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Q9D1A2

- CNDP2_MOUSE

UniProt

Q9D1A2 - CNDP2_MOUSE

Protein

Cytosolic non-specific dipeptidase

Gene

Cndp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Hydrolyzes a variety of dipeptides including L-carnosine. Has a strong preference for Cys-Gly By similarity.By similarity

    Catalytic activityi

    Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.2 Publications

    Enzyme regulationi

    Inhibited by bestatin.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Manganese 21 Publication
    Active sitei101 – 1011By similarity
    Metal bindingi132 – 1321Manganese 11 Publication
    Metal bindingi132 – 1321Manganese 21 Publication
    Active sitei166 – 1661Proton acceptorBy similarity
    Metal bindingi167 – 1671Manganese 11 Publication
    Metal bindingi195 – 1951Manganese 21 Publication
    Binding sitei195 – 1951Substrate; via carbonyl oxygen
    Binding sitei228 – 2281Substrate; shared with homodimeric partner
    Sitei228 – 2281Important for catalytic activity
    Binding sitei330 – 3301Substrate; shared with homodimeric partner
    Binding sitei343 – 3431Substrate
    Binding sitei417 – 4171Substrate; via amide nitrogen and carbonyl oxygen
    Metal bindingi445 – 4451Manganese 11 Publication
    Binding sitei445 – 4451Substrate

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. dipeptidase activity Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. metallopeptidase activity Source: UniProtKB-KW
    5. peptidase activity Source: MGI
    6. tripeptidase activity Source: InterPro

    GO - Biological processi

    1. proteolysis Source: MGI

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_202492. Sulfur amino acid metabolism.
    REACT_210980. Glutathione synthesis and recycling.

    Protein family/group databases

    MEROPSiM20.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic non-specific dipeptidase (EC:3.4.13.18)
    Alternative name(s):
    CNDP dipeptidase 2
    Glutamate carboxypeptidase-like protein 1
    Gene namesi
    Name:Cndp2
    Synonyms:Cn2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1913304. Cndp2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2281H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 475474Cytosolic non-specific dipeptidasePRO_0000185273Add
    BLAST

    Proteomic databases

    MaxQBiQ9D1A2.
    PaxDbiQ9D1A2.
    PRIDEiQ9D1A2.

    2D gel databases

    REPRODUCTION-2DPAGEQ9D1A2.

    PTM databases

    PhosphoSiteiQ9D1A2.

    Expressioni

    Tissue specificityi

    Highly expressed in the parafascicular nucleus of the thalamus, tuberomammillary nucleus of the hypothalamus and the mitral cell layer of the olfactory bulb.1 Publication

    Gene expression databases

    ArrayExpressiQ9D1A2.
    BgeeiQ9D1A2.
    CleanExiMM_CNDP2.
    GenevestigatoriQ9D1A2.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi211181. 1 interaction.
    IntActiQ9D1A2. 2 interactions.
    MINTiMINT-1855384.
    STRINGi10090.ENSMUSP00000025546.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1312
    Helixi15 – 2713
    Helixi35 – 373
    Helixi38 – 5417
    Beta strandi58 – 625
    Beta strandi66 – 683
    Beta strandi74 – 763
    Beta strandi80 – 856
    Beta strandi93 – 997
    Helixi107 – 1093
    Beta strandi119 – 1213
    Beta strandi124 – 1274
    Turni128 – 1336
    Helixi134 – 14916
    Beta strandi155 – 16410
    Helixi166 – 1683
    Helixi173 – 1797
    Turni180 – 1878
    Beta strandi190 – 1934
    Beta strandi199 – 2035
    Beta strandi205 – 2106
    Beta strandi212 – 22110
    Helixi229 – 2324
    Turni233 – 2353
    Helixi239 – 2479
    Turni260 – 2656
    Helixi271 – 2766
    Helixi284 – 2907
    Helixi301 – 3099
    Beta strandi313 – 32210
    Beta strandi325 – 3273
    Beta strandi334 – 34411
    Helixi350 – 36617
    Beta strandi372 – 38211
    Helixi392 – 40514
    Beta strandi410 – 4167
    Helixi420 – 4289
    Beta strandi430 – 4345
    Beta strandi450 – 4523
    Helixi453 – 47220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZOFX-ray2.30A/B1-475[»]
    2ZOGX-ray1.70A/B1-475[»]
    ProteinModelPortaliQ9D1A2.
    SMRiQ9D1A2. Positions 1-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9D1A2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 1672Substrate binding

