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Protein

Adenosine deaminase

Gene

Ada

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

Functioni

Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).By similarity

Catalytic activityi

Adenosine + H2O = inosine + NH3.

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Kineticsi

  1. KM=20 µM for adenosine2 Publications

    pH dependencei

    Optimum pH is 6-8.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi15 – 151Zinc; catalytic
    Metal bindingi17 – 171Zinc; catalytic
    Binding sitei17 – 171Substrate
    Binding sitei19 – 191Substrate
    Binding sitei184 – 1841Substrate; via amide nitrogen and carbonyl oxygen
    Metal bindingi214 – 2141Zinc; catalytic
    Active sitei217 – 2171Proton donor2 Publications
    Sitei238 – 2381Important for catalytic activity
    Metal bindingi295 – 2951Zinc; catalytic
    Binding sitei296 – 2961Substrate

    GO - Molecular functioni

    • adenosine deaminase activity Source: UniProtKB
    • purine nucleoside binding Source: Ensembl
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • adenosine catabolic process Source: UniProtKB
    • aging Source: Ensembl
    • dATP catabolic process Source: MGI
    • deoxyadenosine catabolic process Source: MGI
    • embryonic digestive tract development Source: MGI
    • germinal center B cell differentiation Source: MGI
    • histamine secretion Source: Ensembl
    • hypoxanthine biosynthetic process Source: MGI
    • hypoxanthine salvage Source: GO_Central
    • inosine biosynthetic process Source: UniProtKB
    • in utero embryonic development Source: MGI
    • liver development Source: MGI
    • lung alveolus development Source: MGI
    • lung development Source: MGI
    • negative regulation of adenosine receptor signaling pathway Source: MGI
    • negative regulation of apoptotic process Source: MGI
    • negative regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
    • negative regulation of inflammatory response Source: MGI
    • negative regulation of leukocyte migration Source: MGI
    • negative regulation of mature B cell apoptotic process Source: MGI
    • negative regulation of mucus secretion Source: MGI
    • negative regulation of penile erection Source: MGI
    • negative regulation of thymocyte apoptotic process Source: MGI
    • Peyer's patch development Source: MGI
    • placenta development Source: MGI
    • positive regulation of alpha-beta T cell differentiation Source: MGI
    • positive regulation of B cell proliferation Source: MGI
    • positive regulation of calcium-mediated signaling Source: MGI
    • positive regulation of germinal center formation Source: MGI
    • positive regulation of heart rate Source: MGI
    • positive regulation of smooth muscle contraction Source: MGI
    • positive regulation of T cell activation Source: MGI
    • positive regulation of T cell differentiation Source: MGI
    • positive regulation of T cell differentiation in thymus Source: MGI
    • positive regulation of T cell receptor signaling pathway Source: MGI
    • purine nucleotide salvage Source: MGI
    • purine ribonucleoside monophosphate biosynthetic process Source: InterPro
    • regulation of cell-cell adhesion mediated by integrin Source: MGI
    • regulation of T cell differentiation Source: MGI
    • response to drug Source: Ensembl
    • response to hydrogen peroxide Source: Ensembl
    • response to hypoxia Source: MGI
    • response to morphine Source: Ensembl
    • response to vitamin E Source: Ensembl
    • T cell activation Source: MGI
    • trophectodermal cell differentiation Source: MGI
    • xanthine biosynthetic process Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell adhesion, Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.4.4. 3474.
    ReactomeiREACT_345398. Purine salvage.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosine deaminase (EC:3.5.4.4)
    Alternative name(s):
    Adenosine aminohydrolase
    Gene namesi
    Name:Ada
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 2

