Reviewed, UniProtKB/Swiss-Prot Q86AS5 (PPCE_DICDI)

Names and origin

Protein names

Recommended name:
    Prolyl endopeptidase
    EC=3.4.21.26
Alternative name(s):
    Post-proline cleaving enzyme
    POase

Gene names

Name:	prep
Synonyms:	dpoA
ORF Names:	DDB_G0274387

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long By similarity.
Catalytic activity	Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
Enzyme regulation	Inhibited by chymostatin, Boc-Glu(NHO-Bz)-Pyrrolidide, Z-Pro-L-prolinal dimethyacetal and the peptide H-H-L-P-P-P-V-OH. Ref.1
Subcellular location	Cytoplasm. Ref.1
Disruption phenotype	Resistance to lithium due to elevation of inositol (1,4,5) trisphosphate. Ref.1
Sequence similarities	Belongs to the peptidase S9A family.
biophysicochemical properties	Kinetic parameters: KM=115 µM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees Celsius)

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 760	760	Prolyl endopeptidase		PRO_0000327836
Sites
	Active site	609	1	Charge relay system By similarity
	Active site	693	1	Charge relay system By similarity
	Active site	730	1	Charge relay system By similarity
Experimental info
	Sequence conflict	42	1	E → R in CAB40787. Ref.1
	Sequence conflict	402	1	Q → P in CAB40787. Ref.1
	Sequence conflict	600 – 602	3	QNK → PNQ in CAB40787. Ref.1
	Sequence conflict	664	1	D → E in CAB40787. Ref.1
	Sequence conflict	681	1	Q → P in CAB40787. Ref.1
	Sequence conflict	739	1	Q → P in CAB40787. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q86AS5-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F8DD6D07A348F382	FASTA	760	87,555
	10 20 30 40 50 60 MKFNYPETRR DDSVFDIFKS TEKGSVKVYD PYRHLEDQQS PETKKWVDEE NKITRSFLDQ 70 80 90 100 110 120 DNTSEKISNE IMKMLNFERF DWFRRRGSKL FFSRNPNTLN QNIIYLIDID QISISKDGKS 130 140 150 160 170 180 SAKGFENAIE FLNPNTYSKD GTWSLKSFVI SKSGDHVCFS YSKAGSDWEE IAVKKIITTN 190 200 210 220 230 240 ELKTNKDDEE EKEDLKKKNC LHYAVVDLPD SINWCKFTSI KWDENETGFI YNRYPKPEKV 250 260 270 280 290 300 SDDDKGTETD TNLNNKVYYH KLGDANESFD RVVFECPENP QWIFGTEFSH DHSSLFISAF 310 320 330 340 350 360 RDCNVEHNLY VIRNFQEAIA NKSAFKVEAL IDNFDACYYY ITNTKQGEYF FLTNLSAPFN 370 380 390 400 410 420 RLISIQLNDD QPIVPNSKSK LEFKEIIPEK DYVLESVSRS SQEKFYVSYQ KHVQDIIEVY 430 440 450 460 470 480 DFNGKYLKDI KLPGPGSASL SATEYHDHIF INFSNLVSPS VTYYMDSKND ELLLFKEPHI 490 500 510 520 530 540 EGFKSSDYEC KQVFYESPKD KTKIPMFIAY KKTTDITSGN APTYMTGYGG FNISYTQSFS 550 560 570 580 590 600 IRNIYFLNKF NGIFVIANIR GGGEYGKAWH EAGSKKNKQN CFDDFIGAAE YLIKENYTNQ 610 620 630 640 650 660 NKLAVRGGSN GGLLMGAISN QRPDLFKCVV ADVGVMDMLR FHLHTIGSNW VSDYGRSDNP 670 680 690 700 710 720 DDFDVLIKYS PLNNVPKDSN QYPSIMLCTG DHDDRVIPAH SYKFISELQY QLGKKVDTPL 730 740 750 760 LIRVDKDSGH GAGKGLSKQN NEIADIFNFF SKVLNVKLNF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate." Williams R.S.B., Eames M., Ryves W.J., Viggars J., Harwood A.J. EMBO J. 18:2734-2745(1999) [PubMed: 10329620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
[2]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ238018 mRNA. Translation: CAB40787.1. AC116956 Genomic DNA. Translation: AAO51127.1. AAFI02000012 Genomic DNA. Translation: EAL70086.1.
RefSeq	XP_644295.1.
3D structure databases
HSSP	HSSP built from PDB template 1H2X based on UniProtKB P23687.
ModBase	Search...
Protein family/group databases
MEROPS	S09.001.
Genome annotation databases
GeneID	3395096.
KEGG	ddi:DDB_0185041.
Organism-specific databases
dictyBase	DDB_G0274387. dpoA.
Phylogenomic databases
OMA	Q86AS5. LEWVACV.
Enzyme and pathway databases
BRENDA	3.4.21.26. 424.
Family and domain databases
InterPro	IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR002470. Peptidase_S9A. IPR004106. Peptidase_S9A_N. [Graphical view]
PANTHER	PTHR11757. Peptidase_S9A. 1 hit.
Pfam	PF00326. Peptidase_S9. 1 hit. PF02897. Peptidase_S9_N. 1 hit. [Graphical view]
PRINTS	PR00862. PROLIGOPTASE.
PROSITE	PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPCE_DICDI

Accession

Primary (citable) accession number: Q86AS5
Secondary accession number(s): Q554M8, Q9XZR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)