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P31428

- DPEP1_MOUSE

UniProt

P31428 - DPEP1_MOUSE

Protein

Dipeptidase 1

Gene

Dpep1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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

    Zinc.

    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

    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).

    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. apical plasma membrane Source: UniProtKB-SubCell
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: Ensembl
    6. microvillus membrane Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB

    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

    MVIIWWFWSL LAICASDSFR DQAVAIMRTT PVIDGHNDLP WQLLNLFNNQ    50
    LLRPDADLNK LAQTHTNIPK LKAGFVGGQF WSAYMPCDTQ NKDAVKRILE 100
    QMDVIHRMCQ LYPETFMCVT NSSDILQAFR RGKVASLIGV EGGHLIDSSL 150
    GVLRTLYHLG MRYLTLTHNC NTPWADNWLV DRGDDEAESH GLSPFGKRLL 200
    NEMNRLGVMI DLSHVSVATM KDALQISRAP VIFSHSSAYS LCPHRRNVPD 250
    DVLQLVKNTS SLVMVNFFSN FVSCSDSATL PQVADHLDHI KKVAGAGAVG 300
    LGGDYDGVTM LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLADNLIRVF 350
    SEVELVSNNM QSPEEVPITL KELDGSCRTY YGYSQAHSIH LQTGALVASL 400
    ASLLFRLHLL 410
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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).

    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

    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: October 1, 2014
    This is version 125 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