P9WEW3 · PCH13_PENRB

  • Protein
    Subtilisin-like serine protease Pen ch 13
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Serine protease (PubMed:11893850, PubMed:16436150).
Hydrolyzes casein, gelatin and human collagen type IV, but not elastin in vitro (PubMed:16436150).
Hydrolyzes OCLN of the human lung epithelial cells at 202-Gln-|-Ser-203 and Gln-211-|-Ile-212 (PubMed:16436150).

Activity regulation

Inhibited by phenylmethanesulfonyl fluoride (PMSF) and diethyl pyrocarbonate (DEPC), but not by benzamidine.

pH Dependence

Active at neutral to pH 8 with casein as substrate.

Features

Showing features for active site, site.

139850100150200250300350
TypeIDPosition(s)Description
Active site157Charge relay system
Active site188Charge relay system
Site280Important for catalytic activity
Active site343Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular FunctionIgE binding
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Subtilisin-like serine protease Pen ch 13
  • EC number
  • Alternative names
    • Alkaline serine protease
  • Allergen name
    Pen ch 13

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium > Penicillium chrysogenum species complex

Accessions

  • Primary accession
    P9WEW3
  • Secondary accessions
    • Q8NKG0

Subcellular Location

Keywords

Phenotypes & Variants

Allergenic properties

Causes an allergic reaction in human. Binds to IgE of patients suffering from bronchial asthma (PubMed:10231324, PubMed:11893850, PubMed:12602675, PubMed:15663570).
Binds to IgE in 17% of the 212 asthmatic patients of different age (3 to 94 years old). The binding frequency and intensity to IgE increases significantly with age. Binds also to IgG and IgG4 (PubMed:12602675).
Induces histamine release from basophils of asthmatic patients (PubMed:11893850).
May contribute to asthma by damaging the barrier formed by the airway epithelium by cleaving the tight junction protein OCLN and stimulating the release of mediators, such as PGE2, CXCL8 and TGFB1, in human respiratory epithelial cells (PubMed:16436150).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis164Reduced IgE-binding. Significantly reduced IgE-binding; when associated with M-167.
Mutagenesis167Reduced IgE-binding. Significantly reduced IgE-binding; when associated with M-164.
Mutagenesis318-321Reduced IgE-binding.

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, glycosylation, chain.

TypeIDPosition(s)Description
Signal1-19
PropeptidePRO_000044667720-115Removed in mature form
Glycosylation113N-linked (GlcNAc...) asparagine
ChainPRO_5004312984116-398Subtilisin-like serine protease Pen ch 13
Glycosylation249N-linked (GlcNAc...) asparagine

Keywords

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain35-113Inhibitor I9
Region124-134IgE-binding
Domain125-398Peptidase S8
Region163-170IgE-binding
Region175-195Disordered
Compositional bias176-195Polar residues
Region227-245IgE-binding
Region310-318IgE-binding

Sequence similarities

Belongs to the peptidase S8 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    398
  • Mass (Da)
    40,362
  • Last updated
    2020-12-02 v1
  • Checksum
    8E85FE9E942080D3
MGFLKLLSTSLATLAVVNAGKLLTANDGDEVVPSSYIVVMNDGVSTAQFETHRNWAANVHARTRSLKGGESGPGKHFDINGMKGYSASFDDRTVKDIASDPTVKYVEPDMVVNATANVVQRNAPSWGLSRISSKKSGATDYVYDSTAGEGIVIYGVDTGIDIGHADFGGRAEWGTNTADNDDTDGNGHGTHTASTAAGSKFGVAKKASVVAVKVLGADGSGTNSQVIAGMDWAVKDSKSRGATGKSVMNMSLGGAYSRAMNDAAANVVRSGVFLSVAAGNEAQDASNSSPASAPNVCTIAASTNSDGSASFTNFGSVVDLYAPGKDITAAYPGGGSKTLSGTSMAAPHVAGAAAYLMALEGVTSDKACARIVELAISSISSAPSGTTSKLLYNGINAQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias176-195Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF321100
EMBL· GenBank· DDBJ
AAM33821.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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