ID PPCE_PIG Reviewed; 710 AA. AC P23687; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 02-SEP-2026, entry version 170. 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE RP SER-554. RC TISSUE=Brain; RX PubMed=1900195; DOI=10.1021/bi00222a025; RA Rennex D., Hemmings B.A., Hofsteenge J., Stone S.R.; RT "cDNA cloning of porcine brain prolyl endopeptidase and identification of RT the active-site seryl residue."; RL Biochemistry 30:2195-2203(1991). RN [2] RP ACTIVE SITE HIS-680. RX PubMed=2064618; DOI=10.1042/bj2760837; RA Stone S.R., Rennex D., Wikstrom P., Shaw E., Hofsteenge J.; RT "Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics RT of inactivation and identification of sites of modification."; RL Biochem. J. 276:837-840(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). RX PubMed=9695945; DOI=10.1016/s0092-8674(00)81416-6; RA Fueloep V., Bocskei Z., Polgar L.; RT "Prolyl oligopeptidase: an unusual beta-propeller domain regulates RT proteolysis."; RL Cell 94:161-170(1998). 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 -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: The N-terminus is blocked. 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; M64227; AAA31110.1; -; mRNA. DR PIR; A37942; A37942. DR RefSeq; NP_001004050.1; NM_001004050.1. DR PDB; 1E5T; X-ray; 1.70 A; A=1-710. DR PDB; 1E8M; X-ray; 1.50 A; A=1-710. DR PDB; 1E8N; X-ray; 1.50 A; A=1-710. DR PDB; 1H2W; X-ray; 1.39 A; A=1-710. DR PDB; 1H2X; X-ray; 1.49 A; A=1-710. DR PDB; 1H2Y; X-ray; 1.78 A; A=1-710. DR PDB; 1H2Z; X-ray; 1.65 A; A=1-710. DR PDB; 1O6F; X-ray; 1.60 A; A=1-710. DR PDB; 1O6G; X-ray; 1.40 A; A=1-710. DR PDB; 1QFM; X-ray; 1.40 A; A=1-710. DR PDB; 1QFS; X-ray; 2.00 A; A=1-710. DR PDB; 1UOO; X-ray; 2.35 A; A=1-710. DR PDB; 1UOP; X-ray; 1.85 A; A=1-710. DR PDB; 1UOQ; X-ray; 2.10 A; A=1-710. DR PDB; 1VZ2; X-ray; 2.20 A; A=1-710. DR PDB; 1VZ3; X-ray; 1.60 A; A=1-710. DR PDB; 2XDW; X-ray; 1.35 A; A=1-710. DR PDB; 3EQ7; X-ray; 2.89 A; A=1-710. DR PDB; 3EQ8; X-ray; 2.73 A; A=1-710. DR PDB; 3EQ9; X-ray; 2.47 A; A=1-710. DR PDB; 4AMY; X-ray; 2.00 A; A=1-710. DR PDB; 4AMZ; X-ray; 2.00 A; A=1-710. DR PDB; 4AN0; X-ray; 2.20 A; A=1-710. DR PDB; 4AN1; X-ray; 1.90 A; A=1-710. DR PDB; 4AX4; X-ray; 1.60 A; A=1-710. DR PDB; 4BCB; X-ray; 1.70 A; A=1-710. DR PDB; 4BCC; X-ray; 1.65 A; A=1-710. DR PDB; 4BCD; X-ray; 1.50 A; A=1-710. DR AlphaFoldDB; P23687; -. DR MDposit; P23687; -. DR MDRepo; P23687; -. DR SMR; P23687; -. DR FunCoup; P23687; 1469. DR STRING; 9823.ENSSSCP00000042303; -. DR BindingDB; P23687; -. DR ChEMBL; CHEMBL2461; -. DR ESTHER; pig-ppce; S9N_PPCE_Peptidase_S9. DR MEROPS; S09.001; -. DR PaxDb; 9823-ENSSSCP00000042303; -. DR PeptideAtlas; P23687; -. DR Ensembl; ENSSSCT00000004829.5; ENSSSCP00000004715.4; ENSSSCG00000004368.5. DR Ensembl; ENSSSCT00055025909.1; ENSSSCP00055020588.1; ENSSSCG00055013045.1. DR GeneID; 445540; -. DR KEGG; ssc:445540; -. DR CTD; 5550; -. DR eggNOG; KOG2237; Eukaryota. DR GeneTree; ENSGT00530000063426; -. DR HOGENOM; CLU_011290_1_2_1; -. DR InParanoid; P23687; -. DR OMA; LDPWFSH; -. DR OrthoDB; 248387at2759; -. DR BRENDA; 3.4.21.26; 6170. DR EvolutionaryTrace; P23687; -. DR PRO; PR:P23687; -. DR Proteomes; UP000008227; Chromosome 1. DR ExpressionAtlas; P23687; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR FunFam; 2.130.10.120:FF:000001; Prolyl endopeptidase; 1. DR FunFam; 3.40.50.1820:FF:000005; Prolyl endopeptidase; 1. DR FunFam; 3.40.50.1820:FF:000275; Prolyl endopeptidase; 1. 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_fold. DR InterPro; IPR002471; Pept_S9_AS. DR InterPro; IPR023302; Pept_S9A_N. DR InterPro; IPR001375; Peptidase_S9_cat. DR InterPro; IPR004106; Peptidase_S9_N_sf. DR InterPro; IPR002470; Peptidase_S9A. DR InterPro; IPR051167; Prolyl_oligopep/macrocyclase. 