PPCE_MOUSE
ID PPCE_MOUSE Reviewed; 710 AA.
AC Q9QUR6; Q80YS1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Prolyl endopeptidase;
DE Short=PE;
DE EC=3.4.21.26;
DE AltName: Full=Post-proline cleaving enzyme;
GN Name=Prep; Synonyms=Pep;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9538240; DOI=10.1093/oxfordjournals.jbchem.a021970;
RA Ishino T., Ohtsuki S., Homma K., Natori S.;
RT "cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA
RT synthesis by Swiss 3T3 cells.";
RL J. Biochem. 123:540-545(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10446174; DOI=10.1074/jbc.274.34.24047;
RA Kimura A., Yoshida I., Takagi N., Takahashi T.;
RT "Structure and localization of the mouse prolyl oligopeptidase gene.";
RL J. Biol. Chem. 274:24047-24053(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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DR EMBL; AB007631; BAA88239.1; -; mRNA.
DR EMBL; AB022053; BAA83071.1; -; Genomic_DNA.
DR EMBL; BC012869; AAH12869.1; -; mRNA.
DR EMBL; BC050830; AAH50830.2; -; mRNA.
DR CCDS; CCDS23826.1; -.
DR PIR; JW0080; JW0080.
DR RefSeq; NP_035286.1; NM_011156.2.
DR AlphaFoldDB; Q9QUR6; -.
DR SMR; Q9QUR6; -.
DR BioGRID; 202358; 5.
DR IntAct; Q9QUR6; 4.
DR STRING; 10090.ENSMUSP00000097444; -.
DR BindingDB; Q9QUR6; -.
DR ChEMBL; CHEMBL4935; -.
DR ESTHER; mouse-ppce; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.001; -.
DR iPTMnet; Q9QUR6; -.
DR PhosphoSitePlus; Q9QUR6; -.
DR SwissPalm; Q9QUR6; -.
DR CPTAC; non-CPTAC-3867; -.
DR EPD; Q9QUR6; -.
DR jPOST; Q9QUR6; -.
DR MaxQB; Q9QUR6; -.
DR PaxDb; Q9QUR6; -.
DR PRIDE; Q9QUR6; -.
DR ProteomicsDB; 291709; -.
DR Antibodypedia; 32113; 218 antibodies from 33 providers.
DR DNASU; 19072; -.
DR Ensembl; ENSMUST00000099858; ENSMUSP00000097444; ENSMUSG00000019849.
DR GeneID; 19072; -.
DR KEGG; mmu:19072; -.
DR UCSC; uc007ezx.1; mouse.
DR CTD; 5550; -.
DR MGI; MGI:1270863; Prep.
DR VEuPathDB; HostDB:ENSMUSG00000019849; -.
DR eggNOG; KOG2237; Eukaryota.
DR GeneTree; ENSGT00530000063426; -.
DR HOGENOM; CLU_011290_1_1_1; -.
DR InParanoid; Q9QUR6; -.
DR OMA; ACMTQRP; -.
DR OrthoDB; 225446at2759; -.
DR PhylomeDB; Q9QUR6; -.
DR TreeFam; TF300655; -.
DR BioGRID-ORCS; 19072; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Prep; mouse.
DR PRO; PR:Q9QUR6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QUR6; protein.
DR Bgee; ENSMUSG00000019849; Expressed in endoderm of midgut and 241 other tissues.
DR ExpressionAtlas; Q9QUR6; baseline and differential.
DR Genevisible; Q9QUR6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0070012; F:oligopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0019538; P:protein metabolic process; ISS:MGI.
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_0000122402"
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; 80752 MW; 1B010D5D6CA73C0E CRC64;
MLSFQYPDVY RDETSVQEYH GHKICDPYSW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNTLS
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFTCMAWTH
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL
SDDGRYVLLS IWEGCDPVNR LWYCDLQQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF
TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNI
LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS FLSPGVIYHC DLTKEELEPM
VFREVTVKGI DAADYQTIQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI
TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE
GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG
CSDTKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV
GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIEWIQ
