Q9U6W0 (PA1_POLAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A1 EC=3.1.1.32 Alternative name(s): Allergen=Pol a 1
Organism	Polistes annularis (Paper wasp)
Taxonomic identifier	27505 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Vespoidea › Vespidae › Polistinae › Polistini › Polistes

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Disease	Allergen
Molecular function	Hydrolase
PTM	Disulfide bond
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Phospholipase A1		PRO_0000090376
Sites
	Active site	138	1	Nucleophile By similarity
	Active site	166	1	Charge relay system By similarity
	Active site	227	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9U6W0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6A0B7DC76FDCC047	FASTA	301	33,484
	10 20 30 40 50 60 MSPDCTFNEK DIVFYVYSRD KRDGIILKKE TLTNYDLFTK STISKQVVFL IHGFLSTGNN 70 80 90 100 110 120 ENFVAMSKAL IEKDDFLVIS VDWKKGACNA FASTKDALGY SKAVGNTRHV GKFVADFTKL 130 140 150 160 170 180 LVEKYKVLIS NIRLIGHSLG AHTSGFAGKE VQKLKLGKYK EIIGLDPAGP YFHRSDCPDR 190 200 210 220 230 240 LCVTDAEYVQ VIHTSIILGV YYNVGSVDFY VNYGKNQPGC NEPSCSHTKA VKYLTECIKH 250 260 270 280 290 300 ECCLIGTPWK KYFSTPKPIS QCRGDTCVCV GLNAKSYPAR GAFYAPVEAN APYCHNEGIK L

References

[1]	King T.P., Lu G. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF174527 mRNA. Translation: AAD52615.1.
3D structure databases
ProteinModelPortal	Q9U6W0.
ModBase	Search...
Protein family/group databases
Allergome	3430. Pol a 1.0101. 583. Pol a 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. Lipase. 1 hit.
Pfam	PF00151. Lipase. 1 hit. [Graphical view]
PRINTS	PR00825. DOLALLERGEN. PR00821. TAGLIPASE.
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA1_POLAN

Accession

Primary (citable) accession number: Q9U6W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)