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Q9QUR6

- PPCE_MOUSE

UniProt

Q9QUR6 - PPCE_MOUSE

Protein

Prolyl endopeptidase

Gene

Prep

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    • Comment

    Functioni

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

    Catalytic activityi

    Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei554 – 5541Charge relay systemPROSITE-ProRule annotation
    Active sitei641 – 6411Charge relay systemPROSITE-ProRule annotation
    Active sitei680 – 6801Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro
    2. serine-type exopeptidase activity Source: InterPro

    GO - Biological processi

    1. protein metabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl endopeptidase (EC:3.4.21.26)
    Short name:
    PE
    Alternative name(s):
    Post-proline cleaving enzyme
    Gene namesi
    Name:Prep
    Synonyms:Pep
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1270863. Prep.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 710710Prolyl endopeptidasePRO_0000122402Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei157 – 1571N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9QUR6.
    PaxDbiQ9QUR6.
    PRIDEiQ9QUR6.

    PTM databases

    PhosphoSiteiQ9QUR6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9QUR6.
    BgeeiQ9QUR6.
    CleanExiMM_PREP.
    GenevestigatoriQ9QUR6.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9QUR6. 1 interaction.
    MINTiMINT-1854903.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QUR6.
    SMRiQ9QUR6. Positions 1-709.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    Phylogenomic databases

    eggNOGiCOG1505.
    GeneTreeiENSGT00530000063426.
    HOVERGENiHBG007251.
    InParanoidiQ9QUR6.
    KOiK01322.
    OMAiDYQTIQI.
    OrthoDBiEOG78PV88.
    PhylomeDBiQ9QUR6.
    TreeFamiTF300655.

    Family and domain databases

    Gene3Di2.130.10.120. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR023302. Pept_S9A_N.
    IPR001375. Peptidase_S9.
    IPR002470. Peptidase_S9A.
    [Graphical view]
    PANTHERiPTHR11757. PTHR11757. 1 hit.
    PfamiPF00326. Peptidase_S9. 1 hit.
    PF02897. Peptidase_S9_N. 1 hit.
    [Graphical view]
    PRINTSiPR00862. PROLIGOPTASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QUR6-1 [UniParc]FASTAAdd to Basket

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    MLSFQYPDVY RDETSVQEYH GHKICDPYSW LEDPDSEQTK AFVEAQNKIT    50
    VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL 100
    YVQDSLEGEA RVFLDPNTLS DDGTVALRGY AFSEDGEYFA YGLSASGSDW 150
    VTIKFMKVDG AKELPDVLER VKFTCMAWTH DGKGMFYNSY PQQDGKSDGT 200
    ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS 250
    IWEGCDPVNR LWYCDLQQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF 300
    TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV 350
    LCYLHDVKNI LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS 400
    FLSPGVIYHC DLTKEELEPM VFREVTVKGI DAADYQTIQI FYPSKDGTKI 450
    PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA 500
    VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI 550
    NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG 600
    CSDTKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL 650
    KFIATLQYIV GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI 700
    ARCLNIEWIQ 710
    Length:710
    Mass (Da):80,752
    Last modified:May 1, 2000 - v1
    Checksum:i1B010D5D6CA73C0E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007631 mRNA. Translation: BAA88239.1.
    AB022053 Genomic DNA. Translation: BAA83071.1.
    BC012869 mRNA. Translation: AAH12869.1.
    BC050830 mRNA. Translation: AAH50830.2.
    CCDSiCCDS23826.1.
    PIRiJW0080.
    RefSeqiNP_035286.1. NM_011156.2.
    UniGeneiMm.37294.

    Genome annotation databases

    EnsembliENSMUST00000099858; ENSMUSP00000097444; ENSMUSG00000019849.
    GeneIDi19072.
    KEGGimmu:19072.
    UCSCiuc007ezx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007631 mRNA. Translation: BAA88239.1 .
    AB022053 Genomic DNA. Translation: BAA83071.1 .
    BC012869 mRNA. Translation: AAH12869.1 .
    BC050830 mRNA. Translation: AAH50830.2 .
    CCDSi CCDS23826.1.
    PIRi JW0080.
    RefSeqi NP_035286.1. NM_011156.2.
    UniGenei Mm.37294.

    3D structure databases

    ProteinModelPortali Q9QUR6.
    SMRi Q9QUR6. Positions 1-709.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QUR6. 1 interaction.
    MINTi MINT-1854903.

    Chemistry

    BindingDBi Q9QUR6.
    ChEMBLi CHEMBL4935.

    Protein family/group databases

    MEROPSi S09.001.

    PTM databases

    PhosphoSitei Q9QUR6.

    Proteomic databases

    MaxQBi Q9QUR6.
    PaxDbi Q9QUR6.
    PRIDEi Q9QUR6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099858 ; ENSMUSP00000097444 ; ENSMUSG00000019849 .
    GeneIDi 19072.
    KEGGi mmu:19072.
    UCSCi uc007ezx.1. mouse.

    Organism-specific databases

    CTDi 5550.
    MGIi MGI:1270863. Prep.

    Phylogenomic databases

    eggNOGi COG1505.
    GeneTreei ENSGT00530000063426.
    HOVERGENi HBG007251.
    InParanoidi Q9QUR6.
    KOi K01322.
    OMAi DYQTIQI.
    OrthoDBi EOG78PV88.
    PhylomeDBi Q9QUR6.
    TreeFami TF300655.

    Miscellaneous databases

    ChiTaRSi PREP. mouse.
    NextBioi 295594.
    PROi Q9QUR6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QUR6.
    Bgeei Q9QUR6.
    CleanExi MM_PREP.
    Genevestigatori Q9QUR6.

    Family and domain databases

    Gene3Di 2.130.10.120. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR023302. Pept_S9A_N.
    IPR001375. Peptidase_S9.
    IPR002470. Peptidase_S9A.
    [Graphical view ]
    PANTHERi PTHR11757. PTHR11757. 1 hit.
    Pfami PF00326. Peptidase_S9. 1 hit.
    PF02897. Peptidase_S9_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00862. PROLIGOPTASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells."
      Ishino T., Ohtsuki S., Homma K., Natori S.
      J. Biochem. 123:540-545(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Structure and localization of the mouse prolyl oligopeptidase gene."
      Kimura A., Yoshida I., Takagi N., Takahashi T.
      J. Biol. Chem. 274:24047-24053(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Limb and Mammary gland.

    Entry informationi

    Entry nameiPPCE_MOUSE
    AccessioniPrimary (citable) accession number: Q9QUR6
    Secondary accession number(s): Q80YS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3