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P43477

- DPEP1_SHEEP

UniProt

P43477 - DPEP1_SHEEP

Protein

Dipeptidase 1

Gene

DPEP1

Organism
Ovis aries (Sheep)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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. In lung tissue, it may terminate or significantly reduce the leukotriene induced signal for bronchospasm.1 Publication

    Catalytic activityi

    Hydrolysis of dipeptides.PROSITE-ProRule annotation

    Cofactori

    Zinc.

    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

    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
    OrganismiOvis aries (Sheep)
    Taxonomic identifieri9940 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
    ProteomesiUP000002356: Unplaced

    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. microvillus membrane Source: UniProtKB-SubCell
    6. 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_0000018662Add
    BLAST
    Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018663Add
    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

    Expressioni

    Tissue specificityi

    Expressed in lung, kidney and intestinal tissues.1 Publication

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.

    Structurei

    3D structure databases

    ProteinModelPortaliP43477.
    SMRiP43477. Positions 17-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG002339.

    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.

    P43477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWTGWWLWPL VAVCTADQFR DNAVRLMQST PVIDGHNDLP WALLKKFNNQ    50
    LQDPRANLTS LNSTHTNIPK LKAGFVGAQF WSAYTPCDTQ NKDSVKRTVE 100
    QIDVIQRMCQ LYPETFLCVT DSAGIQQAFQ EGKVASLVGV EGGHSIDSSL 150
    GVLRALYHLG MRYLTLTHSC NTPWADNWLV DTGEDKAQSQ GLSSFGQSVV 200
    KEMNRLGIII DLAHVSVATM EAALQLSKAP VIFSHSSAYS LCHHRRNVPD 250
    HVLQLVKQTG SLVMVNFYND YVSCKAEANL SQVADHLDYI KKVAGAGAVG 300
    FGGDYDGVSR LPSGLEDVSK YPDLVAELLR RQWTEEEVRG ALAENLLRVF 350
    KAVEQASDHK QAPGEEPIPL GQLEASCRTK YGYSGTPSLH LQPGSLLASL 400
    VTLLLSLCLL 410
    Length:410
    Mass (Da):45,096
    Last modified:November 1, 1995 - v1
    Checksum:iAA818C8B8BB91F31
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421A → Q AA sequence (PubMed:8054366)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27113 mRNA. Translation: AAA21725.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27113 mRNA. Translation: AAA21725.1 .

    3D structure databases

    ProteinModelPortali P43477.
    SMRi P43477. Positions 17-384.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M19.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG002339.

    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. "Molecular cloning of sheep lung dipeptidase: a glycosyl phosphatidylinositol-anchored ectoenzyme that converts leukotriene D4 to leukotriene E4."
      An S., Schmidt F.J., Campbell B.J.
      Biochim. Biophys. Acta 1226:337-340(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-56, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Lung.

    Entry informationi

    Entry nameiDPEP1_SHEEP
    AccessioniPrimary (citable) accession number: P43477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 95 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, Direct protein sequencing, 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