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Q3SZM7

- DPEP1_BOVIN

UniProt

Q3SZM7 - DPEP1_BOVIN

Protein

Dipeptidase 1

Gene

DPEP1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      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 By similarity.By similarity

    Catalytic activityi

    Hydrolysis of dipeptides.PROSITE-ProRule annotation

    Cofactori

    Zinc.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by L-penicillamine.By similarity

    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_215847. 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):
    Microsomal dipeptidase
    Gene namesi
    Name:DPEP1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 18

    Subcellular locationi

    Apical cell membrane By similarity; Lipid-anchorGPI-anchor By similarity
    Note: Brush border membrane.By similarity

    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. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616By similarityAdd
    BLAST
    Chaini17 – 384368Dipeptidase 1PRO_0000231601Add
    BLAST
    Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000231602Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)By similarity
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
    Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 – 377InterchainPROSITE-ProRule annotation
    Lipidationi384 – 3841GPI-anchor amidated serineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PRIDEiQ3SZM7.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.PROSITE-ProRule annotation

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000016201.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SZM7.
    SMRiQ3SZM7. 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.
    InParanoidiQ3SZM7.
    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.

    Q3SZM7-1 [UniParc]FASTAAdd to Basket

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    MWTGWWLWPL VAVCTADQFR DNAVRLMQST PVIDGHNDLP WQLLKRFNNQ    50
    LQDPRANLTS LNGTHTNIPK LKAGFVGAQF WSAYTPCDTQ NKDSVKRTLE 100
    QIDVIQRMCQ LYPETFLCVT DSAGIQQAFQ EGKVASLVGV EGGHSIDSSL 150
    GVLRALYHLG MRYLTLTHSC NTPWADNWLV DTGEDEAQSQ GLSSFGQSVV 200
    KEMNRLGVII DLAHVSVATM EAALQLSKAP VIFSHSSAYS VCRHRRNVPD 250
    HVLQLVKQTG SLVMVNFYND YVSCKAEANL SQVADHLDYI KKVAGAGAVG 300
    FGGDYDGVSR LPSGLEDVSK YPDLVAELLR RQWTEEEVRG ALAENLLRVF 350
    KAVEQASDHK QAPGEEPIPL GQLEASCRTN YGYSGAPSLH LQPGTLLASL 400
    VTLLLSLCLL 410
    Length:410
    Mass (Da):45,127
    Last modified:October 11, 2005 - v1
    Checksum:i25174E46E558F95D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102783 mRNA. Translation: AAI02784.1.
    RefSeqiNP_001029644.1. NM_001034472.2.
    XP_005218637.1. XM_005218580.1.
    XP_005218638.1. XM_005218581.1.
    UniGeneiBt.48813.

    Genome annotation databases

    EnsembliENSBTAT00000016201; ENSBTAP00000016201; ENSBTAG00000033326.
    GeneIDi514685.
    KEGGibta:514685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102783 mRNA. Translation: AAI02784.1 .
    RefSeqi NP_001029644.1. NM_001034472.2.
    XP_005218637.1. XM_005218580.1.
    XP_005218638.1. XM_005218581.1.
    UniGenei Bt.48813.

    3D structure databases

    ProteinModelPortali Q3SZM7.
    SMRi Q3SZM7. Positions 17-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000016201.

    Protein family/group databases

    MEROPSi M19.001.

    Proteomic databases

    PRIDEi Q3SZM7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000016201 ; ENSBTAP00000016201 ; ENSBTAG00000033326 .
    GeneIDi 514685.
    KEGGi bta:514685.

    Organism-specific databases

    CTDi 1800.

    Phylogenomic databases

    eggNOGi COG2355.
    GeneTreei ENSGT00390000017920.
    HOGENOMi HOG000072016.
    HOVERGENi HBG002339.
    InParanoidi Q3SZM7.
    KOi K01273.
    OMAi GMRYMTL.
    OrthoDBi EOG7SJD4N.
    TreeFami TF324523.

    Enzyme and pathway databases

    Reactomei REACT_215847. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    NextBioi 20871464.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.

    Entry informationi

    Entry nameiDPEP1_BOVIN
    AccessioniPrimary (citable) accession number: Q3SZM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 75 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3