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Reviewed, UniProtKB/Swiss-Prot Q6Q250 (PA13_POLDO)

Last modified January 19, 2010. Version 39. 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:
    Venom phospholipase A1 3
    EC=3.1.1.32
Alternative name(s):
    Allergen=Pol d 1.03
OrganismPolistes dominula (European paper wasp) (Vespa dominula)
Taxonomic identifier34728 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaePolistinaePolistiniPolistes

Protein attributes

Sequence length316 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCytolysis
Hemolysis
Lipid degradation
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis by symbiont of host erythrocytes

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphospholipase A1 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 15›15
Chain16 – 316301Venom phospholipase A1 3
PRO_5000093093

Sites

Active site1531Nucleophile By similarity
Active site1811Charge relay system By similarity
Active site2421Charge relay system By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q6Q250-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 12CB3A7748F8FE05

FASTA31635,019
        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 

« Hide

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

HSSPHSSP built from PDB template 1GPL based on UniProtKB P16233.
SMRQ6Q250. Positions 10-310.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.32. 288870.

Family and domain databases

InterProIPR002334. Dol/Ves_allerg.
IPR000734. Lipase.
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 namePA13_POLDO
AccessionPrimary (citable) accession number: Q6Q250
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: January 19, 2010
This is version 39 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