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Entry version 65 (16 Oct 2019)
Sequence version 1 (16 Nov 2011)
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Protein

Aldehyde oxidase 3

Gene

Aox3

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

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor.4 Publications

Miscellaneous

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164).1 Publication

<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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by potassium cyanide, menadione, benzamidine, raloxifene and norharmane.2 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

kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) for phthalazine oxidation, 41.9 min(-1) for benzaldehyde oxidation, 14.7 min(-1) for N1-methylnicotinamide oxidation and 51.7 min(-1) for phenanthridine oxidation (PubMed:23019336).3 Publications
  1. KM=2.3 µM for phthalazine3 Publications
  2. KM=1.4 µM for phthalazine (at 37 degrees Celsius and pH 8)3 Publications
  3. KM=2.5 µM for benzaldehyde (at 37 degrees Celsius and pH 8)3 Publications
  4. KM=128.5 µM for N1-methylnicotinamide (at 37 degrees Celsius and pH 8)3 Publications
  5. KM=32.3 µM for phenanthridine (at 37 degrees Celsius and pH 8)3 Publications
  6. KM=13 µM for benzaldehyde (at 37 degrees Celsius and pH 7.4)3 Publications
  7. KM=29 µM for butyraldehyde (at 37 degrees Celsius and pH 8)3 Publications
  8. KM=173 µM for 2-OH-pyrimidine (at 37 degrees Celsius and pH 8)3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi47Iron-sulfur 1 (2Fe-2S)1 Publication1
    Metal bindingi52Iron-sulfur 1 (2Fe-2S)1 Publication1
    Metal bindingi55Iron-sulfur 1 (2Fe-2S)1 Publication1
    Metal bindingi77Iron-sulfur 1 (2Fe-2S)1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei116Molybdopterin1 Publication1
    Metal bindingi117Iron-sulfur 2 (2Fe-2S)1 Publication1
    Metal bindingi120Iron-sulfur 2 (2Fe-2S)1 Publication1
    Metal bindingi152Iron-sulfur 2 (2Fe-2S)1 Publication1
    Metal bindingi154Iron-sulfur 2 (2Fe-2S)1 Publication1
    Binding sitei354FAD1 Publication1
    Binding sitei358FAD1 Publication1
    Binding sitei367FAD1 Publication1
    Binding sitei411FAD; via amide nitrogen1 Publication1
    Binding sitei802Molybdopterin; via amide nitrogen1 Publication1
    Binding sitei1043Molybdopterin; via amide nitrogen1 Publication1
    Binding sitei1199Molybdopterin1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei1266Proton acceptor; for azaheterocycle hydroxylase activity1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi264 – 271FAD1 Publication8

    <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

    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 functionOxidoreductase
    Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.3.1 3474

    <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:
    Aldehyde oxidase 3 (EC:1.2.3.1)
    Alternative name(s):
    Aldehyde oxidase homolog 1
    Azaheterocycle hydroxylase 3 (EC:1.17.3.-)
    <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:Aox3
    Synonyms:Aoh1
    <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 1

    Organism-specific databases

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

    More...
    MGIi
    MGI:1918974 Aox3

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <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

    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>Mutagenesisi807A → V: No effect on kinetic constants with smaller substrates like benzaldehyde or phthalazine. Decreases substrate affinity and slightly increases catalytic efficiency for bulkier substrates like phenanthridine. 1 Publication1
    Mutagenesisi885Y → M: Slightly decreases substrate affinity but no effect on activity with smaller substrates like benzaldehyde or phthalazine. Increases catalytic efficiency with bulkier substrates like phenanthridine or more charged substrates like N1-methylnicotinamide. 1 Publication1
    Mutagenesisi889K → H: No effect on substrate affinity but decreases catalytic efficiency for smaller substrates like benzaldehyde or phthalazine. Increases substrate affinity and activity for bulkier substrates like phenanthridine. 1 Publication1
    Mutagenesisi1266E → Q: Loss of activity with different N-heterocyclic compounds as substrates. 60% reduction of activity with benzaldehyde. 1 Publication1

    <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 ‘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_00004252471 – 1335Aldehyde oxidase 3Add BLAST1335

