A2VBC4 (PA1_POLPI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Venom phospholipase A1 EC=3.1.1.32 Alternative name(s): Allergen=Poly p 1
Organism	Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Taxonomic identifier	291283 [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 › Epiponini › Polybia

Protein attributes

Sequence length	322 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 A1 (EC 3.1.1.32) activity. Has weak hemolytic activity.
Catalytic activity	Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate. Ref.3
Subunit structure	Monomer By similarity.
Subcellular location	Secreted Ref.3.
Tissue specificity	Expressed by the venom gland. Ref.3
Post-translational modification	Contains six disulfide bonds. Is not glycosylated.
Allergenic properties	Causes an allergic reaction in human. Binds to IgE. Ref.3
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.
Mass spectrometry	Molecular mass is 33961 Da from positions 19 - 322. Determined by ESI. Ref.3

Ontologies

Keywords
Biological process	Cytolysis Hemolysis 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	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 – 18	18	Ref.3
	Chain	19 – 322	304	Venom phospholipase A1		PRO_5000223755
Sites
	Active site	156	1	Nucleophile By similarity
	Active site	184	1	Charge relay system By similarity
	Active site	248	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2VBC4 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 64A39D6D33AD86A8	FASTA	322	36,082
	10 20 30 40 50 60 MNFKYSILFI CFGTLDRGLI PECPFNEYDI LFFVYTRQQR DGIVLTEETL QNYDLFKKST 70 80 90 100 110 120 ISRQVVFIDH GFLSNGNNEN FIAMAKALIE KDNFLVISVD WKKGACNAFA STLDYLGYST 130 140 150 160 170 180 AVGNTRHVGK YVADFTKLLV EQYKVSMSNI RLIGHSLGAH TSGFAGKEVQ ELKLNKYSNI 190 200 210 220 230 240 DGLDPAGPSF DSNDCPERLC ETDAEYVQII HTSNILGVYS KIGTVDFYMN YGSHQPGCGR 250 260 270 280 290 300 FFSPSCSHTK AVKYLTECIK HECCLIGTPW KKYFSTPKPI SQCTKDTCVC VGLNAKSYPA 310 320 RGSFYVPVEA TAPYCHNEGI KL

References

[1]	Santos L.D., Santos K.S., de Souza B.M., Neto E.C., Castro F.M., Kalil J.E., Palma M.S. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Proteomic analysis of immunodominant allergens from the venom of the social wasp Polybia paulista." Santos L.D. Thesis (2007), Sao Paulo State University (UNESP), Brazil Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[3]	"Purification, sequencing and structural characterization of the phospholipase A(1) from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae)." Santos L.D., Santos K.S., de Souza B.M., Arcuri H.A., Cunha-Neto E., Castro F.M., Kalil J.E., Palma M.S. Toxicon 50:923-937(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-322, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, ALLERGEN, 3D-STRUCTURE MODELING. Tissue: Venom.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF101736 mRNA. Translation: ABN13879.1. AM491805 mRNA. Translation: CAM33429.1.
3D structure databases
ProteinModelPortal	A2VBC4.
ModBase	Search...
Protein family/group databases
Allergome	3608. Poly p 1. 3609. Poly p 1.0101.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.32. 9385.
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_POLPI

Accession

Primary (citable) accession number: A2VBC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 20, 2007
Last modified:	October 3, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)