PPCE_RAT
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 03-AUG-2022, entry version 120.
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>3.0.co;2-m;
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 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 PRIDE; O70196; -.
DR GeneID; 83471; -.
DR KEGG; rno:83471; -.
DR UCSC; RGD:620841; rat.
DR CTD; 5550; -.
DR RGD; 620841; Prep.
DR InParanoid; O70196; -.
DR OrthoDB; 225446at2759; -.
DR PhylomeDB; O70196; -.
DR BRENDA; 3.4.21.26; 5301.
DR PRO; PR:O70196; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
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; -; 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 Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; SSF53474; 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
