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Protein

Dipeptidase 1

Gene

Dpep1

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

Functioni

Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Enzyme regulationi

Inhibited by L-penicillamine.1 Publication

Kineticsi

  1. KM=10 µM for leukotriene D41 Publication
  2. KM=0.45 mM for cystinyl-bis-glycine1 Publication
  3. KM=111 µM for beta-lactam1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi38 – 381Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi141 – 1411Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi141 – 1411Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei168 – 1681SubstratePROSITE-ProRule annotation
Metal bindingi214 – 2141Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi235 – 2351Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei246 – 2461SubstratePROSITE-ProRule annotation
Binding sitei304 – 3041SubstratePROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  2. dipeptidyl-peptidase activity Source: InterPro
  3. GPI anchor binding Source: UniProtKB
  4. metallodipeptidase activity Source: UniProtKB
  5. modified amino acid binding Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. antibiotic metabolic process Source: UniProtKB
  2. cellular response to calcium ion Source: UniProtKB
  3. cellular response to drug Source: UniProtKB
  4. cellular response to nitric oxide Source: UniProtKB
  5. homocysteine metabolic process Source: UniProtKB
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cell migration Source: UniProtKB
  8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_288150. Aflatoxin activation and detoxification.
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Membrane-bound dipeptidase 1
Short name:
MBD-1
Microsomal dipeptidase
Renal dipeptidase
Gene namesi
Name:Dpep1
Synonyms:Mbd1, Rdp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:94917. Dpep1.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. apical part of cell Source: UniProtKB
  3. apical plasma membrane Source: UniProtKB-SubCell
  4. cell junction Source: MGI
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: MGI
  7. microvillus membrane Source: UniProtKB-SubCell
  8. nucleus Source: MGI
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018654Add
BLAST
Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)By similarity
Disulfide bondi377 – 377InterchainPROSITE-ProRule annotation
Lipidationi384 – 3841GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP31428.
PRIDEiP31428.

PTM databases

PhosphoSiteiP31428.

Expressioni

Gene expression databases

CleanExiMM_DPEP1.
MM_MBD1.
GenevestigatoriP31428.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

IntActiP31428. 3 interactions.
MINTiMINT-4101665.
STRINGi10090.ENSMUSP00000019422.

Structurei

3D structure databases

ProteinModelPortaliP31428.
SMRiP31428. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP31428.
KOiK01273.
OMAiETFLCVT.
OrthoDBiEOG7SJD4N.
TreeFamiTF324523.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P31428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIIWWFWSL LAICASDSFR DQAVAIMRTT PVIDGHNDLP WQLLNLFNNQ
60 70 80 90 100
LLRPDADLNK LAQTHTNIPK LKAGFVGGQF WSAYMPCDTQ NKDAVKRILE
110 120 130 140 150
QMDVIHRMCQ LYPETFMCVT NSSDILQAFR RGKVASLIGV EGGHLIDSSL
160 170 180 190 200
GVLRTLYHLG MRYLTLTHNC NTPWADNWLV DRGDDEAESH GLSPFGKRLL
210 220 230 240 250
NEMNRLGVMI DLSHVSVATM KDALQISRAP VIFSHSSAYS LCPHRRNVPD
260 270 280 290 300
DVLQLVKNTS SLVMVNFFSN FVSCSDSATL PQVADHLDHI KKVAGAGAVG
310 320 330 340 350
LGGDYDGVTM LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLADNLIRVF
360 370 380 390 400
SEVELVSNNM QSPEEVPITL KELDGSCRTY YGYSQAHSIH LQTGALVASL
410
ASLLFRLHLL
Length:410
Mass (Da):45,722
Last modified:October 2, 2012 - v2
Checksum:i46A454B51CA57BB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041N → T in BAA02432 (PubMed:8507661).Curated
Sequence conflicti358 – 3581N → S in BAA02432 (PubMed:8507661).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13139 mRNA. Translation: BAA02432.1.
AC163617 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11712.1.
CCDSiCCDS22750.1.
PIRiS33757.
RefSeqiNP_031902.2. NM_007876.2.
UniGeneiMm.20388.

Genome annotation databases

EnsembliENSMUST00000019422; ENSMUSP00000019422; ENSMUSG00000019278.
GeneIDi13479.
KEGGimmu:13479.
UCSCiuc009nui.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13139 mRNA. Translation: BAA02432.1.
AC163617 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11712.1.
CCDSiCCDS22750.1.
PIRiS33757.
RefSeqiNP_031902.2. NM_007876.2.
UniGeneiMm.20388.

3D structure databases

ProteinModelPortaliP31428.
SMRiP31428. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP31428. 3 interactions.
MINTiMINT-4101665.
STRINGi10090.ENSMUSP00000019422.

Protein family/group databases

MEROPSiM19.001.

PTM databases

PhosphoSiteiP31428.

Proteomic databases

PaxDbiP31428.
PRIDEiP31428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019422; ENSMUSP00000019422; ENSMUSG00000019278.
GeneIDi13479.
KEGGimmu:13479.
UCSCiuc009nui.2. mouse.

Organism-specific databases

CTDi1800.
MGIiMGI:94917. Dpep1.

Phylogenomic databases

eggNOGiCOG2355.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP31428.
KOiK01273.
OMAiETFLCVT.
OrthoDBiEOG7SJD4N.
TreeFamiTF324523.

Enzyme and pathway databases

ReactomeiREACT_288150. Aflatoxin activation and detoxification.
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

NextBioi283967.
PROiP31428.
SOURCEiSearch...

Gene expression databases

CleanExiMM_DPEP1.
MM_MBD1.
GenevestigatoriP31428.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and molecular cloning of mouse renal dipeptidase."
    Satoh S., Keida Y., Konta Y., Maeda M., Matsumoto Y., Niwa M., Kohsaka M.
    Biochim. Biophys. Acta 1163:234-242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Identification of two additional members of the membrane-bound dipeptidase family."
    Habib G.M., Shi Z.-Z., Cuevas A.A., Lieberman M.W.
    FASEB J. 17:1313-1315(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Entry informationi

Entry nameiDPEP1_MOUSE
AccessioniPrimary (citable) accession number: P31428
Secondary accession number(s): G5E824
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1993
Last sequence update: October 2, 2012
Last modified: March 31, 2015
This is version 131 of the entry and version 2 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

External Data

Dasty 3

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 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.