    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 residuei320PhosphoserineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    G3X982

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    G3X982

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

    More...
    PaxDbi
    G3X982

    PeptideAtlas

    More...
    PeptideAtlasi
    G3X982

    PRoteomics IDEntifications database

    More...
    PRIDEi
    G3X982

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    G3X982

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

    More...
    PhosphoSitePlusi
    G3X982

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    G3X982

    <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

    Highly expressed in liver (at protein level). In liver, the expression is greater in males than females.3 Publications

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by testosterone.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000064294 Expressed in 81 organ(s), highest expression level in left lobe of liver

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    G3X982 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    G3X982 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

    Homodimer.

    1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000049391

    <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

    11335
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    G3X982

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 952Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
    Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

    <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

    Belongs to the xanthine dehydrogenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IV7B Eukaryota
    KOG0430 Eukaryota
    COG4630 LUCA
    COG4631 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00950000183114

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    G3X982

    KEGG Orthology (KO)

    More...
    KOi
    K00157

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GKRHGFH

    Database of Orthologous Groups

    More...
    OrthoDBi
    48717at2759

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF353036

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002888 2Fe-2S-bd
    IPR036884 2Fe-2S-bd_dom_sf
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR000674 Ald_Oxase/Xan_DH_a/b
    IPR036856 Ald_Oxase/Xan_DH_a/b_sf
    IPR016208 Ald_Oxase/xanthine_DH
    IPR014313 Aldehyde_oxidase
    IPR008274 AldOxase/xan_DH_Mopterin-bd
    IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
    IPR005107 CO_DH_flav_C
    IPR036683 CO_DH_flav_C_dom_sf
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR002346 Mopterin_DH_FAD-bd

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01315 Ald_Xan_dh_C, 1 hit
    PF02738 Ald_Xan_dh_C2, 1 hit
    PF03450 CO_deh_flav_C, 1 hit
    PF00941 FAD_binding_5, 1 hit
    PF00111 Fer2, 1 hit
    PF01799 Fer2_2, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000127 Xanthine_DH, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01008 Ald_Xan_dh_C, 1 hit
    SM01092 CO_deh_flav_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47741 SSF47741, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF54665 SSF54665, 1 hit
    SSF55447 SSF55447, 1 hit
    SSF56003 SSF56003, 1 hit
    SSF56176 SSF56176, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02969 mam_aldehyde_ox, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51387 FAD_PCMH, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <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.

    This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    G3X982-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSPSKESDEL IFFVNGKKVT ERNADPEVNL LFYLRKVIRL TGTKYGCGGG
    60 70 80 90 100
    DCGACTVMIS RYDPISKRIS HFSATACLVP ICSLHGAAVT TVEGIGSTKT
    110 120 130 140 150
    RIHPVQERIA KGHGTQCGFC TPGMVMSIYT LLRNHPEPST EQIMETLGGN
    160 170 180 190 200
    LCRCTGYRPI VESAKSFCPS STCCQMNGEG KCCLDEEKNE PERKNSVCTK
    210 220 230 240 250
    LYEKKEFQPL DPTQELIFPP ELMRMAEESQ NTVLTFRGER TTWIAPGTLN
    260 270 280 290 300
    DLLELKMKHP SAPLVIGNTY LGLHMKFTDV SYPIIISPAR ILELFVVTNT
    310 320 330 340 350
    KQGLTLGAGL SLTQVKNVLS DVVSRLPKEK TQIYCALLKQ LKTLAGQQIR
    360 370 380 390 400
    NVASLGGHII SRLPTSDLNP ILGIGNCILN VASTEGIQQI PLNDHFLAGV
    410 420 430 440 450
    PDAILKPEQV LISVFVPRSS KWEFVSAFRQ APRQQNAFAT VNAGMKVVFK
    460 470 480 490 500
    EDTNTITDLG ILYGGIGATV ISADKSCRQL IGRCWDEEML DDAGKMICEE
    510 520 530 540 550
    VSLLMAAPGG MEEYRKTLAI SFLFMFYLDV LKQLKTRDPH KYPDISQKLL
    560 570 580 590 600
    HILEDFPLTM PYGMQSFQDV DFQQPLQDPI GRPIMHQSGI KHATGEAVFC
    610 620 630 640 650
    DDMSVLPGEL FLAVVTSSKS HAKIISLDAS EALASLGVVD VVTARDVPGD
    660 670 680 690 700
    NGREEESLYA QDEVICVGQI VCAVAADSYA HAQQAAKKVK IVYQDIEPMI
    710 720 730 740 750
    VTVQDALQYE SFIGPERKLE QGNVEEAFQC ADQILEGEVH LGGQEHFYME
    760 770 780 790 800
    TQSVRVVPKG EDKEMDIYVS SQDAAFTQEM VARTLGIPKN RINCHVKRVG
    810 820 830 840 850
    GAFGGKASKP GLLASVAAVA AQKTGRPIRF ILERRDDMLI TGGRHPLLGK
    860 870 880 890 900
    YKIGFMNNGK IKAADIQLYI NGGCTPDDSE LVIEYALLKL ENAYKIPNLR
    910 920 930 940 950
    VRGRVCKTNL PSNTAFRGFG FPQGAFVTET CMSAVAAKCR LPPEKVRELN
    960 970 980 990 1000
    MYRTIDRTIH NQEFDPTNLL QCWEACVENS SYYNRKKAVD EFNQQRFWKK
    1010 1020 1030 1040 1050
    RGIAIIPMKF SVGFPKTFYY QAAALVQIYT DGSVLVAHGG VELGQGINTK
    1060 1070 1080 1090 1100
    MIQVASRELK IPMSYIHLDE MSTVTVPNTV TTGASTGADV NGRAVQNACQ
    1110 1120 1130 1140 1150
    ILMKRLEPII KQNPSGTWEE WVKEAFVQSI SLSATGYFRG YQADMDWEKG
    1160 1170 1180 1190 1200
    EGDIFPYFVF GAACSEVEID CLTGAHKNIR TDIVMDGSFS INPAVDIGQI
    1210 1220 1230 1240 1250
    EGAFVQGLGL YTLEELKYSP EGVLYTRGPH QYKIASVTDI PEEFHVSLLT
    1260 1270 1280 1290 1300
    PTPNPKAIYS SKGLGEAGTF LGCSVFFAIA AAVAAAREER GLSPIWAINS
    1310 1320 1330
    PATAEVIRMA CEDQFTNLVP QTDSKCCKPW SIPVA
    Length:1,335
    Mass (Da):146,902
    Last modified:November 16, 2011 - v1
    <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:i29683B03DD3E75E9
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A087WQC8A0A087WQC8_MOUSE
    Aldehyde oxidase 3
    Aox3
    270Annotation score:

    Annotation score:1 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 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 conflicti308A → T in AAL36596 (PubMed:11562361).Curated1
    Sequence conflicti541K → R in AAI38877 (PubMed:15489334).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

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    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF322178
    , AF322144, AF322145, AF322146, AF322147, AF322148, AF322149, AF322150, AF322151, AF322152, AF322153, AF322154, AF322155, AF322156, AF322157, AF322158, AF322159, AF322160, AF322161, AF322162, AF322163, AF322164, AF322165, AF322166, AF322167, AF322168, AF322169, AF322170, AF322171, AF322172, AF322173, AF322174, AF322175, AF322176, AF322177 Genomic DNA Translation: AAL36596.1
    AC025116 Genomic DNA No translation available.
    CH466548 Genomic DNA Translation: EDL00068.1
    BC138876 mRNA Translation: AAI38877.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS14969.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_076106.2, NM_023617.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000040999; ENSMUSP00000049391; ENSMUSG00000064294

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    71724

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:71724

    UCSC genome browser

    More...
    UCSCi
    uc007bbm.1 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
    AF322178
    , AF322144, AF322145, AF322146, AF322147, AF322148, AF322149, AF322150, AF322151, AF322152, AF322153, AF322154, AF322155, AF322156, AF322157, AF322158, AF322159, AF322160, AF322161, AF322162, AF322163, AF322164, AF322165, AF322166, AF322167, AF322168, AF322169, AF322170, AF322171, AF322172, AF322173, AF322174, AF322175, AF322176, AF322177 Genomic DNA Translation: AAL36596.1
    AC025116 Genomic DNA No translation available.
    CH466548 Genomic DNA Translation: EDL00068.1
    BC138876 mRNA Translation: AAI38877.1
    CCDSiCCDS14969.1
    RefSeqiNP_076106.2, NM_023617.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

