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O70196 (PPCE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolyl endopeptidase

Short name=PE
EC=3.4.21.26
Alternative name(s):
Post-proline cleaving enzyme
rPop
Gene names
Name:Prep
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Enzyme regulation

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

Subcellular location

Cytoplasm By similarity UniProtKB P23687.

Tissue specificity

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

Developmental stage

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

Sequence similarities

Belongs to the peptidase S9A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 710710Prolyl endopeptidase
PRO_0000365637

Sites

Active site5541Charge relay system By similarity UniProtKB P23687
Active site6411Charge relay system By similarity UniProtKB P23687
Active site6801Charge relay system By similarity UniProtKB P23687

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1571N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O70196 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: EE6A6AD78D79174C

FASTA71080,742
        10         20         30         40         50         60 
MLSFQYPDVY RDETSVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR 

        70         80         90        100        110        120 
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNTLS 

       130        140        150        160        170        180 
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFTCMAWTH 

       190        200        210        220        230        240 
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDVLCAEFPD EPKWMGGAEL 

       250        260        270        280        290        300 
SDDGRYVLLS IWEGCDPVNR LWYCDLQQGS NGINGILKWV KLIDNFEGEY DYITNEGTVF 

       310        320        330        340        350        360 
TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLRNVKNI 

       370        380        390        400        410        420 
LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS FLSPGVIYHC DLTREELEPR 

       430        440        450        460        470        480 
VFREVTVKGI DASDYQTIQV FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI 

       490        500        510        520        530        540 
TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE 

       550        560        570        580        590        600 
GYTTSKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG 

       610        620        630        640        650        660 
CSDSKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV 

       670        680        690        700        710 
GRSRKQSNPL LIHVDTKAGH GPGKPTAKVI EEVSDMFAFI ARCLNIEWIQ 

« Hide

References

[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: Wistar.
Tissue: Liver.
[2]Maurya D.K., Bhargava P.
Submitted (JAN-2009) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012759 mRNA. Translation: BAA25544.1.
RefSeqNP_112614.1. NM_031324.1.
UniGeneRn.11058.

3D structure databases

ProteinModelPortalO70196.
SMRO70196. Positions 1-709.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000000360.

Chemistry

BindingDBO70196.
ChEMBLCHEMBL4035.

Protein family/group databases

MEROPSS09.001.

PTM databases

PhosphoSiteO70196.

Proteomic databases

PaxDbO70196.
PRIDEO70196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83471.
KEGGrno:83471.
UCSCRGD:620841. rat.

Organism-specific databases

CTD5550.
RGD620841. Prep.

Phylogenomic databases

eggNOGCOG1505.
HOGENOMHOG000238967.
HOVERGENHBG007251.
KOK01322.
PhylomeDBO70196.

Gene expression databases

GenevestigatorO70196.

Family and domain databases

Gene3D2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERPTHR11757. PTHR11757. 1 hit.
PfamPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSPR00862. PROLIGOPTASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615881.
PROO70196.

Entry information

Entry namePPCE_RAT
AccessionPrimary (citable) accession number: O70196
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries