Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospholipase A1

Gene
N/A
Organism
Vespa crabro (European hornet)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371NucleophileBy similarity
Active sitei165 – 1651Charge relay systemPROSITE-ProRule annotation
Active sitei230 – 2301Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis, Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A1 (EC:3.1.1.32)
Alternative name(s):
Allergen: Vesp c 1
OrganismiVespa crabro (European hornet)
Taxonomic identifieri7445 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataVespoideaVespidaeVespinaeVespa

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.By similarity

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3525. Vesp c 1.0101.
672. Vesp c 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Phospholipase A1PRO_0000401920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 245By similarity
Disulfide bondi87 ↔ 228By similarity
Disulfide bondi176 ↔ 219By similarity
Disulfide bondi181 ↔ 262By similarity
Disulfide bondi240 ↔ 246By similarity
Disulfide bondi269 ↔ 294By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0CH87.
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.

P0CH87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FNPCPYSDDT VKMIVLTREN KKYDFYTLDT IKNHNEFKDT ITLKPHVFIT
60 70 80 90 100
HGFTSSATAE NFVVMAKALL DKGNYLVILT DWRMAACTNE IAGLKLAYYP
110 120 130 140 150
YAASNTRLVG NYIATVTKML VQKYNVPMAN IRLIGHSLGA HISGFAGKKV
160 170 180 190 200
QELGLGKYPE IIGLDPAGPS FKSNDCSQRI CETDANYVQI IHTSNRLGTE
210 220 230 240 250
RTLGTVDFYM NNGYNQPGCG LPIIGETCSH TRAVKYFTEC IKHECCLIGV
260 270 280 290 300
PKSKNPQPVS KCTRNECVCV GLNAKTYPKT GSFYVPVESK APYCNNKGKI

I
Length:301
Mass (Da):33,384
Last modified:November 30, 2010 - v1
Checksum:i5F788492944BBEB4
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP0CH87.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3525. Vesp c 1.0101.
672. Vesp c 1.

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...

Publicationsi

  1. "Sol i 1, the phospholipase allergen of imported fire ant venom."
    Hoffman D.R., Sakell R.H., Schmidt M.
    J. Allergy Clin. Immunol. 115:611-616(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom.

Entry informationi

Entry nameiPA1_VESCR
AccessioniPrimary (citable) accession number: P0CH87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: November 30, 2010
Last modified: January 7, 2015
This is version 14 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.