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 16-JUN-2009, entry version 40. DE RecName: Full=Prolyl endopeptidase; DE EC=3.4.21.26; DE AltName: Full=Post-proline cleaving enzyme; DE AltName: Full=POase; GN Name=prep; Synonyms=dpoA; ORFNames=DDB_G0274387; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ENZYME RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE. RX MEDLINE=99262411; 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 RT elevation 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 MEDLINE=22092622; PubMed=12097910; DOI=10.1038/nature00847; RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., RA Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., RA Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., RA Platzer M., Rosenthal A., 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., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA 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., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA 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 CC acids long (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in CC oligopeptides. CC -!- ENZYME REGULATION: Inhibited by chymostatin, Boc-Glu(NHO-Bz)- CC Pyrrolidide, Z-Pro-L-prolinal dimethyacetal and the peptide H-H-L- CC P-P-P-V-OH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=115 uM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees CC Celsius); CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DISRUPTION PHENOTYPE: Resistance to lithium due to elevation of CC inositol (1,4,5) trisphosphate. CC -!- SIMILARITY: Belongs to the peptidase S9A family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ238018; CAB40787.1; -; mRNA. DR EMBL; AC116956; AAO51127.1; -; Genomic_DNA. DR EMBL; AAFI02000012; EAL70086.1; -; Genomic_DNA. DR RefSeq; XP_644295.1; -. DR HSSP; P23687; 1H2X. DR MEROPS; S09.001; -. DR GeneID; 3395096; -. DR KEGG; ddi:DDB_0185041; -. DR dictyBase; DDB_G0274387; dpoA. DR OMA; Q86AS5; LEWVACV. DR BRENDA; 3.4.21.26; 424. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR002471; Pept_S9_AS. DR InterPro; IPR001375; Peptidase_S9. DR InterPro; IPR002470; Peptidase_S9A. DR InterPro; IPR004106; Peptidase_S9A_N. DR PANTHER; PTHR11757; Peptidase_S9A; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR Pfam; PF02897; Peptidase_S9_N; 1. DR PRINTS; PR00862; PROLIGOPTASE. DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Hydrolase; Protease; Serine protease. FT CHAIN 1 760 Prolyl endopeptidase. FT /FTId=PRO_0000327836. FT ACT_SITE 609 609 Charge relay system (By similarity). FT ACT_SITE 693 693 Charge relay system (By similarity). FT ACT_SITE 730 730 Charge relay system (By similarity). FT CONFLICT 42 42 E -> R (in Ref. 1; CAB40787). FT CONFLICT 402 402 Q -> P (in Ref. 1; CAB40787). FT CONFLICT 600 602 QNK -> PNQ (in Ref. 1; CAB40787). FT CONFLICT 664 664 D -> E (in Ref. 1; CAB40787). FT CONFLICT 681 681 Q -> P (in Ref. 1; CAB40787). FT CONFLICT 739 739 Q -> P (in Ref. 1; CAB40787). 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 //