PPCE_DICDI
ID PPCE_DICDI Reviewed; 760 AA.
AC Q86AS5; Q554M8; Q9XZR9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Prolyl endopeptidase;
DE Short=PE;
DE EC=3.4.21.26;
DE AltName: Full=POase;
DE AltName: Full=Post-proline cleaving enzyme;
GN Name=prep; Synonyms=dpoA; ORFNames=DDB_G0274387;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=10329620; DOI=10.1093/emboj/18.10.2734;
RA Williams R.S.B., Eames M., Ryves W.J., Viggars J., Harwood A.J.;
RT "Loss of a prolyl oligopeptidase confers resistance to lithium by elevation
RT of inositol (1,4,5) trisphosphate.";
RL EMBO J. 18:2734-2745(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26;
CC -!- ACTIVITY REGULATION: Inhibited by chymostatin, Boc-Glu(NHO-Bz)-
CC Pyrrolidide, Z-Pro-L-prolinal dimethyacetal and the peptide H-H-L-P-P-
CC P-V-OH. {ECO:0000269|PubMed:10329620}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=115 uM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:10329620};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10329620}.
CC -!- DISRUPTION PHENOTYPE: Resistance to lithium due to elevation of
CC inositol (1,4,5) trisphosphate. {ECO:0000269|PubMed:10329620}.
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; AJ238018; CAB40787.1; -; mRNA.
DR EMBL; AAFI02000012; EAL70086.1; -; Genomic_DNA.
DR RefSeq; XP_644295.1; XM_639203.1.
DR AlphaFoldDB; Q86AS5; -.
DR SMR; Q86AS5; -.
DR STRING; 44689.DDB0185041; -.
DR ESTHER; dicdi-DPOA; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.B02; -.
DR PaxDb; Q86AS5; -.
DR PRIDE; Q86AS5; -.
DR EnsemblProtists; EAL70086; EAL70086; DDB_G0274387.
DR GeneID; 8619723; -.
DR KEGG; ddi:DDB_G0274387; -.
DR dictyBase; DDB_G0274387; dpoA.
DR eggNOG; KOG2237; Eukaryota.
DR HOGENOM; CLU_011290_1_1_1; -.
DR InParanoid; Q86AS5; -.
DR OMA; ACMTQRP; -.
DR PhylomeDB; Q86AS5; -.
DR PRO; PR:Q86AS5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0070012; F:oligopeptidase activity; IDA:dictyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:dictyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:0010226; P:response to lithium ion; IMP:dictyBase.
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 Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..760
FT /note="Prolyl endopeptidase"
FT /id="PRO_0000327836"
FT ACT_SITE 609
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 693
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 730
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CONFLICT 42
FT /note="E -> R (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Q -> P (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
FT CONFLICT 600..602
FT /note="QNK -> PNQ (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="D -> E (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="Q -> P (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="Q -> P (in Ref. 1; CAB40787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 87555 MW; F8DD6D07A348F382 CRC64;
MKFNYPETRR DDSVFDIFKS TEKGSVKVYD PYRHLEDQQS PETKKWVDEE NKITRSFLDQ
DNTSEKISNE IMKMLNFERF DWFRRRGSKL FFSRNPNTLN QNIIYLIDID QISISKDGKS
SAKGFENAIE FLNPNTYSKD GTWSLKSFVI SKSGDHVCFS YSKAGSDWEE IAVKKIITTN
ELKTNKDDEE EKEDLKKKNC LHYAVVDLPD SINWCKFTSI KWDENETGFI YNRYPKPEKV
SDDDKGTETD TNLNNKVYYH KLGDANESFD RVVFECPENP QWIFGTEFSH DHSSLFISAF
RDCNVEHNLY VIRNFQEAIA NKSAFKVEAL IDNFDACYYY ITNTKQGEYF FLTNLSAPFN
RLISIQLNDD QPIVPNSKSK LEFKEIIPEK DYVLESVSRS SQEKFYVSYQ KHVQDIIEVY
DFNGKYLKDI KLPGPGSASL SATEYHDHIF INFSNLVSPS VTYYMDSKND ELLLFKEPHI
EGFKSSDYEC KQVFYESPKD KTKIPMFIAY KKTTDITSGN APTYMTGYGG FNISYTQSFS
IRNIYFLNKF NGIFVIANIR GGGEYGKAWH EAGSKKNKQN CFDDFIGAAE YLIKENYTNQ
NKLAVRGGSN GGLLMGAISN QRPDLFKCVV ADVGVMDMLR FHLHTIGSNW VSDYGRSDNP
DDFDVLIKYS PLNNVPKDSN QYPSIMLCTG DHDDRVIPAH SYKFISELQY QLGKKVDTPL
LIRVDKDSGH GAGKGLSKQN NEIADIFNFF SKVLNVKLNF
