Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O70196

- PPCE_RAT

UniProt

O70196 - PPCE_RAT

Protein

Prolyl endopeptidase

Gene

Prep

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4-methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA.1 Publication

    Catalytic activityi

    Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.1 Publication

    Enzyme regulationi

    Inhibited by DFP, Z-Pro-prolinal and poststatin, but not by PMSF, SBTI, EDTA, leupeptin, E-64 and pepstatin.1 Publication

    Sites

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

    GO - Molecular functioni

    1. endopeptidase activity Source: RGD
    2. peptide binding Source: RGD
    3. serine-type endopeptidase activity Source: InterPro
    4. serine-type exopeptidase activity Source: InterPro

    GO - Biological processi

    1. proteolysis Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl endopeptidaseBy similarity (EC:3.4.21.26)
    Short name:
    PEBy similarity
    Alternative name(s):
    Post-proline cleaving enzymeBy similarity
    rPop
    Gene namesi
    Name:PrepImported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620841. Prep.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 710710Prolyl endopeptidasePRO_0000365637Add
    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

    PaxDbiO70196.
    PRIDEiO70196.

    PTM databases

    PhosphoSiteiO70196.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested: uterus, kidney, heart, lung, small intestine, smooth muscle, liver, spleen, thymus, adrenal, pituitary and whole brain.1 Publication

    Developmental stagei

    In the estrous cycle, expression and activity are highest in the luteal phase.1 Publication

    Gene expression databases

    GenevestigatoriO70196.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000000360.

    Structurei

    3D structure databases

    ProteinModelPortaliO70196.
    SMRiO70196. Positions 1-709.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG1505.
    HOGENOMiHOG000238967.
    HOVERGENiHBG007251.
    KOiK01322.
    PhylomeDBiO70196.

    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.

    O70196-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSFQYPDVY RDETSVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT    50
    VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL 100
    YVQDSLEGEA RVFLDPNTLS DDGTVALRGY AFSEDGEYFA YGLSASGSDW 150
    VTIKFMKVDG AKELPDVLER VKFTCMAWTH DGKGMFYNSY PQQDGKSDGT 200
    ETSTNLHQKL CYHVLGTDQS EDVLCAEFPD EPKWMGGAEL SDDGRYVLLS 250
    IWEGCDPVNR LWYCDLQQGS NGINGILKWV KLIDNFEGEY DYITNEGTVF 300
    TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV 350
    LCYLRNVKNI LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS 400
    FLSPGVIYHC DLTREELEPR VFREVTVKGI DASDYQTIQV FYPSKDGTKI 450
    PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA 500
    VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTTSKRLTI 550
    NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG 600
    CSDSKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL 650
    KFIATLQYIV GRSRKQSNPL LIHVDTKAGH GPGKPTAKVI EEVSDMFAFI 700
    ARCLNIEWIQ 710
    Length:710
    Mass (Da):80,742
    Last modified:August 1, 1998 - v1
    Checksum:iEE6A6AD78D79174C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012759 mRNA. Translation: BAA25544.1.
    RefSeqiNP_112614.1. NM_031324.1.
    UniGeneiRn.11058.

    Genome annotation databases

    GeneIDi83471.
    KEGGirno:83471.
    UCSCiRGD:620841. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012759 mRNA. Translation: BAA25544.1 .
    RefSeqi NP_112614.1. NM_031324.1.
    UniGenei Rn.11058.

    3D structure databases

    ProteinModelPortali O70196.
    SMRi O70196. Positions 1-709.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000000360.

    Chemistry

    BindingDBi O70196.
    ChEMBLi CHEMBL4035.

    Protein family/group databases

    MEROPSi S09.001.

    PTM databases

    PhosphoSitei O70196.

    Proteomic databases

    PaxDbi O70196.
    PRIDEi O70196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 83471.
    KEGGi rno:83471.
    UCSCi RGD:620841. rat.

    Organism-specific databases

    CTDi 5550.
    RGDi 620841. Prep.

    Phylogenomic databases

    eggNOGi COG1505.
    HOGENOMi HOG000238967.
    HOVERGENi HBG007251.
    KOi K01322.
    PhylomeDBi O70196.

    Miscellaneous databases

    NextBioi 615881.
    PROi O70196.

    Gene expression databases

    Genevestigatori O70196.

    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 rat prolyl oligopeptidase and its expression in the ovary during the estrous cycle."
      Kimura A., Takahashi T.
      J. Exp. Zool. 286:656-665(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Wistar1 Publication.
      Tissue: Liver1 Publication.
    2. Maurya D.K., Bhargava P.
      Submitted (JAN-2009) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPPCE_RAT
    AccessioniPrimary (citable) accession number: O70196
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 89 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3