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Protein

Dipeptidase 2

Gene

Dpep2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+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

    Complete GO annotation...

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM19.002.

    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 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:2442042. Dpep2.

    Subcellular locationi

    • Membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    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

    MaxQBiQ8C255.
    PaxDbiQ8C255.
    PRIDEiQ8C255.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ8C255.
    CleanExiMM_DPEP2.
    MM_MBD2.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.PROSITE-ProRule annotation

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000080659.

    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.
    InParanoidiQ8C255.
    KOiK01273.
    OMAiVDILETC.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MSLTGLKGHW VLGHGLSVFL LVLLLLGPSQ PLIWTQTKPG FSGASTTSSI
    60 70 80 90 100
    PRALTKPDIS SIPTTPGNPN FPDLRDRARA LMQEFPLIDG HNDMPLVLRQ
    110 120 130 140 150
    FYQNGLQDAN LRNFTHGQTS LDRLKDGLVG AQFWSAYVPC QTQDRDALRL
    160 170 180 190 200
    TLEQIDLIRR ICASYSELEL VTSVKALNST QKLACLIGVE GGHSLDNSLA
    210 220 230 240 250
    VLRSFYLLGV RYLTLTHTCN TPWAETSSKG VHAFYSSVTG LTSFGEKVVA
    260 270 280 290 300
    EMNRLGMMVD LSHVSDAAAR RALEVSQAPV IFSHSAARAV CPNARNLPDD
    310 320 330 340 350
    LLQLLKKNGG IVMVTFSVGV LPCNPLANVS TVADHFDHIR SVIGSEFIGI
    360 370 380 390 400
    GGDYDGTKQF PQGLEDVSTY PVLIEELLRR GWNEQELQGI LRGNLLRVFR
    410 420 430 440 450
    QVEQVRDKSK WQSPLEDMIP EEQLDSACHS ALRPQKQHPE KNQPETPEYH
    460 470
    ILKFSHSKSS PHIVPSLAIV ATLLGLIV
    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:
    EMBLi
    GenBanki
    DDBJi
    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_001288133.1. NM_001301204.1. [Q8C255-1]
    NP_001288134.1. NM_001301205.1. [Q8C255-3]
    NP_795887.2. NM_176913.4. [Q8C255-2]
    UniGeneiMm.248357.
    Mm.470084.

    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:
    EMBLi
    GenBanki
    DDBJi
    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_001288133.1. NM_001301204.1. [Q8C255-1]
    NP_001288134.1. NM_001301205.1. [Q8C255-3]
    NP_795887.2. NM_176913.4. [Q8C255-2]
    UniGeneiMm.248357.
    Mm.470084.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000080659.

    Protein family/group databases

    MEROPSiM19.002.

    Proteomic databases

    MaxQBiQ8C255.
    PaxDbiQ8C255.
    PRIDEiQ8C255.

    Protocols and materials databases

    DNASUi319446.
    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi64174.
    MGIiMGI:2442042. Dpep2.

    Phylogenomic databases

    eggNOGiCOG2355.
    GeneTreeiENSGT00390000017920.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    InParanoidiQ8C255.
    KOiK01273.
    OMAiVDILETC.
    OrthoDBiEOG7SJD4N.
    PhylomeDBiQ8C255.
    TreeFamiTF324523.

    Miscellaneous databases

    NextBioi394746.
    PROiQ8C255.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8C255.
    CleanExiMM_DPEP2.
    MM_MBD2.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 94 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.