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Reviewed, UniProtKB/Swiss-Prot P49369 (PA1_VESVU)

Last modified November 25, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase A1
    EC=3.1.1.32
    EC=3.1.1.4
Alternative name(s):
    Allergen Ves v I
    Allergen=Ves v 1
OrganismVespula vulgaris (Yellow jacket) (Wasp)
Taxonomic identifier7454 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaeVespinaeVespula

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 + H(2)O = 2-acylglycerophosphocholine + a carboxylate.

Phosphatidylcholine + H(2)O = 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 processLipid degradation
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphospholipase A1 activity

Inferred from electronic annotation. Source: InterPro

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636
Chain37 – 336300Phospholipase A1
PRO_0000017813

Sites

Active site1731Charge relay system By similarity
Active site2011Charge relay system By similarity
Active site2651Charge relay system By similarity

Experimental info

Sequence conflict371G → F AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49369-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 65548B7F5BE56456

FASTA33637,676
        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 

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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: 8828537] [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

L43561 mRNA. Translation: AAB48072.1.

3D structure databases

HSSPHSSP built from PDB template 1LPB based on UniProtKB P16233.
ModBaseSearch...

Family and domain databases

InterProIPR002334. Dol/Ves_allerg.
IPR000734. Lipase.
IPR008262. Lipase_AS.
IPR013818. Lipase_N.
[Graphical view]
PANTHERPTHR11610. Lipase. 1 hit.
PfamPF00151. Lipase. 1 hit.
[Graphical view]
PRINTSPR00825. DOLALLERGEN.
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA1_VESVU
AccessionPrimary (citable) accession number: P49369
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 25, 2008
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Allergens

Nomenclature of allergens and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents