Reviewed, UniProtKB/Swiss-Prot Q3ZU95 (PA1_VESGE)

Names and origin

Protein names	Recommended name:     Phospholipase A1     EC=3.1.1.32     EC=3.1.1.4 Alternative name(s):     Allergen=Ves g 1
Organism	Vespula germanica (Yellow jacket) (Wasp)
Taxonomic identifier	30212 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Vespoidea › Vespidae › Vespinae › Vespula

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 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 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	phospholipase A1 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
	Chain	1 – 300	300	Phospholipase A1		PRO_5000076445
Sites
	Active site	137	1	Nucleophile By similarity
	Active site	165	1	Charge relay system By similarity
	Active site	229	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3ZU95-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: CC0E3A26CE8B7D04	FASTA	300	33,240
	10 20 30 40 50 60 GPKCPFNTDT VSMIIETREN RNRDLYTLQT LQNHPEFKEK TITRPVVFIT HGFTSSASET 70 80 90 100 110 120 NFINLSKALV DKDNYMVISI DWQTAACTNE AAGLKYLYYP TAASNTRLVG QYIATITQKL 130 140 150 160 170 180 VKQYKISMAN IRLIGHSLGA HVSGFAGKKV QELKLGKYSE IIGLDPAGPS FSSNKCSDRL 190 200 210 220 230 240 CETDAEYVQI LHTSNHLGTE RILGTVDFYM NNGKNQPGCG RFFTEVCSHS RAVIYMAECI 250 260 270 280 290 300 KHECCLIGIP KSKSSQPISS CTKQECVCVG LNAKKYPSRG SFYVPVESTA PFCNNKGKII

References

[1]	"cDNA cloning of phospholipase A1 from Vespula germanica (Ves g 1)." Suck R., Fiebig H., Cromwell O. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM083318 mRNA. Translation: CAJ28931.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.32. 190836. 3.1.1.4. 190836.
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.
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA1_VESGE

Accession

Primary (citable) accession number: Q3ZU95

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 27, 2005
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)