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. DR PDBsum; 1E5T; -. DR PDBsum; 1E8M; -. DR PDBsum; 1E8N; -. DR PDBsum; 1H2W; -. DR PDBsum; 1H2X; -. DR PDBsum; 1H2Y; -. DR PDBsum; 1H2Z; -. DR PDBsum; 1O6F; -. DR PDBsum; 1O6G; -. DR PDBsum; 1QFM; -. DR PDBsum; 1QFS; -. DR PDBsum; 1UOO; -. DR PDBsum; 1UOP; -. DR PDBsum; 1UOQ; -. DR PDBsum; 1VZ2; -. DR PDBsum; 1VZ3; -. DR PDBsum; 2XDW; -. DR PDBsum; 3EQ7; -. DR PDBsum; 3EQ8; -. DR PDBsum; 3EQ9; -. DR PDBsum; 4AMY; -. DR PDBsum; 4AMZ; -. DR PDBsum; 4AN0; -. DR PDBsum; 4AN1; -. DR PDBsum; 4AX4; -. DR PDBsum; 4BCB; -. DR PDBsum; 4BCC; -. DR PDBsum; 4BCD; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; KW Protease; Reference proteome; Serine protease. FT CHAIN 1..710 FT /note="Prolyl endopeptidase" FT /id="PRO_0000122403" FT ACT_SITE 554 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, FT ECO:0000269|PubMed:1900195" FT ACT_SITE 641 FT /note="Charge relay system" FT ACT_SITE 680 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, FT ECO:0000269|PubMed:2064618" 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" FT VARIANT 29 FT /note="A -> H" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 16..19 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 22..25 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:3EQ8" FT HELIX 37..56 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 59..71 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:1QFM" FT STRAND 125..132 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 136..145 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:2XDW" FT TURN 158..161 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 162..171 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:4AX4" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 246..252 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 290..296 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 299..304 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 312..317 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 323..325 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 337..344 FT /evidence="ECO:0007829|PDB:2XDW" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 348..355 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 358..365 FT /evidence="ECO:0007829|PDB:2XDW" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 371..375 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 379..386 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 392..399 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:1H2W" FT STRAND 406..411 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 420..424 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:4AX4" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 435..443 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:3EQ8" FT STRAND 449..457 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 468..471 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 486..495 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 498..502 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:3EQ7" FT HELIX 511..516 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 520..522 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 524..539 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 545..547 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 548..553 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 555..566 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 568..570 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 572..578 FT /evidence="ECO:0007829|PDB:2XDW" FT TURN 583..585 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 592..595 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 596..599 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 605..614 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 616..618 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 624..627 FT /evidence="ECO:0007829|PDB:3EQ8" FT STRAND 632..638 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 642..644 FT /evidence="ECO:0007829|PDB:1O6G" FT HELIX 647..655 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 656..661 FT /evidence="ECO:0007829|PDB:2XDW" FT STRAND 663..665 FT /evidence="ECO:0007829|PDB:3EQ9" FT STRAND 670..677 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 686..704 FT /evidence="ECO:0007829|PDB:2XDW" FT HELIX 706..708 FT /evidence="ECO:0007829|PDB:2XDW" SQ SEQUENCE 710 AA; 80770 MW; 70286A86238D72C0 CRC64; MLSFQYPDVY RDETAIQDYH GHKVCDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNILS DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFSCMAWTH DGKGMFYNAY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS IREGCDPVNR LWYCDLQQES NGITGILKWV KLIDNFEGEY DYVTNEGTVF TFKTNRHSPN YRLINIDFTD PEESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNT LQLHDLATGA LLKIFPLEVG SVVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI NGGSNGGLLV ATCANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG CSDSKQHFEW LIKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIDWIP //