PPCE_PIG
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 03-AUG-2022, entry version 153.
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}.
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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 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; -.
DR AlphaFoldDB; P23687; -.
DR SMR; P23687; -.
DR STRING; 9823.ENSSSCP00000004715; -.
DR BindingDB; P23687; -.
DR ChEMBL; CHEMBL2461; -.
DR ESTHER; pig-ppce; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.001; -.
DR PaxDb; P23687; -.
DR PeptideAtlas; P23687; -.
DR PRIDE; P23687; -.
DR Ensembl; ENSSSCT00055025909; ENSSSCP00055020588; ENSSSCG00055013045.
DR GeneID; 445540; -.
DR KEGG; ssc:445540; -.
DR CTD; 5550; -.
DR eggNOG; KOG2237; Eukaryota.
DR HOGENOM; CLU_011290_1_2_1; -.
DR InParanoid; P23687; -.
DR OMA; ACMTQRP; -.
DR BRENDA; 3.4.21.26; 6170.
DR EvolutionaryTrace; P23687; -.
DR PRO; PR:P23687; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P23687; SS.
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 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 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 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 STRAND 198..200
FT /evidence="ECO:0007829|PDB:2XDW"
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 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 HELIX 511..516
FT /evidence="ECO:0007829|PDB:2XDW"
FT HELIX 520..523
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..659
FT /evidence="ECO:0007829|PDB:2XDW"
FT TURN 660..662
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"
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
