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Protein

Prolyl endopeptidase

Gene

prep

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

Enzyme regulationi

Inhibited by chymostatin, Boc-Glu(NHO-Bz)-Pyrrolidide, Z-Pro-L-prolinal dimethyacetal and the peptide H-H-L-P-P-P-V-OH.1 Publication

Kineticsi

  1. KM=115 µM for carbobenzoxy-Gly-Pro-p-nitroanilide (at 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei609 – 6091Charge relay systemPROSITE-ProRule annotation
Active sitei693 – 6931Charge relay systemPROSITE-ProRule annotation
Active sitei730 – 7301Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. oligopeptidase activity Source: dictyBase
  2. serine-type endopeptidase activity Source: InterPro
  3. serine-type exopeptidase activity Source: InterPro

GO - Biological processi

  1. proteolysis Source: dictyBase
  2. regulation of signal transduction Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS09.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl endopeptidase (EC:3.4.21.26)
Short name:
PE
Alternative name(s):
POase
Post-proline cleaving enzyme
Gene namesi
Name:prep
Synonyms:dpoA
ORF Names:DDB_G0274387
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0274387. dpoA.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Resistance to lithium due to elevation of inositol (1,4,5) trisphosphate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 760760Prolyl endopeptidasePRO_0000327836Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB_0185041.

Structurei

3D structure databases

ProteinModelPortaliQ86AS5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.Curated

Phylogenomic databases

eggNOGiCOG1505.
InParanoidiQ86AS5.
KOiK01322.
OMAiWHEAGSK.
PhylomeDBiQ86AS5.

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86AS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFNYPETRR DDSVFDIFKS TEKGSVKVYD PYRHLEDQQS PETKKWVDEE
60 70 80 90 100
NKITRSFLDQ DNTSEKISNE IMKMLNFERF DWFRRRGSKL FFSRNPNTLN
110 120 130 140 150
QNIIYLIDID QISISKDGKS SAKGFENAIE FLNPNTYSKD GTWSLKSFVI
160 170 180 190 200
SKSGDHVCFS YSKAGSDWEE IAVKKIITTN ELKTNKDDEE EKEDLKKKNC
210 220 230 240 250
LHYAVVDLPD SINWCKFTSI KWDENETGFI YNRYPKPEKV SDDDKGTETD
260 270 280 290 300
TNLNNKVYYH KLGDANESFD RVVFECPENP QWIFGTEFSH DHSSLFISAF
310 320 330 340 350
RDCNVEHNLY VIRNFQEAIA NKSAFKVEAL IDNFDACYYY ITNTKQGEYF
360 370 380 390 400
FLTNLSAPFN RLISIQLNDD QPIVPNSKSK LEFKEIIPEK DYVLESVSRS
410 420 430 440 450
SQEKFYVSYQ KHVQDIIEVY DFNGKYLKDI KLPGPGSASL SATEYHDHIF
460 470 480 490 500
INFSNLVSPS VTYYMDSKND ELLLFKEPHI EGFKSSDYEC KQVFYESPKD
510 520 530 540 550
KTKIPMFIAY KKTTDITSGN APTYMTGYGG FNISYTQSFS IRNIYFLNKF
560 570 580 590 600
NGIFVIANIR GGGEYGKAWH EAGSKKNKQN CFDDFIGAAE YLIKENYTNQ
610 620 630 640 650
NKLAVRGGSN GGLLMGAISN QRPDLFKCVV ADVGVMDMLR FHLHTIGSNW
660 670 680 690 700
VSDYGRSDNP DDFDVLIKYS PLNNVPKDSN QYPSIMLCTG DHDDRVIPAH
710 720 730 740 750
SYKFISELQY QLGKKVDTPL LIRVDKDSGH GAGKGLSKQN NEIADIFNFF
760
SKVLNVKLNF
Length:760
Mass (Da):87,555
Last modified:June 1, 2003 - v1
Checksum:iF8DD6D07A348F382
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421E → R in CAB40787 (PubMed:10329620).Curated
Sequence conflicti402 – 4021Q → P in CAB40787 (PubMed:10329620).Curated
Sequence conflicti600 – 6023QNK → PNQ in CAB40787 (PubMed:10329620).Curated
Sequence conflicti664 – 6641D → E in CAB40787 (PubMed:10329620).Curated
Sequence conflicti681 – 6811Q → P in CAB40787 (PubMed:10329620).Curated
Sequence conflicti739 – 7391Q → P in CAB40787 (PubMed:10329620).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238018 mRNA. Translation: CAB40787.1.
AAFI02000012 Genomic DNA. Translation: EAL70086.1.
RefSeqiXP_644295.1. XM_639203.1.

Genome annotation databases

EnsemblProtistsiDDB0185041; DDB0185041; DDB_G0274387.
GeneIDi8619723.
KEGGiddi:DDB_G0274387.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238018 mRNA. Translation: CAB40787.1.
AAFI02000012 Genomic DNA. Translation: EAL70086.1.
RefSeqiXP_644295.1. XM_639203.1.

3D structure databases

ProteinModelPortaliQ86AS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0185041.

Protein family/group databases

MEROPSiS09.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0185041; DDB0185041; DDB_G0274387.
GeneIDi8619723.
KEGGiddi:DDB_G0274387.

Organism-specific databases

dictyBaseiDDB_G0274387. dpoA.

Phylogenomic databases

eggNOGiCOG1505.
InParanoidiQ86AS5.
KOiK01322.
OMAiWHEAGSK.
PhylomeDBiQ86AS5.

Miscellaneous databases

PROiQ86AS5.

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
  2. 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiPPCE_DICDI
AccessioniPrimary (citable) accession number: Q86AS5
Secondary accession number(s): Q554M8, Q9XZR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2003
Last modified: April 1, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.