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Protein

Prolyl endopeptidase

Gene

Prep

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

GO - Biological processi

  • protein metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

ESTHERimouse-ppce. S9N_PPCE_Peptidase_S9.
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 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1270863. Prep.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • membrane Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

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

BgeeiQ9QUR6.
CleanExiMM_PREP.
ExpressionAtlasiQ9QUR6. baseline and differential.
GenevisibleiQ9QUR6. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9QUR6. 1 interaction.
MINTiMINT-1854903.
STRINGi10090.ENSMUSP00000097444.

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.
OMAiAHSFKFA.
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

« Hide

        10         20         30         40         50
MLSFQYPDVY RDETSVQEYH GHKICDPYSW LEDPDSEQTK AFVEAQNKIT
60 70 80 90 100
VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL
110 120 130 140 150
YVQDSLEGEA RVFLDPNTLS DDGTVALRGY AFSEDGEYFA YGLSASGSDW
160 170 180 190 200
VTIKFMKVDG AKELPDVLER VKFTCMAWTH DGKGMFYNSY PQQDGKSDGT
210 220 230 240 250
ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS
260 270 280 290 300
IWEGCDPVNR LWYCDLQQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF
310 320 330 340 350
TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV
360 370 380 390 400
LCYLHDVKNI LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS
410 420 430 440 450
FLSPGVIYHC DLTKEELEPM VFREVTVKGI DAADYQTIQI FYPSKDGTKI
460 470 480 490 500
PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA
510 520 530 540 550
VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI
560 570 580 590 600
NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG
610 620 630 640 650
CSDTKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL
660 670 680 690 700
KFIATLQYIV GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI
710
ARCLNIEWIQ
Length:710
Mass (Da):80,752
Last modified:May 1, 2000 - v1
Checksum:i1B010D5D6CA73C0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9QUR6. 1 interaction.
MINTiMINT-1854903.
STRINGi10090.ENSMUSP00000097444.

Chemistry

BindingDBiQ9QUR6.
ChEMBLiCHEMBL4935.

Protein family/group databases

ESTHERimouse-ppce. S9N_PPCE_Peptidase_S9.
MEROPSiS09.001.

PTM databases

PhosphoSiteiQ9QUR6.

Proteomic databases

MaxQBiQ9QUR6.
PaxDbiQ9QUR6.
PRIDEiQ9QUR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5550.
MGIiMGI:1270863. Prep.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiPrep. mouse.
NextBioi295594.
PROiQ9QUR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUR6.
CleanExiMM_PREP.
ExpressionAtlasiQ9QUR6. baseline and differential.
GenevisibleiQ9QUR6. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 120 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.