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P56389

- CDD_MOUSE

UniProt

P56389 - CDD_MOUSE

Protein

Cytidine deaminase

Gene

Cda

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

    This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.By similarity

    Catalytic activityi

    Cytidine + H2O = uridine + NH3.
    2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.

    Cofactori

    Zinc.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi65 – 651Zinc; catalytic
    Active sitei67 – 671Proton donor1 Publication
    Metal bindingi99 – 991Zinc; catalytic
    Metal bindingi102 – 1021Zinc; catalytic

    GO - Molecular functioni

    1. cytidine deaminase activity Source: UniProtKB
    2. identical protein binding Source: MGI
    3. nucleoside binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cytidine deamination Source: UniProtKB
    2. negative regulation of cell growth Source: UniProtKB
    3. negative regulation of nucleotide metabolic process Source: UniProtKB
    4. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytidine deaminase (EC:3.5.4.5)
    Alternative name(s):
    Cytidine aminohydrolase
    Gene namesi
    Name:Cda
    Synonyms:Cdd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1919519. Cda.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 146146Cytidine deaminasePRO_0000171683Add
    BLAST

    Proteomic databases

    MaxQBiP56389.
    PaxDbiP56389.
    PRIDEiP56389.

    PTM databases

    PhosphoSiteiP56389.

    Expressioni

    Gene expression databases

    ArrayExpressiP56389.
    BgeeiP56389.
    CleanExiMM_CDA.
    GenevestigatoriP56389.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    MINTiMINT-218728.

    Structurei

    Secondary structure

    1
    146
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2614
    Turni32 – 343
    Beta strandi38 – 447
    Beta strandi49 – 535
    Helixi60 – 623
    Helixi66 – 7611
    Beta strandi82 – 909
    Beta strandi92 – 943
    Helixi100 – 1089
    Beta strandi114 – 1185
    Beta strandi124 – 1285
    Helixi129 – 1324
    Helixi139 – 1424

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZABX-ray2.36A/B/C/D1-146[»]
    2FR5X-ray1.48A/B/C/D1-146[»]
    2FR6X-ray2.07A/B/C/D1-146[»]
    ProteinModelPortaliP56389.
    SMRiP56389. Positions 10-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56389.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 117102CMP/dCMP deaminase zinc-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 563Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0295.
    GeneTreeiENSGT00390000000911.
    HOGENOMiHOG000014707.
    HOVERGENiHBG005294.
    InParanoidiP56389.
    KOiK01489.
    OMAiTDWAVYM.
    OrthoDBiEOG75B872.
    PhylomeDBiP56389.
    TreeFamiTF314486.

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR006262. Cyt_deam_tetra.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view]
    PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53927. SSF53927. 1 hit.
    TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56389-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF    50
    SGCNIENACY PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG 100
    ACRQVMREFG TDWAVYMTKP DGTFVVRTVQ ELLPASFGPE DLQKIQ 146
    Length:146
    Mass (Da):16,131
    Last modified:March 29, 2005 - v2
    Checksum:iD4181CE6BA9CD794
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK008793 mRNA. Translation: BAB25898.1.
    BC050114 mRNA. Translation: AAH50114.1.
    CCDSiCCDS18826.1.
    RefSeqiNP_082452.1. NM_028176.1.
    UniGeneiMm.46182.

    Genome annotation databases

    EnsembliENSMUST00000030535; ENSMUSP00000030535; ENSMUSG00000028755.
    GeneIDi72269.
    KEGGimmu:72269.
    UCSCiuc008vkw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK008793 mRNA. Translation: BAB25898.1 .
    BC050114 mRNA. Translation: AAH50114.1 .
    CCDSi CCDS18826.1.
    RefSeqi NP_082452.1. NM_028176.1.
    UniGenei Mm.46182.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZAB X-ray 2.36 A/B/C/D 1-146 [» ]
    2FR5 X-ray 1.48 A/B/C/D 1-146 [» ]
    2FR6 X-ray 2.07 A/B/C/D 1-146 [» ]
    ProteinModelPortali P56389.
    SMRi P56389. Positions 10-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-218728.

    Chemistry

    BindingDBi P56389.
    ChEMBLi CHEMBL2110.

    PTM databases

    PhosphoSitei P56389.

    Proteomic databases

    MaxQBi P56389.
    PaxDbi P56389.
    PRIDEi P56389.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030535 ; ENSMUSP00000030535 ; ENSMUSG00000028755 .
    GeneIDi 72269.
    KEGGi mmu:72269.
    UCSCi uc008vkw.1. mouse.

    Organism-specific databases

    CTDi 978.
    MGIi MGI:1919519. Cda.

    Phylogenomic databases

    eggNOGi COG0295.
    GeneTreei ENSGT00390000000911.
    HOGENOMi HOG000014707.
    HOVERGENi HBG005294.
    InParanoidi P56389.
    KOi K01489.
    OMAi TDWAVYM.
    OrthoDBi EOG75B872.
    PhylomeDBi P56389.
    TreeFami TF314486.

    Miscellaneous databases

    EvolutionaryTracei P56389.
    NextBioi 335863.
    PROi P56389.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56389.
    Bgeei P56389.
    CleanExi MM_CDA.
    Genevestigatori P56389.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR006262. Cyt_deam_tetra.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view ]
    Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53927. SSF53927. 1 hit.
    TIGRFAMsi TIGR01354. cyt_deam_tetra. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: C57BL/6J.
      Tissue: Stomach.
    2. "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: Pancreas.
    3. "The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse."
      Teh A.H., Kimura M., Yamamoto M., Tanaka N., Yamaguchi I., Kumasaka T.
      Biochemistry 45:7825-7833(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH CYTIDINE, SUBUNIT, COFACTOR, ACTIVE SITE, SUBSTRATE-BINDING REGION, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiCDD_MOUSE
    AccessioniPrimary (citable) accession number: P56389
    Secondary accession number(s): Q9D7V3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3