Q9QUR6 · PPCE_MOUSE
- ProteinProlyl endopeptidase
- GenePrep
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids710 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 554 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 641 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 680 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | endopeptidase activity | |
Molecular Function | oligopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | protein catabolic process | |
Biological Process | protein metabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProlyl endopeptidase
- EC number
- Short namesPE
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QUR6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000122402 | 1-710 | Prolyl endopeptidase | |||
Sequence: MLSFQYPDVYRDETSVQEYHGHKICDPYSWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTKEELEPMVFREVTVKGIDAADYQTIQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDTKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIEWIQ | ||||||
Modified residue | 157 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length710
- Mass (Da)80,752
- Last updated2000-05-01 v1
- Checksum1B010D5D6CA73C0E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |