ID   PPCE_BOVIN              Reviewed;         710 AA.
AC   Q9XTA2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Prolyl endopeptidase;
DE            Short=PE;
DE            EC=3.4.21.26;
DE   AltName: Full=Post-proline cleaving enzyme;
GN   Name=PREP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9353562; DOI=10.1248/bpb.20.1047;
RA   Yoshimoto T., Miyazaki K., Haraguchi N., Kitazono A., Kabashima T., Ito K.;
RT   "Cloning and expression of the cDNA encoding prolyl oligopeptidase (prolyl
RT   endopeptidase) from bovine brain.";
RL   Biol. Pharm. Bull. 20:1047-1050(1997).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB028866; BAA78907.1; -; mRNA.
DR   PIR; JC5877; JC5877.
DR   RefSeq; NP_777197.1; NM_174772.1.
DR   AlphaFoldDB; Q9XTA2; -.
DR   SMR; Q9XTA2; -.
DR   STRING; 9913.ENSBTAP00000021658; -.
DR   BindingDB; Q9XTA2; -.
DR   ChEMBL; CHEMBL2460; -.
DR   ESTHER; bovin-ppce; S9N_PPCE_Peptidase_S9.
DR   MEROPS; S09.001; -.
DR   PaxDb; Q9XTA2; -.
DR   PRIDE; Q9XTA2; -.
DR   GeneID; 286818; -.
DR   KEGG; bta:286818; -.
DR   CTD; 5550; -.
DR   eggNOG; KOG2237; Eukaryota.
DR   InParanoid; Q9XTA2; -.
DR   OrthoDB; 225446at2759; -.
DR   SABIO-RK; Q9XTA2; -.
DR   PRO; PR:Q9XTA2; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070012; F:oligopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..710
FT                   /note="Prolyl endopeptidase"
FT                   /id="PRO_0000122400"
FT   ACT_SITE        554
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        641
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        680
FT                   /note="Charge relay system"
FT                   /evidence="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;  80641 MW;  CB2E7F0DAE2CFE9C CRC64;
     MLSFQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR
     GLYKERMTEL YDYPKYSCNF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVCLDPNTLS
     DDGTVALRGY AFSEDGEYVA YGLSASGSDW VTIKFMKVDG AKELADVLER VKFSCMAWTH
     DGKGMFYNAY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL
     SDDGRYVLLS IREGCDPVNR LWYCDLHQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF
     TFKTNRHSPN YRLINIDFTD PEESRWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNT
     LQLHDMATGA LLKTFPLEVG SVVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR
     VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI
     TPNYSVCRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE
     GYTSPKRLTI NGGSNGGLLV ATCANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG
     CSDNKQHFEW LIKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSP KFIATLQHLV
     GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIDWIQ