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P23687

- PPCE_PIG

UniProt

P23687 - PPCE_PIG

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Protein

Prolyl endopeptidase

Gene

PREP

Organism
Sus scrofa (Pig)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei554 – 5541Charge relay system1 PublicationPROSITE-ProRule annotation
Active sitei641 – 6411Charge relay system
Active sitei680 – 6801Charge relay system1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type exopeptidase activity Source: InterPro
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):
Post-proline cleaving enzyme
Gene namesi
Name:PREP
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 710710Prolyl endopeptidasePRO_0000122403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei157 – 1571N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23687.
PRIDEiP23687.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004715.

Structurei

Secondary structure

1
710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194Combined sources
Beta strandi22 – 254Combined sources
Helixi29 – 324Combined sources
Beta strandi34 – 363Combined sources
Helixi37 – 5620Combined sources
Helixi59 – 7113Combined sources
Beta strandi80 – 823Combined sources
Beta strandi85 – 917Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi111 – 1144Combined sources
Helixi116 – 1194Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi136 – 14510Combined sources
Beta strandi151 – 1577Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 17110Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi182 – 1898Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi209 – 2146Combined sources
Helixi219 – 2213Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi246 – 2527Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi260 – 2656Combined sources
Helixi266 – 2683Combined sources
Beta strandi269 – 2735Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi290 – 2967Combined sources
Beta strandi299 – 3046Combined sources
Beta strandi312 – 3176Combined sources
Helixi323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi337 – 3448Combined sources
Turni345 – 3473Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi358 – 3658Combined sources
Turni366 – 3683Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi379 – 3868Combined sources
Beta strandi392 – 3998Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4116Combined sources
Beta strandi414 – 4163Combined sources
Beta strandi420 – 4245Combined sources
Beta strandi428 – 4303Combined sources
Helixi432 – 4343Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi445 – 4473Combined sources
Beta strandi449 – 4579Combined sources
Beta strandi468 – 4714Combined sources
Helixi486 – 49510Combined sources
Beta strandi498 – 5025Combined sources
Helixi511 – 5166Combined sources
Helixi520 – 5234Combined sources
Helixi524 – 53916Combined sources
Helixi545 – 5473Combined sources
Beta strandi548 – 5536Combined sources
Helixi555 – 56612Combined sources
Helixi568 – 5703Combined sources
Beta strandi572 – 5787Combined sources
Turni583 – 5853Combined sources
Helixi586 – 5883Combined sources
Helixi592 – 5954Combined sources
Helixi596 – 5994Combined sources
Helixi605 – 61410Combined sources
Helixi616 – 6183Combined sources
Beta strandi624 – 6274Combined sources
Beta strandi632 – 6387Combined sources
Beta strandi642 – 6443Combined sources
Helixi647 – 65913Combined sources
Turni660 – 6623Combined sources
Beta strandi663 – 6653Combined sources
Beta strandi670 – 6778Combined sources
Helixi686 – 70419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-710.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23687.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.Curated

Phylogenomic databases

eggNOGiCOG1505.
HOGENOMiHOG000238967.
HOVERGENiHBG007251.
InParanoidiP23687.
KOiK01322.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291A → H.

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 .
PIRi A37942.
RefSeqi NP_001004050.1. NM_001004050.1.
UniGenei Ssc.10442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E5T X-ray 1.70 A 1-710 [» ]
1E8M X-ray 1.50 A 1-710 [» ]
1E8N X-ray 1.50 A 1-710 [» ]
1H2W X-ray 1.39 A 1-710 [» ]
1H2X X-ray 1.49 A 1-710 [» ]
1H2Y X-ray 1.78 A 1-710 [» ]
1H2Z X-ray 1.65 A 1-710 [» ]
1O6F X-ray 1.60 A 1-710 [» ]
1O6G X-ray 1.40 A 1-710 [» ]
1QFM X-ray 1.40 A 1-710 [» ]
1QFS X-ray 2.00 A 1-710 [» ]
1UOO X-ray 2.35 A 1-710 [» ]
1UOP X-ray 1.85 A 1-710 [» ]
1UOQ X-ray 2.10 A 1-710 [» ]
1VZ2 X-ray 2.20 A 1-710 [» ]
1VZ3 X-ray 1.60 A 1-710 [» ]
2XDW X-ray 1.35 A 1-710 [» ]
3EQ7 X-ray 2.89 A 1-710 [» ]
3EQ8 X-ray 2.73 A 1-710 [» ]
3EQ9 X-ray 2.47 A 1-710 [» ]
4AMY X-ray 2.00 A 1-710 [» ]
4AMZ X-ray 2.00 A 1-710 [» ]
4AN0 X-ray 2.20 A 1-710 [» ]
4AN1 X-ray 1.90 A 1-710 [» ]
4AX4 X-ray 1.60 A 1-710 [» ]
4BCB X-ray 1.70 A 1-710 [» ]
4BCC X-ray 1.65 A 1-710 [» ]
4BCD X-ray 1.50 A 1-710 [» ]
ProteinModelPortali P23687.
SMRi P23687. Positions 1-710.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000004715.

Chemistry

BindingDBi P23687.
ChEMBLi CHEMBL2461.

Protein family/group databases

MEROPSi S09.001.

Proteomic databases

PaxDbi P23687.
PRIDEi P23687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 445540.
KEGGi ssc:445540.

Organism-specific databases

CTDi 5550.

Phylogenomic databases

eggNOGi COG1505.
HOGENOMi HOG000238967.
HOVERGENi HBG007251.
InParanoidi P23687.
KOi K01322.

Miscellaneous databases

EvolutionaryTracei P23687.

Family and domain databases

Gene3Di 2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view ]
PANTHERi PTHR11757. PTHR11757. 1 hit.
Pfami PF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view ]
PRINTSi PR00862. PROLIGOPTASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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 26, 2014
This is version 113 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

External Data

Dasty 3