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    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZYVX-ray2.54A/B/C/D1-1335[»]
    SMRiG3X982
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000049391

    PTM databases

    iPTMnetiG3X982
    PhosphoSitePlusiG3X982
    SwissPalmiG3X982

    Proteomic databases

    jPOSTiG3X982
    MaxQBiG3X982
    PaxDbiG3X982
    PeptideAtlasiG3X982
    PRIDEiG3X982

    Genome annotation databases

    EnsembliENSMUST00000040999; ENSMUSP00000049391; ENSMUSG00000064294
    GeneIDi71724
    KEGGimmu:71724
    UCSCiuc007bbm.1 mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    71724
    MGIiMGI:1918974 Aox3

    Phylogenomic databases

    eggNOGiENOG410IV7B Eukaryota
    KOG0430 Eukaryota
    COG4630 LUCA
    COG4631 LUCA
    GeneTreeiENSGT00950000183114
    InParanoidiG3X982
    KOiK00157
    OMAiGKRHGFH
    OrthoDBi48717at2759
    TreeFamiTF353036

    Enzyme and pathway databases

    BRENDAi1.2.3.1 3474

    Miscellaneous databases

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

    More...
    ChiTaRSi
    Aox3 mouse

    Protein Ontology

    More...
    PROi
    PR:G3X982

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000064294 Expressed in 81 organ(s), highest expression level in left lobe of liver
    ExpressionAtlasiG3X982 baseline and differential
    GenevisibleiG3X982 MM

    Family and domain databases

    InterProiView protein in InterPro
    IPR002888 2Fe-2S-bd
    IPR036884 2Fe-2S-bd_dom_sf
    IPR036010 2Fe-2S_ferredoxin-like_sf
    IPR001041 2Fe-2S_ferredoxin-type
    IPR006058 2Fe2S_fd_BS
    IPR000674 Ald_Oxase/Xan_DH_a/b
    IPR036856 Ald_Oxase/Xan_DH_a/b_sf
    IPR016208 Ald_Oxase/xanthine_DH
    IPR014313 Aldehyde_oxidase
    IPR008274 AldOxase/xan_DH_Mopterin-bd
    IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
    IPR005107 CO_DH_flav_C
    IPR036683 CO_DH_flav_C_dom_sf
    IPR016166 FAD-bd_PCMH
    IPR036318 FAD-bd_PCMH-like_sf
    IPR002346 Mopterin_DH_FAD-bd
    PfamiView protein in Pfam
    PF01315 Ald_Xan_dh_C, 1 hit
    PF02738 Ald_Xan_dh_C2, 1 hit
    PF03450 CO_deh_flav_C, 1 hit
    PF00941 FAD_binding_5, 1 hit
    PF00111 Fer2, 1 hit
    PF01799 Fer2_2, 1 hit
    PIRSFiPIRSF000127 Xanthine_DH, 1 hit
    SMARTiView protein in SMART
    SM01008 Ald_Xan_dh_C, 1 hit
    SM01092 CO_deh_flav_C, 1 hit
    SUPFAMiSSF47741 SSF47741, 1 hit
    SSF54292 SSF54292, 1 hit
    SSF54665 SSF54665, 1 hit
    SSF55447 SSF55447, 1 hit
    SSF56003 SSF56003, 1 hit
    SSF56176 SSF56176, 1 hit
    TIGRFAMsiTIGR02969 mam_aldehyde_ox, 1 hit
    PROSITEiView protein in PROSITE
    PS00197 2FE2S_FER_1, 1 hit
    PS51085 2FE2S_FER_2, 1 hit
    PS51387 FAD_PCMH, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 nameiAOXC_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: G3X982
    Secondary accession number(s): B2RSI5, Q8VI15
    <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: February 19, 2014
    Last sequence update: November 16, 2011
    Last modified: October 16, 2019
    This is version 65 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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