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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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    ESTHERidicdi-DPOA. S9N_PPCE_Peptidase_S9.
    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

    • 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.DDB0185041.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86AS5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    Phylogenomic databases

    eggNOGiCOG1505.
    InParanoidiQ86AS5.
    KOiK01322.
    OMAiVQDYHGH.
    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.DDB0185041.

    Protein family/group databases

    ESTHERidicdi-DPOA. S9N_PPCE_Peptidase_S9.
    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.
    OMAiVQDYHGH.
    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(1999) [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(2005) [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: July 22, 2015
    This is version 85 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.