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Q6Q251

- PA12_POLDO

UniProt

Q6Q251 - PA12_POLDO

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Protein

Phospholipase A1 2

Gene
N/A
Organism
Polistes dominula (European paper wasp) (Vespa dominula)
Status
Reviewed - 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.

Catalytic activityi

Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Nucleophile By similarity
Active sitei181 – 1811Charge relay system By similarity
Active sitei242 – 2421Charge relay system By similarity

GO - Molecular functioni

  1. 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
  2. phosphatidylcholine 1-acylhydrolase activity Source: UniProtKB-EC
  3. phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. hemolysis in other organism Source: UniProtKB-KW
  2. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis, Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A1 2 (EC:3.1.1.32)
Alternative name(s):
Allergen: Pol d 1.02
OrganismiPolistes dominula (European paper wasp) (Vespa dominula)
Taxonomic identifieri743375 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaePolistinaePolistiniPolistes

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

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

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3434. Pol d 1.0102.
586. Pol d 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 4›4 Reviewed prediction
Propeptidei5 – 1410PRO_0000425187
Chaini15 – 316302Phospholipase A1 2PRO_5000093092Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ6Q251.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002334. Dol/Ves_allerg.
IPR000734. Lipase.
IPR013818. Lipase_N.
[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.

Q6Q251-1 [UniParc]FASTAAdd to Basket

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ADDLTTLRNG TLDRGITPDC TFNEKDIELH VYSRDKRNGI ILKKEILKNY    50
DLFQKSQISH QIAILIHGFL STGNNENFDA MAKALIEIDN FLVISVDWKK 100
GACNAFASTN DVLGYSQAVG NTRHVGKYVA DFTKLLVEQY KVPMSNIRLI 150
GHSLGAHTSG FAGKEVQRLK LGKYKEIIGL DPAGPSFLTN KCPNRLCETD 200
AEYVQAIHTS AILGVYYNVG SVDFYVNYGK SQPGCSEPSC SHTKAVKYLT 250
ECIKRECCLI GTPWKSYFST PKPISQCKRD TCVCVGLNAQ SYPAKGSFYV 300
PVEKDAPYCH NEGIKL 316
Length:316
Mass (Da):35,059
Last modified:July 5, 2004 - v1
Checksum:i0DDB3E975309B7F5
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY566646 mRNA. Translation: AAS67042.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY566646 mRNA. Translation: AAS67042.1 .

3D structure databases

ProteinModelPortali Q6Q251.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 3434. Pol d 1.0102.
586. Pol d 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002334. Dol/Ves_allerg.
IPR000734. Lipase.
IPR013818. Lipase_N.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
Pfami PF00151. Lipase. 1 hit.
[Graphical view ]
PRINTSi PR00825. DOLALLERGEN.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPA12_POLDO
AccessioniPrimary (citable) accession number: Q6Q251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 53 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

External Data

Dasty 3

Similar proteinsi