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P48147 (PPCE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolyl endopeptidase

Short name=PE
EC=3.4.21.26
Alternative name(s):
Post-proline cleaving enzyme
Gene names
Name:PREP
Synonyms:PEP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Catalytic activity

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

Subunit structure

Monomer. Ref.7

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peptidase S9A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 710710Prolyl endopeptidase
PRO_0000122401

Sites

Active site5541Charge relay system By similarity
Active site6411Charge relay system By similarity
Active site6801Charge relay system By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue1571N6-acetyllysine Ref.8

Natural variations

Natural variant3511L → V.
Corresponds to variant rs12192054 [ dbSNP | Ensembl ].
VAR_047790
Natural variant7061V → I. Ref.2
Corresponds to variant rs1051484 [ dbSNP | Ensembl ].
VAR_047791

Experimental info

Sequence conflict41L → F in CAA52605. Ref.1
Sequence conflict41L → F in BAA04661. Ref.2
Sequence conflict161V → I in BAA04661. Ref.2
Sequence conflict2451R → C in BAA04661. Ref.2
Sequence conflict2981T → A in BAA04661. Ref.2
Sequence conflict3191R → W in CAA52605. Ref.1
Sequence conflict4401I → L in BAA04661. Ref.2
Sequence conflict4591G → S in BAA04661. Ref.2

Secondary structure

................................................................................................................................... 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48147 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 139072B990820B90

FASTA71080,700
        10         20         30         40         50         60 
MLSLQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR 

        70         80         90        100        110        120 
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNILS 

       130        140        150        160        170        180 
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFSCMAWTH 

       190        200        210        220        230        240 
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL 

       250        260        270        280        290        300 
SDDGRYVLLS IREGCDPVNR LWYCDLQQES SGIAGILKWV KLIDNFEGEY DYVTNEGTVF 

       310        320        330        340        350        360 
TFKTNRQSPN YRVINIDFRD PEESKWKVLV PEHEKDVLEW IACVRSNFLV LCYLHDVKNI 

       370        380        390        400        410        420 
LQLHDLTTGA LLKTFPLDVG SIVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR 

       430        440        450        460        470        480 
VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI 

       490        500        510        520        530        540 
TPNYSVSRLI FVRHMGGILA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE 

       550        560        570        580        590        600 
GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG 

       610        620        630        640        650        660 
CSDSKQHFEW LVKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV 

       670        680        690        700        710 
GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNVDWIP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase."
Vanhoof G., Goossens F., Hendriks L., De Meester I., Hendriks D., Vriend G., van Broeckhoven C., Scharpe S.
Gene 149:363-366(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[2]"Molecular cloning and characterization of prolyl endopeptidase from human T cells."
Shirasawa Y., Osawa T., Hirashima A.
J. Biochem. 115:724-729(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-706.
[3]"cDNA cloning and recombinant expression of human brain prolyl oligopeptidase."
Tarrago T., Giralt E.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[7]"The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family."
Goossens F., De Meester I., Vanhoof G., Hendriks D., Vriend G., Scharpe S.
Eur. J. Biochem. 233:432-441(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 136-149, SUBUNIT, CHARACTERIZATION.
Tissue: Lymphocyte.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)."
Haffner C.D., Diaz C.J., Miller A.B., Reid R.A., Madauss K.P., Hassell A., Hanlon M.H., Porter D.J., Becherer J.D., Carter L.H.
Bioorg. Med. Chem. Lett. 18:4360-4363(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 2-710 IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74496 mRNA. Translation: CAA52605.1.
D21102 mRNA. Translation: BAA04661.1.
AY660966 mRNA. Translation: AAV70495.1.
AL590871, AL133406, AL139191 Genomic DNA. Translation: CAH72545.1.
AL139191, AL133406, AL590871 Genomic DNA. Translation: CAI21416.1.
AL133406, AL139191, AL590871 Genomic DNA. Translation: CAI42689.1.
CH471051 Genomic DNA. Translation: EAW48426.1.
BC030636 mRNA. Translation: AAH30636.1.
PIRI38134.
JC2257.
RefSeqNP_002717.3. NM_002726.4.
UniGeneHs.436564.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DDUX-ray1.56A2-710[»]
ProteinModelPortalP48147.
SMRP48147. Positions 2-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111541. 5 interactions.
MINTMINT-5004282.
STRING9606.ENSP00000358106.

Chemistry

BindingDBP48147.
ChEMBLCHEMBL3202.
DrugBankDB00107. Oxytocin.
GuidetoPHARMACOLOGY2395.

Protein family/group databases

MEROPSS09.001.

PTM databases

PhosphoSiteP48147.

Polymorphism databases

DMDM215273868.

Proteomic databases

PaxDbP48147.
PRIDEP48147.

Protocols and materials databases

DNASU5550.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369110; ENSP00000358106; ENSG00000085377.
GeneID5550.
KEGGhsa:5550.
UCSCuc003prc.3. human.

Organism-specific databases

CTD5550.
GeneCardsGC06M105725.
HGNCHGNC:9358. PREP.
HPACAB025414.
HPA031388.
HPA031389.
HPA031390.
MIM600400. gene.
neXtProtNX_P48147.
PharmGKBPA33730.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1505.
HOGENOMHOG000238967.
HOVERGENHBG007251.
InParanoidP48147.
KOK01322.
OMAPAHSFKF.
OrthoDBEOG78PV88.
PhylomeDBP48147.
TreeFamTF300655.

Gene expression databases

BgeeP48147.
CleanExHS_PREP.
GenevestigatorP48147.

Family and domain databases

Gene3D2.130.10.120. 1 hit.
InterProIPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERPTHR11757. PTHR11757. 1 hit.
PfamPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSPR00862. PROLIGOPTASE.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP48147.
GeneWikiProlyl_endopeptidase.
GenomeRNAi5550.
NextBio21508.
PMAP-CutDBQ8N6D4.
PROP48147.
SOURCESearch...

Entry information

Entry namePPCE_HUMAN
AccessionPrimary (citable) accession number: P48147
Secondary accession number(s): Q8N6D4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM