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Q8C255

- DPEP2_MOUSE

UniProt

Q8C255 - DPEP2_MOUSE

Protein

Dipeptidase 2

Gene

Dpep2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).

    Catalytic activityi

    Hydrolysis of dipeptides.PROSITE-ProRule annotation

    Cofactori

    Zinc.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by L-penicillamine.1 Publication

    Kineticsi

    1. KM=5 µM for LTD41 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi93 – 931Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi190 – 1901Zinc 1; catalyticPROSITE-ProRule annotation
    Metal bindingi190 – 1901Zinc 2; catalyticPROSITE-ProRule annotation
    Binding sitei217 – 2171SubstratePROSITE-ProRule annotation
    Metal bindingi263 – 2631Zinc 2; catalyticPROSITE-ProRule annotation
    Metal bindingi284 – 2841Zinc 2; catalyticPROSITE-ProRule annotation
    Binding sitei295 – 2951SubstratePROSITE-ProRule annotation
    Binding sitei353 – 3531SubstratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. dipeptidase activity Source: UniProtKB-KW
    2. dipeptidyl-peptidase activity Source: InterPro
    3. exopeptidase activity Source: MGI
    4. metal ion binding Source: UniProtKB-KW
    5. metalloexopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Protein family/group databases

    MEROPSiM19.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidase 2 (EC:3.4.13.19)
    Alternative name(s):
    Membrane-bound dipeptidase 2
    Short name:
    MBD-2
    Gene namesi
    Name:Dpep2
    Synonyms:Mbd2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:2442042. Dpep2.

    Subcellular locationi

    Membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 459428Dipeptidase 2PRO_0000231605Add
    BLAST
    Propeptidei460 – 47819Removed in mature formSequence AnalysisPRO_0000231606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...)By similarity
    Disulfide bondi140 ↔ 219PROSITE-ProRule annotation
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi291 ↔ 323PROSITE-ProRule annotation
    Disulfide bondi428 – 428InterchainPROSITE-ProRule annotation
    Lipidationi459 – 4591GPI-anchor amidated serineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiQ8C255.
    PRIDEiQ8C255.

    Expressioni

    Tissue specificityi

    Expressed in heart, lung, testis, spleen and skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ8C255.
    CleanExiMM_DPEP2.
    MM_MBD2.
    GenevestigatoriQ8C255.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.PROSITE-ProRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C255.
    SMRiQ8C255. Positions 74-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2355.
    GeneTreeiENSGT00390000017920.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    OMAiIEATHRQ.
    OrthoDBiEOG7SJD4N.
    PhylomeDBiQ8C255.
    TreeFamiTF324523.

    Family and domain databases

    InterProiIPR000180. Dipep_AS.
    IPR028531. Dpep2.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF9. PTHR10443:SF9. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8C255-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLTGLKGHW VLGHGLSVFL LVLLLLGPSQ PLIWTQTKPG FSGASTTSSI    50
    PRALTKPDIS SIPTTPGNPN FPDLRDRARA LMQEFPLIDG HNDMPLVLRQ 100
    FYQNGLQDAN LRNFTHGQTS LDRLKDGLVG AQFWSAYVPC QTQDRDALRL 150
    TLEQIDLIRR ICASYSELEL VTSVKALNST QKLACLIGVE GGHSLDNSLA 200
    VLRSFYLLGV RYLTLTHTCN TPWAETSSKG VHAFYSSVTG LTSFGEKVVA 250
    EMNRLGMMVD LSHVSDAAAR RALEVSQAPV IFSHSAARAV CPNARNLPDD 300
    LLQLLKKNGG IVMVTFSVGV LPCNPLANVS TVADHFDHIR SVIGSEFIGI 350
    GGDYDGTKQF PQGLEDVSTY PVLIEELLRR GWNEQELQGI LRGNLLRVFR 400
    QVEQVRDKSK WQSPLEDMIP EEQLDSACHS ALRPQKQHPE KNQPETPEYH 450
    ILKFSHSKSS PHIVPSLAIV ATLLGLIV 478
    Length:478
    Mass (Da):52,664
    Last modified:March 1, 2003 - v1
    Checksum:i0790B97009F5D41F
    GO
    Isoform 2 (identifier: Q8C255-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAWHGETYCL...VPACSALSKM
         176-179: ALNS → VKWIYSG
         334-340: DHFDHIR → EKGQQKHQFTPPRDTHFV

    Show »
    Length:578
    Mass (Da):63,675
    Checksum:i253DC762000875A4
    GO
    Isoform 3 (identifier: Q8C255-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-93: Missing.

    Show »
    Length:385
    Mass (Da):42,667
    Checksum:iD28E45A1A5169543
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781A → T in BAE42354. (PubMed:16141072)Curated
    Sequence conflicti89 – 891D → G in BAE42559. (PubMed:16141072)Curated
    Sequence conflicti99 – 991R → G in BAE42559. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9393Missing in isoform 3. 1 PublicationVSP_017852Add
    BLAST
    Alternative sequencei1 – 11M → MAWHGETYCLIGGYRVYGDA PLPTPAKAEQEEKPVPRRAP KRQRVQEESDQDLGCPGAKV PRLKLKHGGKGLSRPSSVPA CSALSKM in isoform 2. 1 PublicationVSP_017853
    Alternative sequencei176 – 1794ALNS → VKWIYSG in isoform 2. 1 PublicationVSP_017854
    Alternative sequencei334 – 3407DHFDHIR → EKGQQKHQFTPPRDTHFV in isoform 2. 1 PublicationVSP_017855

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF488552 mRNA. Translation: AAP84986.1.
    AK089244 mRNA. Translation: BAC40810.1.
    AK155417 mRNA. Translation: BAE33255.1.
    AK170094 mRNA. Translation: BAE41559.1.
    AK170970 mRNA. Translation: BAE42149.1.
    AK171044 mRNA. Translation: BAE42209.1.
    AK171122 mRNA. Translation: BAE42264.1.
    AK171155 mRNA. Translation: BAE42280.1.
    AK171196 mRNA. Translation: BAE42306.1.
    AK171268 mRNA. Translation: BAE42354.1.
    AK171503 mRNA. Translation: BAE42494.1.
    AK171606 mRNA. Translation: BAE42559.1.
    CCDSiCCDS22625.1. [Q8C255-2]
    RefSeqiNP_795887.2. NM_176913.3. [Q8C255-2]
    XP_006531142.1. XM_006531079.1. [Q8C255-1]
    XP_006531143.1. XM_006531080.1. [Q8C255-3]
    UniGeneiMm.248357.

    Genome annotation databases

    EnsembliENSMUST00000034373; ENSMUSP00000034373; ENSMUSG00000053687. [Q8C255-1]
    ENSMUST00000081998; ENSMUSP00000080659; ENSMUSG00000053687. [Q8C255-2]
    ENSMUST00000117555; ENSMUSP00000113877; ENSMUSG00000053687. [Q8C255-3]
    GeneIDi319446.
    KEGGimmu:319446.
    UCSCiuc009nev.1. mouse. [Q8C255-3]
    uc009ney.1. mouse. [Q8C255-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF488552 mRNA. Translation: AAP84986.1 .
    AK089244 mRNA. Translation: BAC40810.1 .
    AK155417 mRNA. Translation: BAE33255.1 .
    AK170094 mRNA. Translation: BAE41559.1 .
    AK170970 mRNA. Translation: BAE42149.1 .
    AK171044 mRNA. Translation: BAE42209.1 .
    AK171122 mRNA. Translation: BAE42264.1 .
    AK171155 mRNA. Translation: BAE42280.1 .
    AK171196 mRNA. Translation: BAE42306.1 .
    AK171268 mRNA. Translation: BAE42354.1 .
    AK171503 mRNA. Translation: BAE42494.1 .
    AK171606 mRNA. Translation: BAE42559.1 .
    CCDSi CCDS22625.1. [Q8C255-2 ]
    RefSeqi NP_795887.2. NM_176913.3. [Q8C255-2 ]
    XP_006531142.1. XM_006531079.1. [Q8C255-1 ]
    XP_006531143.1. XM_006531080.1. [Q8C255-3 ]
    UniGenei Mm.248357.

    3D structure databases

    ProteinModelPortali Q8C255.
    SMRi Q8C255. Positions 74-430.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M19.004.

    Proteomic databases

    PaxDbi Q8C255.
    PRIDEi Q8C255.

    Protocols and materials databases

    DNASUi 319446.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034373 ; ENSMUSP00000034373 ; ENSMUSG00000053687 . [Q8C255-1 ]
    ENSMUST00000081998 ; ENSMUSP00000080659 ; ENSMUSG00000053687 . [Q8C255-2 ]
    ENSMUST00000117555 ; ENSMUSP00000113877 ; ENSMUSG00000053687 . [Q8C255-3 ]
    GeneIDi 319446.
    KEGGi mmu:319446.
    UCSCi uc009nev.1. mouse. [Q8C255-3 ]
    uc009ney.1. mouse. [Q8C255-2 ]

    Organism-specific databases

    CTDi 64174.
    MGIi MGI:2442042. Dpep2.

    Phylogenomic databases

    eggNOGi COG2355.
    GeneTreei ENSGT00390000017920.
    HOGENOMi HOG000072016.
    HOVERGENi HBG002339.
    OMAi IEATHRQ.
    OrthoDBi EOG7SJD4N.
    PhylomeDBi Q8C255.
    TreeFami TF324523.

    Enzyme and pathway databases

    Reactomei REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    NextBioi 394746.
    PROi Q8C255.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C255.
    CleanExi MM_DPEP2.
    MM_MBD2.
    Genevestigatori Q8C255.

    Family and domain databases

    InterProi IPR000180. Dipep_AS.
    IPR028531. Dpep2.
    IPR008257. Renal_dipep_fam.
    [Graphical view ]
    PANTHERi PTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF9. PTHR10443:SF9. 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. "Identification of two additional members of the membrane-bound dipeptidase family."
      Habib G.M., Shi Z.-Z., Cuevas A.A., Lieberman M.W.
      FASEB J. 17:1313-1315(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.
      Strain: C57BL/6.
      Tissue: Heart, Lung and Spleen.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell.

    Entry informationi

    Entry nameiDPEP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8C255
    Secondary accession number(s): Q3TAV9
    , Q3TBF7, Q3TBK3, Q3TBM9, Q7TQ53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 89 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

    External Data

    Dasty 3