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P03958

- ADA_MOUSE

UniProt

P03958 - ADA_MOUSE

Protein

Adenosine deaminase

Gene

Ada

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    1. adenosine deaminase activity Source: UniProtKB
    2. purine nucleoside binding Source: Ensembl
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. adenosine catabolic process Source: UniProtKB
    2. aging Source: Ensembl
    3. cell adhesion Source: UniProtKB-KW
    4. dATP catabolic process Source: MGI
    5. deoxyadenosine catabolic process Source: MGI
    6. embryonic digestive tract development Source: MGI
    7. germinal center B cell differentiation Source: MGI
    8. histamine secretion Source: Ensembl
    9. hypoxanthine biosynthetic process Source: MGI
    10. hypoxanthine salvage Source: RefGenome
    11. inosine biosynthetic process Source: UniProtKB
    12. in utero embryonic development Source: MGI
    13. liver development Source: MGI
    14. lung alveolus development Source: MGI
    15. lung development Source: MGI
    16. negative regulation of adenosine receptor signaling pathway Source: RefGenome
    17. negative regulation of apoptotic process Source: MGI
    18. negative regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
    19. negative regulation of inflammatory response Source: MGI
    20. negative regulation of leukocyte migration Source: MGI
    21. negative regulation of mature B cell apoptotic process Source: MGI
    22. negative regulation of mucus secretion Source: MGI
    23. negative regulation of penile erection Source: MGI
    24. negative regulation of thymocyte apoptotic process Source: MGI
    25. Peyer's patch development Source: MGI
    26. placenta development Source: MGI
    27. positive regulation of alpha-beta T cell differentiation Source: MGI
    28. positive regulation of B cell proliferation Source: MGI
    29. positive regulation of calcium-mediated signaling Source: MGI
    30. positive regulation of germinal center formation Source: MGI
    31. positive regulation of heart rate Source: MGI
    32. positive regulation of smooth muscle contraction Source: MGI
    33. positive regulation of T cell activation Source: MGI
    34. positive regulation of T cell differentiation Source: MGI
    35. positive regulation of T cell differentiation in thymus Source: MGI
    36. positive regulation of T cell receptor signaling pathway Source: MGI
    37. purine nucleotide salvage Source: Ensembl
    38. purine ribonucleoside monophosphate biosynthetic process Source: InterPro
    39. regulation of cell-cell adhesion mediated by integrin Source: Ensembl
    40. regulation of T cell differentiation Source: MGI
    41. response to drug Source: Ensembl
    42. response to hydrogen peroxide Source: Ensembl
    43. response to hypoxia Source: Ensembl
    44. response to morphine Source: Ensembl
    45. response to vitamin E Source: Ensembl
    46. T cell activation Source: Ensembl
    47. trophectodermal cell differentiation Source: MGI
    48. xanthine biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell adhesion, Nucleotide metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    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: Chromosome 2

    Organism-specific databases

    MGIiMGI:87916. Ada.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity. Cell junction By similarity. Cytoplasmic vesicle lumen 1 Publication. Cytoplasm By similarity
    Note: Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cytoplasm Source: MGI
    3. cytoplasmic membrane-bounded vesicle lumen Source: UniProtKB-SubCell
    4. cytosol Source: RefGenome
    5. dendrite cytoplasm Source: Ensembl
    6. external side of plasma membrane Source: RefGenome
    7. extracellular space Source: Ensembl
    8. lysosome Source: Ensembl
    9. neuronal cell body Source: Ensembl

    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

    ArrayExpressiP03958.
    BgeeiP03958.
    CleanExiMM_ADA.
    GenevestigatoriP03958.

    Interactioni

    Subunit structurei

    Interacts with DPP4 (extracellular domain).By similarity

    Protein-protein interaction databases

    IntActiP03958. 1 interaction.
    MINTiMINT-4087128.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiDWMVAVL.
    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

    MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII    50
    GMDKPLSLPG FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV 100
    RYSPHLLANS KVDPMPWNQT EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS 150
    ILCCMRHQPS WSLEVLELCK KYNQKTVVAM DLAGDETIEG SSLFPGHVEA 200
    YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY HTIEDEALYN 250
    RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF 300
    KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE 350
    YQ 352
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17015.1.
    PIRi A01010. DUMSA.
    RefSeqi NP_001258981.1. NM_001272052.1.
    NP_031424.1. NM_007398.4.
    UniGenei Mm.388.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A4L X-ray 2.60 A/B/C/D 4-352 [» ]
    1A4M X-ray 1.95 A/B/C/D 4-352 [» ]
    1ADD X-ray 2.40 A 4-352 [» ]
    1FKW X-ray 2.40 A 4-352 [» ]
    1FKX X-ray 2.40 A 4-352 [» ]
    1UIO X-ray 2.40 A 4-352 [» ]
    1UIP X-ray 2.40 A 4-352 [» ]
    2ADA X-ray 2.40 A 1-352 [» ]
    3KM8 X-ray 2.00 A/B 1-352 [» ]
    3MVI X-ray 1.60 A/B 4-352 [» ]
    3MVT X-ray 2.20 A/C 4-352 [» ]
    3T1G X-ray 2.35 A 4-352 [» ]
    ProteinModelPortali P03958.
    SMRi P03958. Positions 4-352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03958. 1 interaction.
    MINTi MINT-4087128.

    Chemistry

    BindingDBi P03958.
    ChEMBLi CHEMBL3206.

    PTM databases

    PhosphoSitei P03958.

    2D gel databases

    REPRODUCTION-2DPAGE P03958.

    Proteomic databases

    MaxQBi P03958.
    PaxDbi P03958.
    PRIDEi P03958.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017841 ; ENSMUSP00000017841 ; ENSMUSG00000017697 .
    GeneIDi 11486.
    KEGGi mmu:11486.
    UCSCi uc008ntl.1. mouse.

    Organism-specific databases

    CTDi 100.
    MGIi MGI:87916. Ada.

    Phylogenomic databases

    eggNOGi COG1816.
    HOGENOMi HOG000218816.
    HOVERGENi HBG001718.
    InParanoidi P03958.
    KOi K01488.
    OMAi DWMVAVL.
    OrthoDBi EOG7GN2MZ.
    PhylomeDBi P03958.
    TreeFami TF314270.

    Miscellaneous databases

    ChiTaRSi ADA. mouse.
    EvolutionaryTracei P03958.
    NextBioi 278844.
    PROi P03958.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P03958.
    Bgeei P03958.
    CleanExi MM_ADA.
    Genevestigatori P03958.

    Family and domain databases

    HAMAPi MF_00540. A_deaminase.
    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR028893. A_deaminase.
    IPR006330. Ado/ade_deaminase.
    [Graphical view ]
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01430. aden_deam. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 151 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