    Organism-specific databases

    MGIiMGI:87916. Ada.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Lethal at perinatal stages. Fetuses are viable up to 18 dpc, but after this survival decreases rapidly. Fewer that 10% of mutant pups are born live, and these die within hours after birth. Mutant fetuses display much higher than normal levels of adenosine and dATP, respiratory distress, hepatocellular degeneration and necrosis. Prenatal lethality can be avoided using an ADA expression vector with a trophoblast-specific promoter. Mutant mice die after about three weeks due to immunodeficiency, disturbances in purine metabolism and severe lung inflammation.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi217 – 2171E → D: Reduces catalytic activity 700-fold. No effect on affinity for adenosine. 1 Publication
    Mutagenesisi217 – 2171E → G: Reduces catalytic activity 3200-fold. No effect on affinity for adenosine. 1 Publication
    Mutagenesisi217 – 2171E → Q: Reduces catalytic activity 4800-fold, and slighly increases affinity for substrate. 1 Publication
    Mutagenesisi217 – 2171E → S: Loss of activity. 1 Publication
    Mutagenesisi238 – 2381H → A: Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold. 1 Publication
    Mutagenesisi238 – 2381H → E: Nearly abolishes enzyme activity. 1 Publication
    Mutagenesisi238 – 2381H → R: Reduces enzyme activity 1500-fold. No effect on affinity for adenosine. 1 Publication
    Mutagenesisi295 – 2951D → E: No effect on affinity for adenosine. Reduces enzyme activity 2750-fold. 1 Publication
    Mutagenesisi296 – 2961D → A: Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold. 1 Publication
    Mutagenesisi296 – 2961D → N: Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 352351Adenosine deaminasePRO_0000194353Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei54 – 541N6-acetyllysineBy similarity
    Modified residuei232 – 2321N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP03958.
    PaxDbiP03958.
    PRIDEiP03958.

    2D gel databases

    REPRODUCTION-2DPAGEP03958.

    PTM databases

    PhosphoSiteiP03958.

    Expressioni

    Tissue specificityi

    Detected in brain neurons in the median emninence (at protein level). Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues.1 Publication

    Gene expression databases

    BgeeiP03958.
    CleanExiMM_ADA.
    ExpressionAtlasiP03958. baseline and differential.
    GenevisibleiP03958. MM.

    Interactioni

    Subunit structurei

    Interacts with DPP4 (extracellular domain).By similarity

    Protein-protein interaction databases

    IntActiP03958. 1 interaction.
    MINTiMINT-4087128.
    STRINGi10090.ENSMUSP00000017841.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 133Combined sources
    Helixi18 – 203Combined sources
    Helixi24 – 3411Combined sources
    Helixi43 – 508Combined sources
    Helixi58 – 625Combined sources
    Helixi65 – 728Combined sources
    Helixi76 – 9217Combined sources
    Beta strandi95 – 1028Combined sources
    Helixi105 – 1073Combined sources
    Beta strandi109 – 1113Combined sources
    Helixi116 – 1183Combined sources
    Helixi126 – 14419Combined sources
    Beta strandi147 – 1559Combined sources
    Helixi159 – 1613Combined sources
    Helixi162 – 17110Combined sources
    Turni174 – 1763Combined sources
    Beta strandi177 – 1848Combined sources
    Helixi191 – 1933Combined sources
    Helixi195 – 20713Combined sources
    Beta strandi210 – 21910Combined sources
    Helixi221 – 2299Combined sources
    Beta strandi234 – 2385Combined sources
    Helixi240 – 2445Combined sources
    Helixi246 – 2549Combined sources
    Beta strandi258 – 2614Combined sources
    Helixi263 – 2686Combined sources
    Beta strandi270 – 2723Combined sources
    Helixi279 – 2857Combined sources
    Beta strandi289 – 2924Combined sources
    Helixi297 – 3004Combined sources
    Helixi304 – 31512Combined sources
    Helixi319 – 33214Combined sources
    Beta strandi333 – 3353Combined sources
    Helixi337 – 35014Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4LX-ray2.60A/B/C/D4-352[»]
    1A4MX-ray1.95A/B/C/D4-352[»]
    1ADDX-ray2.40A4-352[»]
    1FKWX-ray2.40A4-352[»]
    1FKXX-ray2.40A4-352[»]
    1UIOX-ray2.40A4-352[»]
    1UIPX-ray2.40A4-352[»]
    2ADAX-ray2.40A1-352[»]
    3KM8X-ray2.00A/B1-352[»]
    3MVIX-ray1.60A/B4-352[»]
    3MVTX-ray2.20A/C4-352[»]
    3T1GX-ray2.35A4-352[»]
    ProteinModelPortaliP03958.
    SMRiP03958. Positions 4-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03958.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    HOGENOMiHOG000218816.
    HOVERGENiHBG001718.
    InParanoidiP03958.
    KOiK01488.
    OMAiLYKAYGM.
    OrthoDBiEOG7GN2MZ.
    PhylomeDBiP03958.
    TreeFamiTF314270.

