ID   PPCE_RAT                Reviewed;         710 AA.
AC   O70196;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000250|UniProtKB:P23687};
DE            Short=PE {ECO:0000250|UniProtKB:P23687};
DE            EC=3.4.21.26;
DE   AltName: Full=Post-proline cleaving enzyme {ECO:0000250|UniProtKB:P23687};
DE   AltName: Full=rPop;
GN   Name=Prep {ECO:0000312|RGD:620841};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA25544.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Wistar {ECO:0000269|PubMed:10766975};
RC   TISSUE=Liver {ECO:0000269|PubMed:10766975};
RX   PubMed=10766975;
RX   DOI=10.1002/(sici)1097-010x(20000501)286:6<656::aid-jez13>3.3.co;2-d;
RA   Kimura A., Takahashi T.;
RT   "cDNA cloning of rat prolyl oligopeptidase and its expression in the ovary
RT   during the estrous cycle.";
RL   J. Exp. Zool. 286:656-665(2000).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Maurya D.K., Bhargava P.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl
CC       residues within peptides that are up to approximately 30 amino acids
CC       long. Has high activity on the succinyl- (suc-) peptide-4-
CC       methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA,
CC       suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA. {ECO:0000269|PubMed:10766975}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000269|PubMed:10766975};
CC   -!- ACTIVITY REGULATION: Inhibited by DFP, Z-Pro-prolinal and poststatin,
CC       but not by PMSF, SBTI, EDTA, leupeptin, E-64 and pepstatin.
CC       {ECO:0000269|PubMed:10766975}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23687}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested: uterus, kidney,
CC       heart, lung, small intestine, smooth muscle, liver, spleen, thymus,
CC       adrenal, pituitary and whole brain. {ECO:0000269|PubMed:10766975}.
CC   -!- DEVELOPMENTAL STAGE: In the estrous cycle, expression and activity are
CC       highest in the luteal phase. {ECO:0000269|PubMed:10766975}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000255}.
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DR   EMBL; AB012759; BAA25544.1; -; mRNA.
DR   RefSeq; NP_112614.1; NM_031324.1.
DR   AlphaFoldDB; O70196; -.
DR   SMR; O70196; -.
DR   STRING; 10116.ENSRNOP00000071906; -.
DR   BindingDB; O70196; -.
DR   ChEMBL; CHEMBL4035; -.
DR   ESTHER; ratno-RPOP; S9N_PPCE_Peptidase_S9.
DR   MEROPS; S09.001; -.
DR   iPTMnet; O70196; -.
DR   PhosphoSitePlus; O70196; -.
DR   jPOST; O70196; -.
DR   GeneID; 83471; -.
DR   KEGG; rno:83471; -.
DR   UCSC; RGD:620841; rat.
DR   AGR; RGD:620841; -.
DR   CTD; 5550; -.
DR   RGD; 620841; Prep.
DR   InParanoid; O70196; -.
DR   OrthoDB; 7264at2759; -.
DR   PhylomeDB; O70196; -.
DR   BRENDA; 3.4.21.26; 5301.
DR   PRO; PR:O70196; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR   GO; GO:0070012; F:oligopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IDA:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..710
FT                   /note="Prolyl endopeptidase"
FT                   /id="PRO_0000365637"
FT   ACT_SITE        554
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23687,
FT                   ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        641
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23687,
FT                   ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        680
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P23687,
FT                   ECO:0000255|PROSITE-ProRule:PRU10084"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P48147"
FT   MOD_RES         157
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P48147"
SQ   SEQUENCE   710 AA;  80742 MW;  EE6A6AD78D79174C CRC64;
     MLSFQYPDVY RDETSVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR
     GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNTLS
     DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFTCMAWTH
     DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDVLCAEFPD EPKWMGGAEL
     SDDGRYVLLS IWEGCDPVNR LWYCDLQQGS NGINGILKWV KLIDNFEGEY DYITNEGTVF
     TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLRNVKNI
     LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS FLSPGVIYHC DLTREELEPR
     VFREVTVKGI DASDYQTIQV FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI
     TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE
     GYTTSKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG
     CSDSKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV
     GRSRKQSNPL LIHVDTKAGH GPGKPTAKVI EEVSDMFAFI ARCLNIEWIQ
//