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    eggNOGiCOG0624.
    GeneTreeiENSGT00390000009682.
    HOGENOMiHOG000216709.
    HOVERGENiHBG051103.
    InParanoidiQ3U7B9.
    KOiK08660.
    OMAiTDGAHSI.
    OrthoDBiEOG7JHM55.
    PhylomeDBiQ9D1A2.
    TreeFamiTF300633.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR001261. ArgE/DapE_CS.
    IPR017153. GSH_degradosome_DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
    PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9D1A2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSALKAVFQY IDENQDRYVK KLAEWVAIQS VSAWPEKRGE IRRMMEVAAA    50
    DVQRLGGSVE LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL 100
    DVQPAALEDG WDSEPFTLVE REGKLYGRGS TDDKGPVAGW MNALEAYQKT 150
    GQEIPVNLRF CLEGMEESGS EGLDELIFAQ KDKFFKDVDY VCISDNYWLG 200
    KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM TDLISLMGCL 250
    VDKKGKILIP GINDAVAPVT DEEHALYDHI DFDMEEFAKD VGAETLLHSC 300
    KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPDMIP 350
    EVVSEQVSSY LSKKFAELQS PNKFKVYMGH GGKPWVSDFN HPHYQAGRRA 400
    LKTVFGVEPD LTREGGSIPV TLTFQEATGK NVMLLPVGSA DDGAHSQNEK 450
    LNRLNYIEGT KMLAAYLYEV SQLKN 475
    Length:475
    Mass (Da):52,767
    Last modified:June 1, 2001 - v1
    Checksum:i086950275A698500
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451M → I in BAE31451. (PubMed:16141072)Curated
    Sequence conflicti105 – 1051A → T in BAE42789. (PubMed:16141072)Curated
    Sequence conflicti357 – 3571V → A in BAB21596. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046738 mRNA. Translation: BAB21596.1.
    AK003779 mRNA. Translation: BAB22991.1.
    AK151013 mRNA. Translation: BAE30033.1.
    AK152729 mRNA. Translation: BAE31451.1.
    AK168029 mRNA. Translation: BAE40014.1.
    AK168652 mRNA. Translation: BAE40509.1.
    AK172034 mRNA. Translation: BAE42789.1.
    BC005532 mRNA. Translation: AAH05532.1.
    CCDSiCCDS29383.1.
    RefSeqiNP_001276460.1. NM_001289531.1.
    NP_075638.2. NM_023149.3.
    UniGeneiMm.29646.

    Genome annotation databases

    EnsembliENSMUST00000025546; ENSMUSP00000025546; ENSMUSG00000024644.
    ENSMUST00000168419; ENSMUSP00000128696; ENSMUSG00000024644.
    GeneIDi66054.
    KEGGimmu:66054.
    UCSCiuc008fut.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046738 mRNA. Translation: BAB21596.1 .
    AK003779 mRNA. Translation: BAB22991.1 .
    AK151013 mRNA. Translation: BAE30033.1 .
    AK152729 mRNA. Translation: BAE31451.1 .
    AK168029 mRNA. Translation: BAE40014.1 .
    AK168652 mRNA. Translation: BAE40509.1 .
    AK172034 mRNA. Translation: BAE42789.1 .
    BC005532 mRNA. Translation: AAH05532.1 .
    CCDSi CCDS29383.1.
    RefSeqi NP_001276460.1. NM_001289531.1.
    NP_075638.2. NM_023149.3.
    UniGenei Mm.29646.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZOF X-ray 2.30 A/B 1-475 [» ]
    2ZOG X-ray 1.70 A/B 1-475 [» ]
    ProteinModelPortali Q9D1A2.
    SMRi Q9D1A2. Positions 1-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211181. 1 interaction.
    IntActi Q9D1A2. 2 interactions.
    MINTi MINT-1855384.
    STRINGi 10090.ENSMUSP00000025546.

    Protein family/group databases

    MEROPSi M20.005.

    PTM databases

    PhosphoSitei Q9D1A2.

    2D gel databases

    REPRODUCTION-2DPAGE Q9D1A2.

    Proteomic databases

    MaxQBi Q9D1A2.
    PaxDbi Q9D1A2.
    PRIDEi Q9D1A2.

    Protocols and materials databases

    DNASUi 66054.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025546 ; ENSMUSP00000025546 ; ENSMUSG00000024644 .
    ENSMUST00000168419 ; ENSMUSP00000128696 ; ENSMUSG00000024644 .
    GeneIDi 66054.
    KEGGi mmu:66054.
    UCSCi uc008fut.1. mouse.

    Organism-specific databases

    CTDi 55748.
    MGIi MGI:1913304. Cndp2.

    Phylogenomic databases

    eggNOGi COG0624.
    GeneTreei ENSGT00390000009682.
    HOGENOMi HOG000216709.
    HOVERGENi HBG051103.
    InParanoidi Q3U7B9.
    KOi K08660.
    OMAi TDGAHSI.
    OrthoDBi EOG7JHM55.
    PhylomeDBi Q9D1A2.
    TreeFami TF300633.

    Enzyme and pathway databases

    Reactomei REACT_202492. Sulfur amino acid metabolism.
    REACT_210980. Glutathione synthesis and recycling.

    Miscellaneous databases

    EvolutionaryTracei Q9D1A2.
    NextBioi 320490.
    PROi Q9D1A2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D1A2.
    Bgeei Q9D1A2.
    CleanExi MM_CNDP2.
    Genevestigatori Q9D1A2.

    Family and domain databases

    Gene3Di 3.30.70.360. 1 hit.
    InterProi IPR001261. ArgE/DapE_CS.
    IPR017153. GSH_degradosome_DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view ]
    Pfami PF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037242. CNDP_dipeptidase. 1 hit.
    PROSITEi PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel mouse gene differentially expressed in kidney."
      Yoshikawa T., Nagasugi Y., Sugano S., Hashimoto K., Masuho Y., Seki N.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    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].
      Strain: BALB/c, C57BL/6J and NOD.
      Tissue: Bone marrow macrophage, Embryonic heart, Heart and Spleen.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Mammary gland.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-17; 311-329 AND 414-430, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "Identification and characterization of a mouse dipeptidase that hydrolyzes L-carnosine."
      Otani H., Okumura N., Hashida-Okumura A., Nagai K.
      J. Biochem. 137:167-175(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    6. "Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2."
      Unno H., Yamashita T., Ujita S., Okumura N., Otani H., Okumura A., Nagai K., Kusunoki M.
      J. Biol. Chem. 283:27289-27299(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MANGANESE AND BESTATIN, MUTAGENESIS OF HIS-228, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiCNDP2_MOUSE
    AccessioniPrimary (citable) accession number: Q9D1A2
    Secondary accession number(s): Q3TA80
    , Q3TI32, Q3U7B9, Q99PV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 107 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3