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Q9ESW8 (PGPI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Pyroglutamyl-peptidase 1

EC=3.4.19.3
Alternative name(s):
5-oxoprolyl-peptidase
Pyroglutamyl aminopeptidase I
Short name=PAP-I
Pyroglutamyl-peptidase I
Short name=PGP-I
Pyrrolidone-carboxylate peptidase
Gene names
Name:Pgpep1
Synonyms:Pgpi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Removes 5-oxoproline from various penultimate amino acid residues except L-proline By similarity.

Catalytic activity

Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase C15 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from sequence alignment Ref.1. Source: MGI

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activity

Inferred from sequence alignment Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Pyroglutamyl-peptidase 1
PRO_0000184762

Sites

Active site851 By similarity
Active site1491 By similarity
Active site1681 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ESW8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F8CD222CD61AE853

FASTA20922,934
        10         20         30         40         50         60 
MEQPRKAVVV TGFGPFGEHT VNASWIAVQE LEKLGLGDSV DLHVYEIPVE YQTVQRLIPA 

        70         80         90        100        110        120 
LWEKHSPQLV VHVGVSGMAT TVTLEKCGHN KGYKGLDNCR FCPGSQCCVE DGPESIDSII 

       130        140        150        160        170        180 
DMDAVCKRVT TLGLDVSVTI SQDAGRYLCD FTYYTSLYQG RGRSAFVHVP PLGKPYNADQ 

       190        200 
LGRALRAIIE EMLGVLEQAE GDISCCRQL 

« Hide

References

« Hide 'large scale' references
[1]"Pyroglutamyl-peptidase I: cloning, sequencing, and characterisation of the recombinant human enzyme."
Dando P.M., Fortunato M., Strand G.B., Smith T.S., Barrett A.J.
Protein Expr. Purif. 28:111-119(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Head and Spinal cord.
[3]"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].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278829 mRNA. Translation: CAC03615.1.
AK003373 mRNA. Translation: BAB22746.1.
AK012658 mRNA. Translation: BAB28388.1.
AK047835 mRNA. Translation: BAC33170.1.
AK049632 mRNA. Translation: BAC33848.1.
BC051938 mRNA. Translation: AAH51938.1.
CCDSCCDS22377.1.
RefSeqNP_075706.1. NM_023217.4.
UniGeneMm.154906.
Mm.372568.
Mm.487385.

3D structure databases

ProteinModelPortalQ9ESW8.
SMRQ9ESW8. Positions 3-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000070778.

Protein family/group databases

MEROPSC15.010.

PTM databases

PhosphoSiteQ9ESW8.

Proteomic databases

MaxQBQ9ESW8.
PaxDbQ9ESW8.
PRIDEQ9ESW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070173; ENSMUSP00000070778; ENSMUSG00000056204.
GeneID66522.
KEGGmmu:66522.
UCSCuc009mbc.2. mouse.

Organism-specific databases

CTD54858.
MGIMGI:1913772. Pgpep1.

Phylogenomic databases

eggNOGCOG2039.
GeneTreeENSGT00390000015368.
HOGENOMHOG000007775.
HOVERGENHBG019147.
InParanoidQ9ESW8.
KOK01304.
OMATVNASWV.
OrthoDBEOG7VDXQV.
PhylomeDBQ9ESW8.
TreeFamTF313278.

Enzyme and pathway databases

BRENDA3.4.19.3. 3474.
SABIO-RKQ9ESW8.

Gene expression databases

BgeeQ9ESW8.
CleanExMM_PGPEP1.
GenevestigatorQ9ESW8.

Family and domain databases

Gene3D3.40.630.20. 1 hit.
InterProIPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
[Graphical view]
PANTHERPTHR23402. PTHR23402. 1 hit.
PfamPF01470. Peptidase_C15. 1 hit.
[Graphical view]
PIRSFPIRSF015592. Prld-crbxl_pptds. 1 hit.
PRINTSPR00706. PYROGLUPTASE.
SUPFAMSSF53182. SSF53182. 1 hit.
PROSITEPS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio321928.
PROQ9ESW8.
SOURCESearch...

Entry information

Entry namePGPI_MOUSE
AccessionPrimary (citable) accession number: Q9ESW8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot