000734. Lipase. IPR013818. Lipase_N. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit.
Pfam	PF00151. Lipase. 1 hit. [Graphical view]
PRINTS	PR00825. DOLALLERGEN.
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA1_VESVU

Accession

Primary (citable) accession number: P49369

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)