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Q9XTA2

- PPCE_BOVIN

UniProt

Q9XTA2 - PPCE_BOVIN

Protein

Prolyl endopeptidase

Gene

PREP

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 710710Prolyl endopeptidasePRO_0000122400Add
    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

    PRIDEiQ9XTA2.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XTA2.
    SMRiQ9XTA2. Positions 1-709.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    Phylogenomic databases

    eggNOGiCOG1505.
    HOGENOMiHOG000238967.
    HOVERGENiHBG007251.
    InParanoidiQ9XTA2.
    KOiK01322.

    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.

    Q9XTA2-1 [UniParc]FASTAAdd to Basket

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    MLSFQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT    50
    VPFLEQCPIR GLYKERMTEL YDYPKYSCNF KKGKRYFYFY NTGLQNQRVL 100
    YVQDSLEGEA RVCLDPNTLS DDGTVALRGY AFSEDGEYVA YGLSASGSDW 150
    VTIKFMKVDG AKELADVLER VKFSCMAWTH DGKGMFYNAY PQQDGKSDGT 200
    ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS 250
    IREGCDPVNR LWYCDLHQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF 300
    TFKTNRHSPN YRLINIDFTD PEESRWKVLV PEHEKDVLEW VACVRSNFLV 350
    LCYLHDVKNT LQLHDMATGA LLKTFPLEVG SVVGYSGQKK DTEIFYQFTS 400
    FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI 450
    PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVCRLI FVRHMGGVLA 500
    VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI 550
    NGGSNGGLLV ATCANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG 600
    CSDNKQHFEW LIKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSP 650
    KFIATLQHLV GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI 700
    ARCLNIDWIQ 710
    Length:710
    Mass (Da):80,641
    Last modified:November 1, 1999 - v1
    Checksum:iCB2E7F0DAE2CFE9C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028866 mRNA. Translation: BAA78907.1.
    PIRiJC5877.
    RefSeqiNP_777197.1. NM_174772.1.
    UniGeneiBt.4796.

    Genome annotation databases

    GeneIDi286818.
    KEGGibta:286818.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028866 mRNA. Translation: BAA78907.1 .
    PIRi JC5877.
    RefSeqi NP_777197.1. NM_174772.1.
    UniGenei Bt.4796.

    3D structure databases

    ProteinModelPortali Q9XTA2.
    SMRi Q9XTA2. Positions 1-709.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q9XTA2.
    ChEMBLi CHEMBL2460.

    Protein family/group databases

    MEROPSi S09.001.

    Proteomic databases

    PRIDEi Q9XTA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 286818.
    KEGGi bta:286818.

    Organism-specific databases

    CTDi 5550.

    Phylogenomic databases

    eggNOGi COG1505.
    HOGENOMi HOG000238967.
    HOVERGENi HBG007251.
    InParanoidi Q9XTA2.
    KOi K01322.

    Miscellaneous databases

    NextBioi 20806472.

    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. "Cloning and expression of the cDNA encoding prolyl oligopeptidase (prolyl endopeptidase) from bovine brain."
      Yoshimoto T., Miyazaki K., Haraguchi N., Kitazono A., Kabashima T., Ito K.
      Biol. Pharm. Bull. 20:1047-1050(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiPPCE_BOVIN
    AccessioniPrimary (citable) accession number: Q9XTA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 90 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