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Reviewed, UniProtKB/Swiss-Prot Q6Q252 (PA11_POLDO)

Last modified September 22, 2009. Version 38. 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 1
    EC=3.1.1.32
Alternative name(s):
    Allergen=Pol d 1.01
OrganismPolistes dominula (European paper wasp) (Vespa dominula)
Taxonomic identifier34728 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaePolistinaePolistiniPolistes

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
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 peptide1 – 2121 Potential
Propeptide22 – 337316 Potential
PRO_5000093090
Chain36 – 337302Venom phospholipase A1 1
PRO_5000093091

Sites

Active site1741Nucleophile By similarity
Active site2021Charge relay system By similarity
Active site2631Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6Q252-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: C0A7E0E5EBDE448C

FASTA33737,559
        10         20         30         40         50         60 
MNFKYSILFI CFVKVLDNCY AADDLTTLRN GTLDRGITPD CTFNEKDIEL HVYSRDKRNG 

        70         80         90        100        110        120 
IILKKEILKN YDLFQKSQIS HQIAILIHGF LSTGNNENFD AMAKALIEID NFLVISVDWK 

       130        140        150        160        170        180 
KGACNAFAST NDVLGYSQAV GNTRHVGKYV ADFTKLLVEQ YKVPMSNIRL IGHSLGAHTS 

       190        200        210        220        230        240 
GFAGKEVQRL KLGKYKEIIG LDPAGPSFLT NKCPNRLCET DAEYVQAIHT SAILGVYYNV 

       250        260        270        280        290        300 
GSVDFYVNYG KSQPGCSEPS CSHTKAVKYL TECIKRECCL IGTPWKSYFS TPKPISQCKR 

       310        320        330 
DTCVCVGLNA QSYPAKGSFY VPVDKDAPYC HNEGIKL 

« 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

AY566645 mRNA. Translation: AAS67041.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.32. 288870.

Family and domain databases

InterProIPR002334. Dol/Ves_allerg.
IPR000734. Lipase.
IPR013818. Lipase_N.
IPR008262. Lipase_Ser_AS.
[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 namePA11_POLDO
AccessionPrimary (citable) accession number: Q6Q252
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: September 22, 2009
This is version 38 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