Q6Q250 (PA13_POLDO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Venom phospholipase A1 3 EC=3.1.1.32 Alternative name(s): Allergen=Pol d 1.03
Organism	Polistes dominula (European paper wasp) (Vespa dominula)
Taxonomic identifier	34728 [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 › Polistinae › Polistini › Polistes

Protein attributes

Sequence length	316 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Cytolysis Hemolysis Lipid degradation Lipid metabolism
Cellular component	Secreted
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW 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
	Signal peptide	‹1 – 15	›15
	Chain	16 – 316	301	Venom phospholipase A1 3		PRO_5000093093
Sites
	Active site	153	1	Nucleophile By similarity
	Active site	181	1	Charge relay system By similarity
	Active site	242	1	Charge relay system By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q6Q250 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 12CB3A7748F8FE05	FASTA	316	35,019
	10 20 30 40 50 60 ADDLTTLRNG TLDRGITPDC TFNEKDIELH VYSRDKRNGI ILKKEILKNY DLFQKSQISH 70 80 90 100 110 120 QIAILIHGFL STGNNENFDA MAKALIEIDN FLVISVDWKK GACNAFASTN DVLGYSQAVG 130 140 150 160 170 180 NTRHVGKYVA DFTKLLVEQY KVPMSNIRLI GHSLGAHTSG FAGKEVQRLK LGKYKEIIGL 190 200 210 220 230 240 DPAGPSFLTS KCPDRLCETD AEYVQAIHTS AILGVYYNVG SVDFYVNYGK SQPGCSEPSC 250 260 270 280 290 300 SHTKAVKYLT ECIKRECCLI GTPWKSYFST PKPISQCKRD TCVCVGLNAQ SYPAKGSFYV 310 PVDKDAPYCH NEGIKL

References

[1]	Moawad T.I.S., Hoffman D.R. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY566647 mRNA. Translation: AAS67043.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPL based on UniProtKB P16233.
ProteinModelPortal	Q6Q250.
ModBase	Search...
Protein family/group databases
Allergome	3435. Pol d 1.0103. 586. Pol d 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

PA13_POLDO

Accession

Primary (citable) accession number: Q6Q250

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 5, 2004
Last modified:	October 3, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)