Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P22412

- DPEP1_PIG

UniProt

P22412 - DPEP1_PIG

Protein

Dipeptidase 1

Gene

DPEP1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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 insulin stimulus Source: UniProtKB
    5. cellular response to nitric oxide Source: UniProtKB
    6. GPI anchor release Source: UniProtKB
    7. homocysteine metabolic process Source: UniProtKB
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of cell migration Source: UniProtKB
    10. 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

    BioCyciMetaCyc:MONOMER-9981.

    Protein family/group databases

    MEROPSiM19.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidase 1 (EC:3.4.13.19)
    Alternative name(s):
    Microsomal dipeptidase
    Renal dipeptidase
    Gene namesi
    Name:DPEP1
    Synonyms:RDP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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. endoplasmic reticulum membrane Source: UniProtKB
    5. extracellular space Source: UniProtKB
    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 – 16161 PublicationAdd
    BLAST
    Chaini17 – 384368Dipeptidase 1PRO_0000018656Add
    BLAST
    Propeptidei385 – 40925Removed in mature formBy similarityPRO_0000018657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
    Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
    Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 – 377Interchain
    Lipidationi384 – 3841GPI-anchor amidated serine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.

    Structurei

    3D structure databases

    ProteinModelPortaliP22412.
    SMRiP22412. Positions 17-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG002339.
    KOiK01273.

    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.

    P22412-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWTSWWLWPL VAVCAADQFR DLAVRIMQDT PVIDGHNDLP WQLLNLFNNQ    50
    LQDPGANLSS LAHTHTNIPK LKAGFVGGQF WSAYVPCDTQ NRDAVKRTLE 100
    QIDVIQRMCQ AYPETFACVT SSTGIRQAFR EGKVASLVGV EGGHSIDSSL 150
    GVLRALYHLG MRYMTLTHSC NTPWADNWLV DTGDDKAQSQ GLSHFGQSVV 200
    KEMNRLGVMI DLAHVSVATM RAALKLSQAP VIFSHSSAYS LCPHRRNVPD 250
    DVLQLVKETG SLVMVNFYND YVSCSAKANL SQVADHLDHI KKVAGAAAVG 300
    FGGDYDGVSR VPSGLEDVSK YPDLVAELLR RQWTEAEVRG ALADNLLRVF 350
    EAVEQASNHA QVPGEEPIPL GQLEASCRTN YGYSAAPSLH LPPGSLLASL 400
    VPLLLLSLP 409
    Length:409
    Mass (Da):44,700
    Last modified:August 1, 1991 - v1
    Checksum:i926B7F0044FA055F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53730 mRNA. Translation: CAA37762.1.
    D13142 mRNA. Translation: BAA02433.1.
    PIRiJS0759.
    RefSeqiNP_999273.1. NM_214108.1.
    UniGeneiSsc.315.

    Genome annotation databases

    GeneIDi397196.
    KEGGissc:397196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53730 mRNA. Translation: CAA37762.1 .
    D13142 mRNA. Translation: BAA02433.1 .
    PIRi JS0759.
    RefSeqi NP_999273.1. NM_214108.1.
    UniGenei Ssc.315.

    3D structure databases

    ProteinModelPortali P22412.
    SMRi P22412. Positions 17-385.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P22412.
    ChEMBLi CHEMBL2626.

    Protein family/group databases

    MEROPSi M19.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397196.
    KEGGi ssc:397196.

    Organism-specific databases

    CTDi 1800.

    Phylogenomic databases

    HOVERGENi HBG002339.
    KOi K01273.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-9981.

    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. "cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme."
      Rached E., Hooper N.M., James P., Semenza G., Turner A.J., Mantei N.
      Biochem. J. 271:755-760(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-57.
      Tissue: Kidney cortex.
    2. "Purification and cDNA cloning for porcine renal dipeptidase."
      Satoh S., Koyama S., Ohtuka K., Keida Y., Niwa M., Kohsaka M.
      Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme."
      Hooper N.M., Keen J.N., Turner A.J.
      Biochem. J. 265:429-433(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-39.
    4. "Site-directed mutagenesis of conserved cysteine residues in porcine membrane dipeptidase. Cys-361 alone is involved in disulfide-linked dimerization."
      Keynan S., Habgood N.T., Hooper N.M., Turner A.J.
      Biochemistry 35:12511-12517(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERCHAIN DISULFIDE BOND.
    5. "Isolation and characterization of glycosylphosphatidylinositol-anchored peptides by hydrophilic interaction chromatography and MALDI tandem mass spectrometry."
      Omaetxebarria M.J., Hagglund P., Elortza F., Hooper N.M., Arizmendi J.M., Jensen O.N.
      Anal. Chem. 78:3335-3341(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiDPEP1_PIG
    AccessioniPrimary (citable) accession number: P22412
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 113 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