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P31429

- DPEP1_RABIT

UniProt

P31429 - DPEP1_RABIT

Protein

Dipeptidase 1

Gene

DPEP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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.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):
    43 kDa renal band 3-related protein
    Microsomal dipeptidase
    Gene namesi
    Name:DPEP1
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: 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 – 16161 PublicationAdd
    BLAST
    Chaini17 – 384368Dipeptidase 1PRO_0000018658Add
    BLAST
    Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018659Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Miscellaneous databases

    PMAP-CutDBP31429.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000008950.

    Structurei

    3D structure databases

    ProteinModelPortaliP31429.
    SMRiP31429. Positions 17-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2355.
    HOGENOMiHOG000072016.
    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.

    P31429-1 [UniParc]FASTAAdd to Basket

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    MWTSWWLWPL VAVCTADSFL DQAVQILRVT PVIDGHNDLP WQLLNKFNNR    50
    LQDSRANLTV LADTHTNIPK LRAGFVGGQF WSAYTPCDTQ NKDTVRRTLE 100
    QMDVVHRMCQ LYPETFLCVT DSAGIQQAFR EGKVASLIGV EGGHSIDSSL 150
    GVLRALYRLG MRYLTLTHNC NTPWADNWLV DRGDDEAQSG GLSVFGQRVV 200
    REMNRLGVMI DLAHVSVATM KAALQLSTAP VIFSHSSAFT VCAHKRNVPD 250
    DVLQLVKETG SLVMVNFYND YVSCASEATL SQVADHLDYI KNVAGAAAVR 300
    FGGDFDGVTR LPVGLEDVSK YPDLVAELLR RGWTEAEVRG ALAENLLRVF 350
    REVEQVSNQA QVPEEEPISL EQLGGSCRTQ YGYSEAPSLH RRPGALLASL 400
    SLLLLSLGLL 410
    Length:410
    Mass (Da):45,305
    Last modified:July 1, 1993 - v1
    Checksum:i2033F7BFBBF2CC72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61503 mRNA. Translation: CAA43720.1.
    PIRiS18442.
    RefSeqiNP_001095167.1. NM_001101697.1.
    UniGeneiOcu.3249.

    Genome annotation databases

    GeneIDi100009273.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61503 mRNA. Translation: CAA43720.1 .
    PIRi S18442.
    RefSeqi NP_001095167.1. NM_001101697.1.
    UniGenei Ocu.3249.

    3D structure databases

    ProteinModelPortali P31429.
    SMRi P31429. Positions 17-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000008950.

    Protein family/group databases

    MEROPSi M19.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009273.

    Organism-specific databases

    CTDi 1800.

    Phylogenomic databases

    eggNOGi COG2355.
    HOGENOMi HOG000072016.
    HOVERGENi HBG002339.

    Miscellaneous databases

    PMAP-CutDB P31429.

    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. "Cloning of cDNAs encoding a rabbit renal brush border membrane protein immunologically related to band 3. Sequence similarity with microsomal dipeptidase."
      Igarashi P., Karniski L.P.
      Biochem. J. 280:71-78(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-40.
      Tissue: Kidney.

    Entry informationi

    Entry nameiDPEP1_RABIT
    AccessioniPrimary (citable) accession number: P31429
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 110 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