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Protein

Phospholipase A1 2

Gene
N/A
Organism
Dolichovespula maculata (Bald-faced hornet) (Vespula maculata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.

Catalytic activityi

Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.
Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei140 – 1401NucleophileBy similarity
Active sitei168 – 1681Charge relay systemPROSITE-ProRule annotation
Active sitei232 – 2321Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERidolma-ppla12. Phospholipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A1 2 (EC:3.1.1.32, EC:3.1.1.4)
Alternative name(s):
Allergen Dol m I
Allergen: Dol m 1.02
OrganismiDolichovespula maculata (Bald-faced hornet) (Vespula maculata)
Taxonomic identifieri7441 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaeVespinaeDolichovespula

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei1668. Dol m 1.02.
328. Dol m 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Phospholipase A1 2PRO_0000090375Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 247By similarity
Disulfide bondi90 ↔ 230By similarity
Disulfide bondi179 ↔ 222By similarity
Disulfide bondi184 ↔ 264By similarity
Disulfide bondi242 ↔ 248By similarity
Disulfide bondi271 ↔ 296By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP53357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002334. Allerg_PlipaseA1.
IPR013818. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
PRINTSiPR00825. DOLALLERGEN.
PR00821. TAGLIPASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GILPECKLVP EEISFVLSTR ENRDGVYLTL QKLKNGKMFK NSDLSSKKVP
60 70 80 90 100
FLIHGFISSA TNKNYADMTR ALLDKDDIMV ISIDWRDGAC SNEFALLKFI
110 120 130 140 150
GYPKAVENTR AVGKYIADFS KILIQKYKVL LENIRLIGHS LGAQIAGFAG
160 170 180 190 200
KEFQRFKLGK YPEIIGLDPA GPSFKKKDCP ERICETDAHY VQILHTSSNL
210 220 230 240 250
GTERTLGTVD FYINDGSNQP GCTYIIGETC SHTRAVKYLT ECIRRECCLI
260 270 280 290 300
GVPQSKNPQP VSKCTRNECV CVGLNAKEYP KKGSFYVPVE AKAPFCNNNG

KII
Length:303
Mass (Da):33,782
Last modified:October 1, 1996 - v1
Checksum:i85816A837C0F3AF8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551G → E.
Natural varianti295 – 2951F → Y.

Sequence databases

PIRiA44563.

Cross-referencesi

Sequence databases

PIRiA44563.

3D structure databases

ProteinModelPortaliP53357.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1668. Dol m 1.02.
328. Dol m 1.
ESTHERidolma-ppla12. Phospholipase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002334. Allerg_PlipaseA1.
IPR013818. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
PRINTSiPR00825. DOLALLERGEN.
PR00821. TAGLIPASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA12_DOLMA
AccessioniPrimary (citable) accession number: P53357
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.