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Protein

Phospholipase A1 4

Gene
N/A
Organism
Polistes dominula (European paper wasp) (Vespa dominula)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolysis of phosphatidylcholine with phospholipase A1 (EC 3.1.1.32) activity. Has weak hemolytic activity (By similarity).By similarity

Catalytic activityi

Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei153NucleophileBy similarity1
Active sitei181Charge relay systemPROSITE-ProRule annotation1
Active sitei242Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis, Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERipoldo-q6q252. Phospholipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A1 4 (EC:3.1.1.32)
Alternative name(s):
Allergen: Pol d 1.04
OrganismiPolistes dominula (European paper wasp) (Vespa dominula)
Taxonomic identifieri743375 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaePolistinaePolistiniPolistes

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE (By similarity).By similarity

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3436. Pol d 1.0104.
586. Pol d 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 4Sequence analysis›4
PropeptideiPRO_00004251895 – 14By similarity10
ChainiPRO_500009309415 – 316Phospholipase A1 4Add BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 257By similarity
Disulfide bondi103 ↔ 240By similarity
Disulfide bondi192 ↔ 235By similarity
Disulfide bondi197 ↔ 277By similarity
Disulfide bondi252 ↔ 258By similarity
Disulfide bondi284 ↔ 309By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6Q249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002334. Allerg_PlipaseA1.
IPR013818. Lipase/vitellogenin.
IPR033906. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
PRINTSiPR00825. DOLALLERGEN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6Q249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADDLTTLRNG TLDRGITPDC TFNEKDIELH VYSRDKRNGI ILKKEILKNY
60 70 80 90 100
DLFQKSQISH QIAILIHGFL STGNNENFDA MAKALIEIDN FLVISVDWKK
110 120 130 140 150
GACNAFASTN DVLGYSQAVG NTRHVGKYVA DFTKLLVEQY KVPMSNIRLI
160 170 180 190 200
GHSLGAHTSG FAGKEVQRLK LGKYKEIIGL DPAGPSFLTS KCPDRLCETD
210 220 230 240 250
AEYVQAIHTS AILGVYYNVG SVDFYVNYGK SQPGCSEPSC SHTKAVKYLT
260 270 280 290 300
ECIKRECCLI GTPWKSYFST PKSISQCKRD TCVCVGLNAQ SYPAKGSFYV
310
PVEKDAPYCH NEGIKL
Length:316
Mass (Da):35,023
Last modified:July 5, 2004 - v1
Checksum:i12CB3A74BB368405
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566649 mRNA. Translation: AAS67044.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566649 mRNA. Translation: AAS67044.1.

3D structure databases

ProteinModelPortaliQ6Q249.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3436. Pol d 1.0104.
586. Pol d 1.
ESTHERipoldo-q6q252. Phospholipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002334. Allerg_PlipaseA1.
IPR013818. Lipase/vitellogenin.
IPR033906. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
PRINTSiPR00825. DOLALLERGEN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA14_POLDO
AccessioniPrimary (citable) accession number: Q6Q249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.