    Family and domain databases

    HAMAPiMF_00540. A_deaminase.
    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR028893. A_deaminase.
    IPR006330. Ado/ade_deaminase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01430. aden_deam. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P03958-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII
    60 70 80 90 100
    GMDKPLSLPG FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV
    110 120 130 140 150
    RYSPHLLANS KVDPMPWNQT EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS
    160 170 180 190 200
    ILCCMRHQPS WSLEVLELCK KYNQKTVVAM DLAGDETIEG SSLFPGHVEA
    210 220 230 240 250
    YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY HTIEDEALYN
    260 270 280 290 300
    RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF
    310 320 330 340 350
    KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE

    YQ
    Length:352
    Mass (Da):39,992
    Last modified:January 23, 2007 - v3
    Checksum:iE53A8A1FABA148CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411E → R in AAB07142 (PubMed:2387582).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M10319 mRNA. Translation: AAA37173.1.
    M34251
    , M34242, M34243, M34244, M34246, M34247, M34248, M34249, M34250 Genomic DNA. Translation: AAB07142.1.
    U73107 Genomic DNA. Translation: AAC08442.1.
    AF483480 mRNA. Translation: AAL90754.1.
    AF483481 mRNA. Translation: AAL90755.1.
    AK075899 mRNA. Translation: BAC36039.1.
    BC002075 mRNA. Translation: AAH02075.1.
    CCDSiCCDS17015.1.
    PIRiA01010. DUMSA.
    RefSeqiNP_001258981.1. NM_001272052.1.
    NP_031424.1. NM_007398.4.
    UniGeneiMm.388.

    Genome annotation databases

    EnsembliENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697.
    GeneIDi11486.
    KEGGimmu:11486.
    UCSCiuc008ntl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M10319 mRNA. Translation: AAA37173.1.
    M34251
    , M34242, M34243, M34244, M34246, M34247, M34248, M34249, M34250 Genomic DNA. Translation: AAB07142.1.
    U73107 Genomic DNA. Translation: AAC08442.1.
    AF483480 mRNA. Translation: AAL90754.1.
    AF483481 mRNA. Translation: AAL90755.1.
    AK075899 mRNA. Translation: BAC36039.1.
    BC002075 mRNA. Translation: AAH02075.1.
    CCDSiCCDS17015.1.
    PIRiA01010. DUMSA.
    RefSeqiNP_001258981.1. NM_001272052.1.
    NP_031424.1. NM_007398.4.
    UniGeneiMm.388.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4LX-ray2.60A/B/C/D4-352[»]
    1A4MX-ray1.95A/B/C/D4-352[»]
    1ADDX-ray2.40A4-352[»]
    1FKWX-ray2.40A4-352[»]
    1FKXX-ray2.40A4-352[»]
    1UIOX-ray2.40A4-352[»]
    1UIPX-ray2.40A4-352[»]
    2ADAX-ray2.40A1-352[»]
    3KM8X-ray2.00A/B1-352[»]
    3MVIX-ray1.60A/B4-352[»]
    3MVTX-ray2.20A/C4-352[»]
    3T1GX-ray2.35A4-352[»]
    ProteinModelPortaliP03958.
    SMRiP03958. Positions 4-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP03958. 1 interaction.
    MINTiMINT-4087128.
    STRINGi10090.ENSMUSP00000017841.

    Chemistry

    BindingDBiP03958.
    ChEMBLiCHEMBL3206.

    PTM databases

    PhosphoSiteiP03958.

    2D gel databases

    REPRODUCTION-2DPAGEP03958.

    Proteomic databases

    MaxQBiP03958.
    PaxDbiP03958.
    PRIDEiP03958.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697.
    GeneIDi11486.
    KEGGimmu:11486.
    UCSCiuc008ntl.1. mouse.

