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UniProtKB/Swiss-Prot entry P23687

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPCE_PIG
Primary accession number P23687
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Prolyl endopeptidase
Synonyms PE
EC 3.4.21.26
Post-proline cleaving enzyme
Gene name
Name: PREP
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE SER-554.
TISSUE=Brain;
DOI=10.1021/bi00222a025; PubMed=1900195 [NCBI, ExPASy, EBI, Israel, Japan]
Rennex D., Hemmings B.A., Hofsteenge J., Stone S.R.;
"cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.";
Biochemistry 30:2195-2203(1991).
[2]
 ACTIVE SITE HIS-680.
PubMed=2064618 [NCBI, ExPASy, EBI, Israel, Japan]
Stone S.R., Rennex D., Wikstrom P., Shaw E., Hofsteenge J.;
"Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.";
Biochem. J. 276:837-840(1991).
[3]
 X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
DOI=10.1016/S0092-8674(00)81416-6; PubMed=9695945 [NCBI, ExPASy, EBI, Israel, Japan]
Fueloep V., Bocskei Z., Polgar L.;
"Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.";
Cell 94:161-170(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64227; AAA31110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37942; A37942.
RefSeq NP_001004050.1; -.
UniGene Ssc.10442
3D structure databases
PDB
1E5T; X-ray; 1.70 A; A=1-710.[ExPASy / RCSB / EBI]
1E8M; X-ray; 1.50 A; A=1-710.[ExPASy / RCSB / EBI]
1E8N; X-ray; 1.50 A; A=1-710.[ExPASy / RCSB / EBI]
1H2W; X-ray; 1.39 A; A=1-710.[ExPASy / RCSB / EBI]
1H2X; X-ray; 1.49 A; A=1-710.[ExPASy / RCSB / EBI]
1H2Y; X-ray; 1.78 A; A=1-710.[ExPASy / RCSB / EBI]
1H2Z; X-ray; 1.65 A; A=1-710.[ExPASy / RCSB / EBI]
1O6F; X-ray; 1.60 A; A=1-710.[ExPASy / RCSB / EBI]
1O6G; X-ray; 1.40 A; A=1-710.[ExPASy / RCSB / EBI]
1QFM; X-ray; 1.40 A; A=1-710.[ExPASy / RCSB / EBI]
1QFS; X-ray; 2.00 A; A=1-710.[ExPASy / RCSB / EBI]
1UOO; X-ray; 2.35 A; A=1-710.[ExPASy / RCSB / EBI]
1UOP; X-ray; 1.85 A; A=1-710.[ExPASy / RCSB / EBI]
1UOQ; X-ray; 2.10 A; A=1-710.[ExPASy / RCSB / EBI]
1VZ2; X-ray; 2.20 A; A=1-710.[ExPASy / RCSB / EBI]
1VZ3; X-ray; 1.60 A; A=1-710.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E5T; -.
1E8M; -.
1E8N; -.
1H2W; -.
1H2X; -.
1H2Y; -.
1H2Z; -.
1O6F; -.
1O6G; -.
1QFM; -.
1QFS; -.
1UOO; -.
1UOP; -.
1UOQ; -.
1VZ2; -.
1VZ3; -.
ModBase P23687.
Protein family/group databases
MEROPS S09.001; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002470; Peptidase_S9A.
IPR004106; Peptidase_S9A_N.
Graphical view of domain structure.
PANTHER PTHR11757; Peptidase_S9A; 1.
Pfam PF00326; Peptidase_S9; 1.
PF02897; Peptidase_S9_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00862; PROLIGOPTASE.
PROSITE PS00708; PRO_ENDOPEP_SER; 1.
BLOCKS P23687.
ProtoNet P23687.
Genome annotation databases
GeneID 445540; -.
KEGG ssc:445540; -.
Phylogenomic databases
HOVERGEN P23687; -.
Other
LinkHub P23687; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Serine protease.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   710  710     Prolyl endopeptidase. PRO_0000122403
ACT_SITE   554   554        Charge relay system. 
ACT_SITE   641   641        Charge relay system. 
ACT_SITE   680   680        Charge relay system. 
VARIANT   29    29  1     A -> H. 
STRAND   16    19  4      
STRAND   22    25  4      
HELIX   29    32  4      
HELIX   37    55  19      
HELIX   59    70  12      
STRAND   80    82  3      
STRAND   85    91  7      
STRAND   99   105  7      
STRAND   111   114  4      
HELIX   116   119  4      
STRAND   125   132  8      
STRAND   136   145  10      
STRAND   151   157  7      
TURN   158   161  4      
STRAND   162   171  10      
STRAND   176   178  3      
STRAND   182   189  8      
STRAND   198   200  3      
STRAND   209   214  6      
HELIX   219   221  3      
STRAND   223   226  4      
STRAND   235   240  6      
STRAND   246   252  7      
STRAND   254   257  4      
STRAND   260   265  6      
HELIX   266   268  3      
STRAND   272   276  5      
STRAND   280   283  4      
STRAND   285   288  4      
STRAND   290   296  7      
STRAND   299   304  6      
STRAND   312   317  6      
HELIX   323   325  3      
STRAND   327   330  4      
STRAND   337   344  8      
TURN   345   347  3      
STRAND   348   355  8      
STRAND   358   365  8      
TURN   366   368  3      
STRAND   371   375  5      
STRAND   379   386  8      
STRAND   392   399  8      
STRAND   401   403  3      
STRAND   406   411  6      
STRAND   414   416  3      
STRAND   420   424  5      
HELIX   432   434  3      
STRAND   435   443  9      
STRAND   449   457  9      
STRAND   468   471  4      
HELIX   486   495  10      
STRAND   498   502  5      
HELIX   511   516  6      
HELIX   520   523  4      
HELIX   524   539  16      
HELIX   545   547  3      
STRAND   548   553  6      
HELIX   555   566  12      
HELIX   568   570  3      
STRAND   572   578  7      
TURN   583   585  3      
HELIX   586   588  3      
HELIX   592   595  4      
HELIX   596   599  4      
HELIX   605   614  10      
HELIX   616   618  3      
STRAND   632   638  7      
HELIX   647   659  13      
TURN   660   662  3      
STRAND   670   677  8      
HELIX   686   704  19      
Sequence information
Length: 710 AA [This is the length of the unprocessed precursor] Molecular weight: 80770 Da [This is the MW of the unprocessed precursor] CRC64: 70286A86238D72C0 [This is a checksum on the sequence] 
        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
P23687 in FASTA format

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