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Protein

Adenosine deaminase

Gene

Ada

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:9272950). Plays an important role in purine metabolism and in adenosine homeostasis (PubMed:9272950, PubMed:10720488). Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events (PubMed:11435465). Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (By similarity). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity). Stimulates plasminogen activation (By similarity). Plays a role in male fertility (By similarity). Plays a protective role in early postimplantation embryonic development (PubMed:9272950).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=20 µM for adenosine2 Publications

    pH dependencei

    Optimum pH is 6-8.5.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi15Zinc; catalyticCombined sources4 Publications1
    Metal bindingi17Zinc; catalyticCombined sources4 Publications1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei17SubstrateCombined sources4 Publications1
    Binding sitei19SubstrateCombined sources4 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei58Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity1
    Sitei62Important for interaction with adenosine receptors and increasing their affinity for agonistsBy similarity1
    Binding sitei184Substrate; via amide nitrogen and carbonyl oxygenCombined sources4 Publications1
    Metal bindingi214Zinc; catalyticCombined sources4 Publications1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei217Proton donor2 Publications1
    Sitei238Important for catalytic activity2 Publications1
    Metal bindingi295Zinc; catalyticCombined sources4 Publications1
    Binding sitei296SubstrateCombined sources2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    Biological processCell adhesion, Nucleotide metabolism
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.4.4 3474

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-74217 Purine salvage

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P03958

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Adenosine deaminase (EC:3.5.4.45 Publications)
    Alternative name(s):
    Adenosine aminohydrolase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Ada
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:87916 Ada

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi217E → D: Reduces catalytic activity 700-fold. No effect on affinity for adenosine. 1 Publication1
    Mutagenesisi217E → G: Reduces catalytic activity 3200-fold. No effect on affinity for adenosine. 1 Publication1
    Mutagenesisi217E → Q: Reduces catalytic activity 4800-fold, and slighly increases affinity for substrate. 1 Publication1
    Mutagenesisi217E → S: Loss of activity. 1 Publication1
    Mutagenesisi238H → A: Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold. 1 Publication1
    Mutagenesisi238H → E: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi238H → R: Reduces enzyme activity 1500-fold. No effect on affinity for adenosine. 1 Publication1
    Mutagenesisi295D → E: No effect on affinity for adenosine. Reduces enzyme activity 2750-fold. 1 Publication1
    Mutagenesisi296D → A: Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold. 1 Publication1
    Mutagenesisi296D → N: Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3206

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001943532 – 352Adenosine deaminaseAdd BLAST351

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
    Modified residuei54N6-acetyllysineBy similarity1
    Modified residuei232N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P03958

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P03958

    PeptideAtlas

    More...
    PeptideAtlasi
    P03958

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P03958

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    P03958

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P03958

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P03958

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Detected in brain neurons in the median emninence (at protein level) (PubMed:8783262). Expressed in secondary deciduum (at protein level) (PubMed:9272950). Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues.2 Publications

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expressed in trophoblast at 7.5 dpc and 9.5 dpc.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000017697 Expressed in 202 organ(s), highest expression level in esophagus

    CleanEx database of gene expression profiles

    More...
    CleanExi
    MM_ADA

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P03958 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P03958 MM

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with DPP4 (via extracellular domain). Interacts with PLG (via Kringle 4 domain); the interaction stimulates PLG activation when in complex with DPP4.By similarity

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P03958, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P03958

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000017841

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P03958

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1352
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB 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[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P03958

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P03958

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P03958

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1097 Eukaryota
    COG1816 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153501

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000218816

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG001718

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P03958

    KEGG Orthology (KO)

    More...
    KOi
    K01488

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QWCGADR

    Database of Orthologous Groups

    More...
    OrthoDBi
    1045809at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P03958

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF314270

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01320 ADA, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00540 A_deaminase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006650 A/AMP_deam_AS
    IPR001365 A/AMP_deaminase_dom
    IPR028893 A_deaminase
    IPR006330 Ado/ade_deaminase
    IPR032466 Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00962 A_deaminase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51556 SSF51556, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01430 aden_deam, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00485 A_DEAMINASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE53A8A1FABA148CD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti141E → R in AAB07142 (PubMed:2387582).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS17015.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A01010 DUMSA

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001258981.1, NM_001272052.1
    NP_031424.1, NM_007398.4

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Mm.388

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    11486

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:11486

    UCSC genome browser

    More...
    UCSCi
    uc008ntl.2 mouse

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    PDB 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
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP03958, 2 interactors
    MINTiP03958
    STRINGi10090.ENSMUSP00000017841

    Chemistry databases

    BindingDBiP03958
    ChEMBLiCHEMBL3206

    PTM databases

    iPTMnetiP03958
    PhosphoSitePlusiP03958

    2D gel databases

    REPRODUCTION-2DPAGEiP03958

    Proteomic databases

    EPDiP03958
    PaxDbiP03958
    PeptideAtlasiP03958
    PRIDEiP03958

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697
    GeneIDi11486
    KEGGimmu:11486
    UCSCiuc008ntl.2 mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    100
    MGIiMGI:87916 Ada

    Phylogenomic databases

    eggNOGiKOG1097 Eukaryota
    COG1816 LUCA
    GeneTreeiENSGT00940000153501
    HOGENOMiHOG000218816
    HOVERGENiHBG001718
    InParanoidiP03958
    KOiK01488
    OMAiQWCGADR
    OrthoDBi1045809at2759
    PhylomeDBiP03958
    TreeFamiTF314270

    Enzyme and pathway databases

    BRENDAi3.5.4.4 3474
    ReactomeiR-MMU-74217 Purine salvage
    SABIO-RKiP03958

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    Ada mouse
    EvolutionaryTraceiP03958

    Protein Ontology

    More...
    PROi
    PR:P03958

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000017697 Expressed in 202 organ(s), highest expression level in esophagus
    CleanExiMM_ADA
    ExpressionAtlasiP03958 baseline and differential
    GenevisibleiP03958 MM

    Family and domain databases

    CDDicd01320 ADA, 1 hit
    HAMAPiMF_00540 A_deaminase, 1 hit
    InterProiView protein in InterPro
    IPR006650 A/AMP_deam_AS
    IPR001365 A/AMP_deaminase_dom
    IPR028893 A_deaminase
    IPR006330 Ado/ade_deaminase
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF00962 A_deaminase, 1 hit
    SUPFAMiSSF51556 SSF51556, 1 hit
    TIGRFAMsiTIGR01430 aden_deam, 1 hit
    PROSITEiView protein in PROSITE
    PS00485 A_DEAMINASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiADA_MOUSE
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03958
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 186 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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