    Organism-specific databases

    CTDi100.
    MGIiMGI:87916. Ada.

    Phylogenomic databases

    eggNOGiCOG1816.
    HOGENOMiHOG000218816.
    HOVERGENiHBG001718.
    InParanoidiP03958.
    KOiK01488.
    OMAiLYKAYGM.
    OrthoDBiEOG7GN2MZ.
    PhylomeDBiP03958.
    TreeFamiTF314270.

    Enzyme and pathway databases

    BRENDAi3.5.4.4. 3474.
    ReactomeiREACT_345398. Purine salvage.

    Miscellaneous databases

    ChiTaRSiAda. mouse.
    EvolutionaryTraceiP03958.
    NextBioi278844.
    PROiP03958.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP03958.
    CleanExiMM_ADA.
    ExpressionAtlasiP03958. baseline and differential.
    GenevisibleiP03958. MM.

    Family and domain databases

    HAMAPiMF_00540. A_deaminase.
    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR028893. A_deaminase.
    IPR006330. Ado/ade_deaminase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01430. aden_deam. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli."
      Yeung C.-Y., Ingolia D.E., Roth D.B., Shoemaker C., Al-Ubaidi M.R., Yen J.-Y., Ching C., Bobonis C., Kaufman R.J., Kellems R.E.
      J. Biol. Chem. 260:10299-10307(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural and functional analysis of the murine adenosine deaminase gene."
      Al-Ubaidi M.R., Ramamurthy V., Maa M.C., Ingolia D.E., Chinsky J.M., Martin B.D., Kellems R.E.
      Genomics 7:476-485(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The comparative sequence analysis of murine and human ADA genes."
      Xu P., Winston J.W., Lu J., Muzny D.M., Gibbs R.A., Kellems R.E.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ILS and ISS.
    5. "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: Tongue.
    6. "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 tumor.
    7. "Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death."
      Migchielsen A.A., Breuer M.L., van Roon M.A., te Riele H., Zurcher C., Ossendorp F., Toutain S., Hershfield M.S., Berns A., Valerio D.
      Nat. Genet. 10:279-287(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. Cited for: DISRUPTION PHENOTYPE.
    9. "Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase."
      Mohamedali K.A., Kurz L.C., Rudolph F.B.
      Biochemistry 35:1672-1680(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-217, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE, PROPOSED ENZYME MECHANISM.
    10. "Adenosine deaminase in rodent median eminence: detection by antibody to the mouse enzyme and co-localization with adenosine deaminase-complexing protein (CD26)."
      Nagy J.I., Yamamoto T., Uemura H., Schrader W.P.
      Neuroscience 73:459-471(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Metabolic consequences of adenosine deaminase deficiency in mice are associated with defects in alveogenesis, pulmonary inflammation, and airway obstruction."
      Blackburn M.R., Volmer J.B., Thrasher J.L., Zhong H., Crosby J.R., Lee J.J., Kellems R.E.
      J. Exp. Med. 192:159-170(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    12. "Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations."
      Wilson D.K., Rudolph F.B., Quiocho F.A.
      Science 252:1278-1284(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TRANSITION STATE ANALOG 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE, COFACTOR, PROPOSED ENZYME MECHANISM.
    13. "Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase."
      Sideraki V., Mohamedali K.A., Wilson D.K., Chang Z., Kellems R.E., Quiocho F.A., Rudolph F.B.
      Biochemistry 35:7862-7872(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-352 OF MUTANTS GLU-295 AND ALA-296 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-295 AND ASP-296.
    14. "Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation."
      Sideraki V., Wilson D.K., Kurz L.C., Quiocho F.A., Rudolph F.B.
      Biochemistry 35:15019-15028(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS ALA-238 AND GLU-238 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, MUTAGENESIS OF HIS-238.
    15. "Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity."
      Wang Z., Quiocho F.A.
      Biochemistry 37:8314-8324(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND INHIBITOR, COFACTOR, ACTIVE SITE.

    Entry informationi

    Entry nameiADA_MOUSE
    AccessioniPrimary (citable) accession number: P03958
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 158 of the entry and version 3 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

    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.