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P31428

- DPEP1_MOUSE

UniProt

P31428 - DPEP1_MOUSE

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Protein

Dipeptidase 1

Gene

Dpep1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_237136. Aflatoxin activation and detoxification.

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: 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. cell projection Source: UniProtKB-KW
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: Ensembl
  6. 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.
OMAiGMRYMTL.
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 3, 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 .
CCDSi CCDS22750.1.
PIRi S33757.
RefSeqi NP_031902.2. NM_007876.2.
UniGenei Mm.20388.

3D structure databases

ProteinModelPortali P31428.
SMRi P31428. Positions 17-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P31428. 3 interactions.
MINTi MINT-4101665.
STRINGi 10090.ENSMUSP00000019422.

Protein family/group databases

MEROPSi M19.001.

PTM databases

PhosphoSitei P31428.

Proteomic databases

PaxDbi P31428.
PRIDEi P31428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019422 ; ENSMUSP00000019422 ; ENSMUSG00000019278 .
GeneIDi 13479.
KEGGi mmu:13479.
UCSCi uc009nui.2. mouse.

Organism-specific databases

CTDi 1800.
MGIi MGI:94917. Dpep1.

Phylogenomic databases

eggNOGi COG2355.
GeneTreei ENSGT00390000017920.
HOGENOMi HOG000072016.
HOVERGENi HBG002339.
InParanoidi P31428.
KOi K01273.
OMAi GMRYMTL.
OrthoDBi EOG7SJD4N.
TreeFami TF324523.

Enzyme and pathway databases

Reactomei REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_237136. Aflatoxin activation and detoxification.

Miscellaneous databases

NextBioi 283967.
PROi P31428.
SOURCEi Search...

Gene expression databases

CleanExi MM_DPEP1.
MM_MBD1.
Genevestigatori P31428.

Family and domain databases

InterProi IPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view ]
PANTHERi PTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
Pfami PF01244. Peptidase_M19. 1 hit.
[Graphical view ]
PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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 (JUL-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(2003) [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: July 1, 1993
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 127 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