Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dipeptidase 3

Gene

Dpep3

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

Functioni

Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis.1 Publication

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+PROSITE-ProRule annotation

Enzyme regulationi

Inhibited by L-penicillamine.1 Publication

Kineticsi

  1. KM=2.5 mM for cystinyl-bis-glycine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi94Zinc 1; catalyticPROSITE-ProRule annotation1
    Metal bindingi96Zinc 1; catalyticPROSITE-ProRule annotation1
    Metal bindingi193Zinc 1; catalyticPROSITE-ProRule annotation1
    Metal bindingi193Zinc 2; catalyticPROSITE-ProRule annotation1
    Metal bindingi266Zinc 2; catalyticPROSITE-ProRule annotation1
    Metal bindingi287Zinc 2; catalyticPROSITE-ProRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    • male meiosis Source: UniProtKB
    • proteolysis Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Meiosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM19.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidase 3 (EC:3.4.13.19)
    Alternative name(s):
    Membrane-bound dipeptidase 3
    Short name:
    MBD-3
    Protein expressed in male leptotene and zygotene spermatocytes 136
    Short name:
    MLZ-136
    Gene namesi
    Name:Dpep3
    Synonyms:Mbd3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:1919104. Dpep3.

    Subcellular locationi

    GO - Cellular componenti

    • anchored component of membrane Source: UniProtKB-KW
    • membrane Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 35Sequence analysisAdd BLAST35
    ChainiPRO_000023161336 – 462Dipeptidase 3Add BLAST427
    PropeptideiPRO_0000231614463 – 493Removed in mature formSequence analysisAdd BLAST31

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi143 ↔ 222PROSITE-ProRule annotation
    Disulfide bondi294 ↔ 326PROSITE-ProRule annotation
    Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi431InterchainPROSITE-ProRule annotation
    Lipidationi462GPI-anchor amidated serineSequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ9DA79.
    PeptideAtlasiQ9DA79.
    PRIDEiQ9DA79.

    PTM databases

    iPTMnetiQ9DA79.
    PhosphoSitePlusiQ9DA79.

    Expressioni

    Tissue specificityi

    Expressed in testis but not ovary.2 Publications

    Developmental stagei

    expressed in ovary and testis at E15.5.1 Publication

    Gene expression databases

    BgeeiENSMUSG00000031898.
    CleanExiMM_DPEP3.
    MM_MBD3.
    GenevisibleiQ9DA79. MM.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.PROSITE-ProRule annotation

    Protein-protein interaction databases

    IntActiQ9DA79. 1 interactor.
    MINTiMINT-8174108.
    STRINGi10090.ENSMUSP00000034371.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DA79.
    SMRiQ9DA79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG4127. Eukaryota.
    COG2355. LUCA.
    GeneTreeiENSGT00390000017920.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    InParanoidiQ9DA79.
    KOiK01273.
    OMAiFYTNVSG.
    OrthoDBiEOG091G09CU.
    PhylomeDBiQ9DA79.
    TreeFamiTF324523.

    Family and domain databases

    CDDicd01301. rDP_like. 1 hit.
    InterProiIPR000180. Dipep_AS.
    IPR028533. Dpep3.
    IPR032466. Metal_Hydrolase.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF14. PTHR10443:SF14. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    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.

    Q9DA79-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQPAGLEGPR ALGLRPLGHR LSLLGVLLLV PSLWVTCTLT TPSPSSAPTT
    60 70 80 90 100
    PEASNATTAP GIPNDTATSG VTSDPRLREQ ALALMRDFPL VDGHNDLPLL
    110 120 130 140 150
    LRELFQNQLQ DVNLRNFTRG QTNLDRLRDG LVGAQFWSAY IPCQTQDRDA
    160 170 180 190 200
    VRLALEQIDL IRRMCSAYPE LELVTSADGL NNTQKLACLI GVEGGHSLDT
    210 220 230 240 250
    SLAVLRSFYE LGVRYLTLTF TCSTPWAESA TKFRHHFYTN ISGLTSFGEK
    260 270 280 290 300
    VVEEMNRLGM MIDLSHASDT LVKQTLEVSQ APVIFSHSAA RSVCDNLLNI
    310 320 330 340 350
    PDDILQLLKK NGGIVMVTLS MGVLQCSLFA NVSTVADHFD HIRTVIGSEF
    360 370 380 390 400
    IGIGGSYDGS GRFPQGLEDV STYPVLIEEL LSRGWDEREL QGVLRGNLLR
    410 420 430 440 450
    VFRQVEQVRE KSLGQSPVEV KFPERQQSNT CHSHLLPQPQ EDQHQDTHLK
    460 470 480 490
    VTKLPNILQR ASKAPPHPLP GLMATLTSLA LILWLCCSGH RAV
    Length:493
    Mass (Da):54,247
    Last modified:June 1, 2001 - v1
    Checksum:iB9A0D39BB7CEB619
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF488553 mRNA. Translation: AAP84987.1.
    AK006085 mRNA. Translation: BAB24402.1.
    BC051148 mRNA. Translation: AAH51148.1.
    CCDSiCCDS22624.1.
    RefSeqiNP_082236.1. NM_027960.2.
    UniGeneiMm.173395.

    Genome annotation databases

    EnsembliENSMUST00000034371; ENSMUSP00000034371; ENSMUSG00000031898.
    GeneIDi71854.
    KEGGimmu:71854.
    UCSCiuc009net.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF488553 mRNA. Translation: AAP84987.1.
    AK006085 mRNA. Translation: BAB24402.1.
    BC051148 mRNA. Translation: AAH51148.1.
    CCDSiCCDS22624.1.
    RefSeqiNP_082236.1. NM_027960.2.
    UniGeneiMm.173395.

    3D structure databases

    ProteinModelPortaliQ9DA79.
    SMRiQ9DA79.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9DA79. 1 interactor.
    MINTiMINT-8174108.
    STRINGi10090.ENSMUSP00000034371.

    Protein family/group databases

    MEROPSiM19.011.

    PTM databases

    iPTMnetiQ9DA79.
    PhosphoSitePlusiQ9DA79.

    Proteomic databases

    PaxDbiQ9DA79.
    PeptideAtlasiQ9DA79.
    PRIDEiQ9DA79.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000034371; ENSMUSP00000034371; ENSMUSG00000031898.
    GeneIDi71854.
    KEGGimmu:71854.
    UCSCiuc009net.1. mouse.

    Organism-specific databases

    CTDi64180.
    MGIiMGI:1919104. Dpep3.

    Phylogenomic databases

    eggNOGiKOG4127. Eukaryota.
    COG2355. LUCA.
    GeneTreeiENSGT00390000017920.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    InParanoidiQ9DA79.
    KOiK01273.
    OMAiFYTNVSG.
    OrthoDBiEOG091G09CU.
    PhylomeDBiQ9DA79.
    TreeFamiTF324523.

    Miscellaneous databases

    PROiQ9DA79.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000031898.
    CleanExiMM_DPEP3.
    MM_MBD3.
    GenevisibleiQ9DA79. MM.

    Family and domain databases

    CDDicd01301. rDP_like. 1 hit.
    InterProiIPR000180. Dipep_AS.
    IPR028533. Dpep3.
    IPR032466. Metal_Hydrolase.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF14. PTHR10443:SF14. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDPEP3_MOUSE
    AccessioniPrimary (citable) accession number: Q9DA79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: June 1, 2001
    Last modified: November 30, 2016
    This is version 111 of the entry and version 1 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.