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Protein

Xaa-Pro dipeptidase

Gene

Pepd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen.

Catalytic activityi

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761Manganese 1By similarity
Metal bindingi287 – 2871Manganese 1By similarity
Metal bindingi287 – 2871Manganese 2By similarity
Metal bindingi370 – 3701Manganese 2By similarity
Metal bindingi412 – 4121Manganese 2By similarity
Metal bindingi452 – 4521Manganese 1By similarity
Metal bindingi452 – 4521Manganese 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

MEROPSiM24.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidase (EC:3.4.13.9)
Short name:
X-Pro dipeptidase
Alternative name(s):
Imidodipeptidase
Peptidase 4
Peptidase D
Proline dipeptidase
Short name:
Prolidase
Gene namesi
Name:Pepd
Synonyms:Pep4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:97542. Pepd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 493492Xaa-Pro dipeptidasePRO_0000185088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineSequence analysisBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ11136.
MaxQBiQ11136.
PaxDbiQ11136.
PRIDEiQ11136.

PTM databases

iPTMnetiQ11136.
PhosphoSiteiQ11136.

Expressioni

Gene expression databases

BgeeiQ11136.
CleanExiMM_PEPD.
ExpressionAtlasiQ11136. baseline and differential.
GenevisibleiQ11136. MM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiQ11136. 1 interaction.
MINTiMINT-4107049.
STRINGi10090.ENSMUSP00000075683.

Structurei

3D structure databases

ProteinModelPortaliQ11136.
SMRiQ11136. Positions 7-482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2737. Eukaryota.
COG0006. LUCA.
GeneTreeiENSGT00550000074992.
HOGENOMiHOG000008763.
HOVERGENiHBG053562.
InParanoidiQ11136.
KOiK14213.
OMAiGCYGVID.
OrthoDBiEOG7FNC76.
PhylomeDBiQ11136.
TreeFamiTF313396.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SMARTiSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q11136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTVRPSFS LGNETLKVPL ALFALNRQRL CERLRKNGAV QAASAVVLQG
60 70 80 90 100
GEEMQRYCTD TSIIFRQESF FHWAFGVVES GCYGVIDVDT GKSTLFVPRL
110 120 130 140 150
PDSYATWMGK IHSKEYFKEK YAVDDVQYTD EIASVLTSRN PSVLLTLRGV
160 170 180 190 200
NTDSGSVCRE ASFEGISKFN VNNTILHPEI VECRVFKTDM ELEVLRYTNR
210 220 230 240 250
ISSEAHREVM KAVKVGMKEY EMESLFQHYC YSRGGMRHTS YTCICCSGEN
260 270 280 290 300
AAVLHYGHAG APNDRTIKDG DICLFDMGGE YYCFASDITC SFPANGKFTE
310 320 330 340 350
DQKAIYEAVL RSCRTVMSTM KPGVWWPDMH RLADRIHLEE LARIGLLSGS
360 370 380 390 400
VDAMLQVHLG AVFMPHGLGH FLGLDVHDVG GYPEGVERID EPGLRSLRTA
410 420 430 440 450
RHLEPGMVLT VEPGIYFIDH LLDQALADPA QACFFNQEVL QRFRNFGGVR
460 470 480 490
IEEDVVVTDS GMELLTCVPR TVEEIEACMA GCDKASVPFS GQK
Length:493
Mass (Da):55,029
Last modified:January 23, 2007 - v3
Checksum:i5CC6BC66665BEACA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221L → I in AAA92975 (Ref. 1) Curated
Sequence conflicti296 – 2961G → R in AAA92975 (Ref. 1) Curated
Sequence conflicti349 – 3491G → C in BAB11685 (PubMed:8765744).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51014 mRNA. Translation: AAA92975.1.
D82983 mRNA. Translation: BAB11685.1.
AK010581 mRNA. Translation: BAB27043.1.
AK145843 mRNA. Translation: BAE26691.1.
AK168384 mRNA. Translation: BAE40312.1.
BC086644 mRNA. Translation: AAH86644.1.
CCDSiCCDS21143.1.
RefSeqiNP_032846.2. NM_008820.2.
UniGeneiMm.69751.

Genome annotation databases

EnsembliENSMUST00000075068; ENSMUSP00000075683; ENSMUSG00000063931.
GeneIDi18624.
KEGGimmu:18624.
UCSCiuc009gjj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51014 mRNA. Translation: AAA92975.1.
D82983 mRNA. Translation: BAB11685.1.
AK010581 mRNA. Translation: BAB27043.1.
AK145843 mRNA. Translation: BAE26691.1.
AK168384 mRNA. Translation: BAE40312.1.
BC086644 mRNA. Translation: AAH86644.1.
CCDSiCCDS21143.1.
RefSeqiNP_032846.2. NM_008820.2.
UniGeneiMm.69751.

3D structure databases

ProteinModelPortaliQ11136.
SMRiQ11136. Positions 7-482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ11136. 1 interaction.
MINTiMINT-4107049.
STRINGi10090.ENSMUSP00000075683.

Protein family/group databases

MEROPSiM24.007.

PTM databases

iPTMnetiQ11136.
PhosphoSiteiQ11136.

Proteomic databases

EPDiQ11136.
MaxQBiQ11136.
PaxDbiQ11136.
PRIDEiQ11136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075068; ENSMUSP00000075683; ENSMUSG00000063931.
GeneIDi18624.
KEGGimmu:18624.
UCSCiuc009gjj.2. mouse.

Organism-specific databases

CTDi5184.
MGIiMGI:97542. Pepd.

Phylogenomic databases

eggNOGiKOG2737. Eukaryota.
COG0006. LUCA.
GeneTreeiENSGT00550000074992.
HOGENOMiHOG000008763.
HOVERGENiHBG053562.
InParanoidiQ11136.
KOiK14213.
OMAiGCYGVID.
OrthoDBiEOG7FNC76.
PhylomeDBiQ11136.
TreeFamiTF313396.

Miscellaneous databases

ChiTaRSiPepd. mouse.
PROiQ11136.
SOURCEiSearch...

Gene expression databases

BgeeiQ11136.
CleanExiMM_PEPD.
ExpressionAtlasiQ11136. baseline and differential.
GenevisibleiQ11136. MM.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SMARTiSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Ledoux P., Savoie P., Scriver C., Hechtman P.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "Cloning of mouse prolidase cDNA: predominant expression of prolidase mRNA in kidney."
    Ishii T., Tsujino S., Matsunobu S., Endo F., Sato K., Sakuragawa N.
    Biochim. Biophys. Acta 1308:15-16(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "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.
    , 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: Amnion, Embryonic stem cell and Liver.
  4. "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/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPEPD_MOUSE
AccessioniPrimary (citable) accession number: Q11136
Secondary accession number(s): P97735, Q3TH86, Q9CWK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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