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Protein

Prolyl endopeptidase

Gene

PREP

Organism
Sus scrofa (Pig)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei554Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei641Charge relay system1
Active sitei680Charge relay systemPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.26. 6170.

Protein family/group databases

ESTHERisussc-ppce. 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):
Post-proline cleaving enzyme
Gene namesi
Name:PREP
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001224031 – 710Prolyl endopeptidaseAdd BLAST710

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei157N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23687.
PeptideAtlasiP23687.
PRIDEiP23687.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSSSCG00000004368.
GenevisibleiP23687. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004715.

Chemistry databases

BindingDBiP23687.

Structurei

Secondary structure

1710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Beta strandi22 – 25Combined sources4
Helixi29 – 32Combined sources4
Beta strandi34 – 36Combined sources3
Helixi37 – 56Combined sources20
Helixi59 – 71Combined sources13
Beta strandi80 – 82Combined sources3
Beta strandi85 – 91Combined sources7
Beta strandi99 – 105Combined sources7
Beta strandi111 – 114Combined sources4
Helixi116 – 119Combined sources4
Beta strandi121 – 123Combined sources3
Beta strandi125 – 132Combined sources8
Beta strandi136 – 145Combined sources10
Beta strandi151 – 157Combined sources7
Turni158 – 161Combined sources4
Beta strandi162 – 171Combined sources10
Beta strandi176 – 178Combined sources3
Beta strandi182 – 189Combined sources8
Beta strandi198 – 200Combined sources3
Beta strandi209 – 214Combined sources6
Helixi219 – 221Combined sources3
Beta strandi223 – 226Combined sources4
Beta strandi235 – 240Combined sources6
Beta strandi246 – 252Combined sources7
Beta strandi254 – 257Combined sources4
Beta strandi260 – 265Combined sources6
Helixi266 – 268Combined sources3
Beta strandi269 – 273Combined sources5
Beta strandi280 – 283Combined sources4
Beta strandi285 – 288Combined sources4
Beta strandi290 – 296Combined sources7
Beta strandi299 – 304Combined sources6
Beta strandi312 – 317Combined sources6
Helixi323 – 325Combined sources3
Beta strandi327 – 330Combined sources4
Beta strandi337 – 344Combined sources8
Turni345 – 347Combined sources3
Beta strandi348 – 355Combined sources8
Beta strandi358 – 365Combined sources8
Turni366 – 368Combined sources3
Beta strandi371 – 375Combined sources5
Beta strandi379 – 386Combined sources8
Beta strandi392 – 399Combined sources8
Beta strandi401 – 403Combined sources3
Beta strandi406 – 411Combined sources6
Beta strandi414 – 416Combined sources3
Beta strandi420 – 424Combined sources5
Beta strandi428 – 430Combined sources3
Helixi432 – 434Combined sources3
Beta strandi435 – 443Combined sources9
Beta strandi445 – 447Combined sources3
Beta strandi449 – 457Combined sources9
Beta strandi468 – 471Combined sources4
Helixi486 – 495Combined sources10
Beta strandi498 – 502Combined sources5
Helixi511 – 516Combined sources6
Helixi520 – 523Combined sources4
Helixi524 – 539Combined sources16
Helixi545 – 547Combined sources3
Beta strandi548 – 553Combined sources6
Helixi555 – 566Combined sources12
Helixi568 – 570Combined sources3
Beta strandi572 – 578Combined sources7
Turni583 – 585Combined sources3
Helixi586 – 588Combined sources3
Helixi592 – 595Combined sources4
Helixi596 – 599Combined sources4
Helixi605 – 614Combined sources10
Helixi616 – 618Combined sources3
Beta strandi624 – 627Combined sources4
Beta strandi632 – 638Combined sources7
Beta strandi642 – 644Combined sources3
Helixi647 – 659Combined sources13
Turni660 – 662Combined sources3
Beta strandi663 – 665Combined sources3
Beta strandi670 – 677Combined sources8
Helixi686 – 704Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP23687.
SMRiP23687.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23687.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.Curated

Phylogenomic databases

eggNOGiKOG2237. Eukaryota.
COG1505. LUCA.
HOGENOMiHOG000238967.
HOVERGENiHBG007251.
InParanoidiP23687.
KOiK01322.
OrthoDBiEOG091G023D.

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.

P23687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFQYPDVY RDETAIQDYH GHKVCDPYAW LEDPDSEQTK AFVEAQNKIT
60 70 80 90 100
VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL
110 120 130 140 150
YVQDSLEGEA RVFLDPNILS DDGTVALRGY AFSEDGEYFA YGLSASGSDW
160 170 180 190 200
VTIKFMKVDG AKELPDVLER VKFSCMAWTH DGKGMFYNAY PQQDGKSDGT
210 220 230 240 250
ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS
260 270 280 290 300
IREGCDPVNR LWYCDLQQES NGITGILKWV KLIDNFEGEY DYVTNEGTVF
310 320 330 340 350
TFKTNRHSPN YRLINIDFTD PEESKWKVLV PEHEKDVLEW VACVRSNFLV
360 370 380 390 400
LCYLHDVKNT LQLHDLATGA LLKIFPLEVG SVVGYSGQKK DTEIFYQFTS
410 420 430 440 450
FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI
460 470 480 490 500
PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGVLA
510 520 530 540 550
VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI
560 570 580 590 600
NGGSNGGLLV ATCANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG
610 620 630 640 650
CSDSKQHFEW LIKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL
660 670 680 690 700
KFIATLQYIV GRSRKQNNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI
710
ARCLNIDWIP
Length:710
Mass (Da):80,770
Last modified:November 1, 1991 - v1
Checksum:i70286A86238D72C0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti29A → H.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64227 mRNA. Translation: AAA31110.1.
PIRiA37942.
RefSeqiNP_001004050.1. NM_001004050.1.
UniGeneiSsc.10442.

Genome annotation databases

GeneIDi445540.
KEGGissc:445540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64227 mRNA. Translation: AAA31110.1.
PIRiA37942.
RefSeqiNP_001004050.1. NM_001004050.1.
UniGeneiSsc.10442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP23687.
SMRiP23687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004715.

Chemistry databases

BindingDBiP23687.
ChEMBLiCHEMBL2461.

Protein family/group databases

ESTHERisussc-ppce. S9N_PPCE_Peptidase_S9.
MEROPSiS09.001.

Proteomic databases

PaxDbiP23687.
PeptideAtlasiP23687.
PRIDEiP23687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi445540.
KEGGissc:445540.

Organism-specific databases

CTDi5550.

Phylogenomic databases

eggNOGiKOG2237. Eukaryota.
COG1505. LUCA.
HOGENOMiHOG000238967.
HOVERGENiHBG007251.
InParanoidiP23687.
KOiK01322.
OrthoDBiEOG091G023D.

Enzyme and pathway databases

BRENDAi3.4.21.26. 6170.

Miscellaneous databases

EvolutionaryTraceiP23687.
PROiP23687.

Gene expression databases

BgeeiENSSSCG00000004368.
GenevisibleiP23687. SS.

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...

Entry informationi

Entry nameiPPCE_PIG
AccessioniPrimary (citable) accession number: P23687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.