[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND KNOCKOUT. DOI=10.1093/emboj/18.10.2734; PubMed=10329620 [NCBI, ExPASy, EBI, Israel, Japan] Williams R.S.B., Eames M., Ryves W.J., Viggars J., Harwood A.J.; "Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate."; EMBO J. 18:2734-2745(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AX4; DOI=10.1038/nature00847; PubMed=12097910 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; Nature 418:79-85(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AX4; DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The genome of the social amoeba Dictyostelium discoideum."; Nature 435:43-57(2005).

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.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=115 µM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees Celsius);
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Cells lacking dpoA display resistance to lithium due to elevation of inositol (1,4,5) trisphosphate.
SIMILARITY: Belongs to the peptidase S9A family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ238018; CAB40787.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC116956; AAO51127.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000012; EAL70086.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_644295.1; -.

3D structure databases

HSSP

P23687; 1H2X. [HSSP ENTRY / PDB]

ModBase

Q86AS5.

Protein family/group databases

MEROPS

S09.001; -.

Organism-specific databases

dictyBase

DDB0185041; dpoA.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from dictyBase).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0009966;	Biological process: regulation of signal transduction (inferred from mutant phenotype from dictyBase).
QuickGo view.

Family and domain databases

InterPro

IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002470; Peptidase_S9A.
IPR004106; Peptidase_S9A_N.
Graphical view of domain structure.

PANTHER

PTHR11757; Peptidase_S9A; 1.

Pfam

PF00326; Peptidase_S9; 1.
PF02897; Peptidase_S9_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00862; PROLIGOPTASE.

PROSITE

PS00708; PRO_ENDOPEP_SER; 1.

ProtoNet

Q86AS5.

Genome annotation databases

GeneID

3395096; -.

KEGG

ddi:DDB_0185041; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Hydrolase; Protease; Serine protease.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 760`	`760`	`Prolyl endopeptidase.`	`PRO_0000327836`
`ACT_SITE`	`609 609`		`Charge relay system (By similarity).`
`ACT_SITE`	`693 693`		`Charge relay system (By similarity).`
`ACT_SITE`	`730 730`		`Charge relay system (By similarity).`
`CONFLICT`	`42 42`		`E -> R (in Ref. 1; CAB40787).`
`CONFLICT`	`402 402`		`Q -> P (in Ref. 1; CAB40787).`
`CONFLICT`	`600 602`		`QNK -> PNQ (in Ref. 1; CAB40787).`
`CONFLICT`	`664 664`		`D -> E (in Ref. 1; CAB40787).`
`CONFLICT`	`681 681`		`Q -> P (in Ref. 1; CAB40787).`
`CONFLICT`	`739 739`		`Q -> P (in Ref. 1; CAB40787).`

Sequence information

Length: 760 AA [This is the length of the unprocessed precursor]

Molecular weight: 87555 Da [This is the MW of the unprocessed precursor]

CRC64: F8DD6D07A348F382 [This is a checksum on the sequence]

        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

Q86AS5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools