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P23687 (PPCE_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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.

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peptidase S9A family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Serine protease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Compara

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 710710Prolyl endopeptidase
PRO_0000122403

Sites

Active site5541Charge relay system Ref.1
Active site6411Charge relay system
Active site6801Charge relay system Ref.2

Amino acid modifications

Modified residue1571N6-acetyllysine By similarity

Natural variations

Natural variant291A → H.

Secondary structure

1 .............................................................................................................................................. 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23687 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 70286A86238D72C0

FASTA71080,770
        10         20         30         40         50         60 
MLSFQYPDVY RDETAIQDYH GHKVCDPYAW 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 
DGKGMFYNAY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL 

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

       310        320        330        340        350        360 
TFKTNRHSPN YRLINIDFTD PEESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNT 

       370        380        390        400        410        420 
LQLHDLATGA LLKIFPLEVG SVVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR 

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

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

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

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

       670        680        690        700        710 
GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIDWIP

« Hide

References

[1]"cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue."
Rennex D., Hemmings B.A., Hofsteenge J., Stone S.R.
Biochemistry 30:2195-2203(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACTIVE SITE SER-554.
Tissue: Brain.
[2]"Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification."
Stone S.R., Rennex D., Wikstrom P., Shaw E., Hofsteenge J.
Biochem. J. 276:837-840(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE HIS-680.
[3]"Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis."
Fueloep V., Bocskei Z., Polgar L.
Cell 94:161-170(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M64227 mRNA. Translation: AAA31110.1.
PIRA37942.
RefSeqNP_001004050.1. NM_001004050.1.
UniGeneSsc.10442.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5TX-ray1.70A1-710[»]
1E8MX-ray1.50A1-710[»]
1E8NX-ray1.50A1-710[»]
1H2WX-ray1.39A1-710[»]
1H2XX-ray1.49A1-710[»]
1H2YX-ray1.78A1-710[»]
1H2ZX-ray1.65A1-710[»]
1O6FX-ray1.60A1-710[»]
1O6GX-ray1.40A1-710[»]
1QFMX-ray1.40A1-710[»]
1QFSX-ray2.00A1-710[»]
1UOOX-ray2.35A1-710[»]
1UOPX-ray1.85A1-710[»]
1UOQX-ray2.10A1-710[»]
1VZ2X-ray2.20A1-710[»]
1VZ3X-ray1.60A1-710[»]
2XDWX-ray1.35A1-710[»]
3EQ7X-ray2.89A1-710[»]
3EQ8X-ray2.73A1-710[»]
3EQ9X-ray2.47A1-710[»]
4AMYX-ray2.00A1-710[»]
4AMZX-ray2.00A1-710[»]
4AN0X-ray2.20A1-710[»]
4AN1X-ray1.90A1-710[»]
4AX4X-ray1.60A1-710[»]
4BCBX-ray1.70A1-710[»]
4BCCX-ray1.65A1-710[»]
4BCDX-ray1.50A1-710[»]
ProteinModelPortalP23687.
SMRP23687. Positions 1-710.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000004715.

Protein family/group databases

MEROPSS09.001.

Proteomic databases

PaxDbP23687.
PRIDEP23687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID445540.
KEGGssc:445540.

Organism-specific databases

CTD5550.

Phylogenomic databases

eggNOGCOG1505.
HOGENOMHOG000238967.
HOVERGENHBG007251.
KOK01322.
OrthoDBEOG4548Z1.

Gene expression databases

ArrayExpressP23687.

Family and domain databases

Gene3D2.130.10.120. 1 hit.
InterProIPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_oligopept_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
IPR004106. Peptidase_S9A_B_C_N.
[Graphical view]
PANTHERPTHR11757. PTHR11757. 1 hit.
PfamPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSPR00862. PROLIGOPTASE.
SUPFAMSSF50993. Peptidase_S9A_N. 1 hit.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP23687.
ChEMBLCHEMBL2461.
EvolutionaryTraceP23687.

Entry information

Entry namePPCE_PIG
AccessionPrimary (citable) accession number: P23687
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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