P82242 · PLAL1_PLALA

Function

Features

Showing features for binding site.

1131102030405060708090100110120130
TypeIDPosition(s)Description
Binding site21Zn2+ (UniProtKB | ChEBI)
Binding site45Zn2+ (UniProtKB | ChEBI)
Binding site73Zn2+ (UniProtKB | ChEBI)
Binding site88Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionzinc ion binding

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Major pollen allergen Pla l 1
  • Allergen name
    Pla l 1

Organism names

Accessions

  • Primary accession
    P82242
  • Secondary accessions
    • Q93X26
    • Q949A3
    • Q949A4

Subcellular Location

Keywords

Phenotypes & Variants

Allergenic properties

Causes an allergic reaction in human. Binds to IgE. The English plantain pollen is an important cause of pollinosis in the temperate regions of North America, Australia and Europe. The glycan moiety does not seem to constitute a relevant allergenic epitope.

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant58in Pla l 1.0102 and 1.0103
Natural variant82in Pla l 1.0103

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Protein family/group databases

PTM/Processing

Features

Showing features for chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00002151171-131Major pollen allergen Pla l 1
Disulfide bond17↔86
Disulfide bond20↔131
Disulfide bond42↔74
Glycosylation107N-linked (GlcNAc...) asparagine

Post-translational modification

Exists in two variants: glycosylated and non-glycosylated. Carries a complex, major N-linked glycan, with a alpha-1,3-fucose residue in its structure and probably also a beta-1,2-xylose. The average modification of molecular mass due to glycosylation is approximately 969 Da.

Keywords

Family & Domains

Sequence similarities

Belongs to the Ole e I family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    131
  • Mass (Da)
    14,521
  • Last updated
    2003-02-12 v2
  • Checksum
    62F9B279ED3A4BC6
TQTSHPAKFHVEGEVYCNVCHSRNLINELSERMAGAQVQLDCKDDSKKVIYSIGGETDQDGVYRLPVVGYHEDCEIKLVKSSRPDCSEIPKLAKGTIQTSKVDLSKNTTITEKTRHVKPLSFRAKTDAPGC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ313166
EMBL· GenBank· DDBJ
CAC41633.1
EMBL· GenBank· DDBJ
mRNA
AJ313167
EMBL· GenBank· DDBJ
CAC41634.1
EMBL· GenBank· DDBJ
mRNA
AJ313168
EMBL· GenBank· DDBJ
CAC41635.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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