Q9QUR6 · PPCE_MOUSE

  • Protein
    Prolyl endopeptidase
  • Gene
    Prep
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.

Catalytic activity

Features

Showing features for active site.

1710100200300400500600700
TypeIDPosition(s)Description
Active site554Charge relay system
Active site641Charge relay system
Active site680Charge relay system

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionendopeptidase activity
Molecular Functionoligopeptidase activity
Molecular Functionpeptide binding
Molecular Functionserine-type endopeptidase activity
Biological Processprotein catabolic process
Biological Processprotein metabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Prolyl endopeptidase
  • EC number
  • Short names
    PE
  • Alternative names
    • Post-proline cleaving enzyme

Gene names

    • Name
      Prep
    • Synonyms
      Pep

Organism names

  • Taxonomic identifier
  • Strain
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9QUR6
  • Secondary accessions
    • Q80YS1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Variants

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The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00001224021-710Prolyl endopeptidase
Modified residue157N6-acetyllysine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase S9A family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    710
  • Mass (Da)
    80,752
  • Last updated
    2000-05-01 v1
  • Checksum
    1B010D5D6CA73C0E
MLSFQYPDVYRDETSVQEYHGHKICDPYSWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTKEELEPMVFREVTVKGIDAADYQTIQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDTKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIEWIQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB007631
EMBL· GenBank· DDBJ
BAA88239.1
EMBL· GenBank· DDBJ
mRNA
AB022053
EMBL· GenBank· DDBJ
BAA83071.1
EMBL· GenBank· DDBJ
Genomic DNA
BC012869
EMBL· GenBank· DDBJ
AAH12869.1
EMBL· GenBank· DDBJ
mRNA
BC050830
EMBL· GenBank· DDBJ
AAH50830.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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