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Q9QXN5

- MIOX_MOUSE

UniProt

Q9QXN5 - MIOX_MOUSE

Protein

Inositol oxygenase

Gene

Miox

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (08 Nov 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Myo-inositol + O2 = D-glucuronate + H2O.

    Cofactori

    Binds 2 iron ions per subunit.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei29 – 291Substrate
    Metal bindingi98 – 981Iron 12 Publications
    Metal bindingi123 – 1231Iron 12 Publications
    Metal bindingi124 – 1241Iron 12 Publications
    Metal bindingi124 – 1241Iron 22 Publications
    Binding sitei127 – 1271Substrate
    Metal bindingi194 – 1941Iron 22 Publications
    Metal bindingi220 – 2201Iron 22 Publications
    Metal bindingi253 – 2531Iron 12 Publications

    GO - Molecular functioni

    1. aldo-keto reductase (NADP) activity Source: UniProtKB
    2. ferric iron binding Source: UniProtKB
    3. inositol oxygenase activity Source: UniProtKB
    4. NADP binding Source: Ensembl
    5. oxidoreductase activity Source: MGI
    6. oxidoreductase activity, acting on NAD(P)H Source: UniProtKB
    7. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen Source: UniProtKB

    GO - Biological processi

    1. inositol catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.99.1. 3474.
    SABIO-RKQ9QXN5.
    UniPathwayiUPA00111; UER00527.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol oxygenase (EC:1.13.99.1)
    Alternative name(s):
    Aldehyde reductase-like 6
    Myo-inositol oxygenase
    Short name:
    MI oxygenase
    Renal-specific oxidoreductase
    Gene namesi
    Name:Miox
    Synonyms:Aldrl6, Rsor
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1891725. Miox.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. inclusion body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Inositol oxygenasePRO_0000079149Add
    BLAST

    Proteomic databases

    MaxQBiQ9QXN5.
    PaxDbiQ9QXN5.
    PRIDEiQ9QXN5.

    2D gel databases

    REPRODUCTION-2DPAGEQ9QXN5.

    PTM databases

    PhosphoSiteiQ9QXN5.

    Expressioni

    Tissue specificityi

    Kidney specific. Renal proximal tubules.1 Publication

    Gene expression databases

    BgeeiQ9QXN5.
    CleanExiMM_MIOX.
    GenevestigatoriQ9QXN5.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9QXN5. 1 interaction.
    MINTiMINT-4102022.

    Structurei

    Secondary structure

    1
    285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 333
    Helixi37 – 5014
    Helixi53 – 6311
    Helixi73 – 797
    Helixi80 – 823
    Helixi95 – 10915
    Helixi114 – 1229
    Helixi125 – 1328
    Helixi136 – 1383
    Beta strandi145 – 1484
    Turni155 – 1595
    Helixi165 – 1684
    Turni170 – 1723
    Beta strandi173 – 1764
    Helixi185 – 1873
    Helixi194 – 20411
    Helixi211 – 2199
    Helixi223 – 2264
    Turni232 – 2343
    Helixi237 – 25519
    Helixi264 – 27815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HUOX-ray2.00A1-285[»]
    3BXDX-ray2.00A1-285[»]
    ProteinModelPortaliQ9QXN5.
    SMRiQ9QXN5. Positions 28-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QXN5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 884Substrate binding
    Regioni141 – 1422Substrate binding
    Regioni220 – 2212Substrate binding

    Sequence similaritiesi

    Belongs to the myo-inositol oxygenase family.Curated

    Phylogenomic databases

    eggNOGiNOG135479.
    GeneTreeiENSGT00390000016211.
    HOGENOMiHOG000163182.
    HOVERGENiHBG039556.
    InParanoidiQ9QXN5.
    KOiK00469.
    OMAiNFYREQH.
    OrthoDBiEOG7DZ8KD.
    PhylomeDBiQ9QXN5.
    TreeFamiTF300089.

    Family and domain databases

    InterProiIPR018170. Aldo/ket_reductase_CS.
    IPR007828. Inositol_oxygenase.
    [Graphical view]
    PANTHERiPTHR12588. PTHR12588. 1 hit.
    PfamiPF05153. DUF706. 1 hit.
    [Graphical view]
    PROSITEiPS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QXN5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVDVGPDPS LVYRPDVDPE MAKSKDSFRN YTSGPLLDRV FTTYKLMHTH    50
    QTVDFVSRKR IQYGSFSYKK MTIMEAVGML DDLVDESDPD VDFPNSFHAF 100
    QTAEGIRKAH PDKDWFHLVG LLHDLGKIMA LWGEPQWAVV GDTFPVGCRP 150
    QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLENVLM SWGHDEYLYQ 200
    MMKFNKFSLP SEAFYMIRFH SFYPWHTGGD YRQLCSQQDL DMLPWVQEFN 250
    KFDLYTKCPD LPDVESLRPY YQGLIDKYCP GTLSW 285
    Length:285
    Mass (Da):33,164
    Last modified:November 8, 2005 - v2
    Checksum:iC6877BFF2B60D1A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651S → G in AAF25202. (PubMed:10944187)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197127 mRNA. Translation: AAF25202.1.
    AY738257 mRNA. Translation: AAV65815.1.
    BC013543 mRNA. Translation: AAH13543.1.
    CCDSiCCDS27745.1.
    RefSeqiNP_064361.2. NM_019977.2.
    UniGeneiMm.158200.

    Genome annotation databases

    EnsembliENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613.
    GeneIDi56727.
    KEGGimmu:56727.
    UCSCiuc007xgc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197127 mRNA. Translation: AAF25202.1 .
    AY738257 mRNA. Translation: AAV65815.1 .
    BC013543 mRNA. Translation: AAH13543.1 .
    CCDSi CCDS27745.1.
    RefSeqi NP_064361.2. NM_019977.2.
    UniGenei Mm.158200.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HUO X-ray 2.00 A 1-285 [» ]
    3BXD X-ray 2.00 A 1-285 [» ]
    ProteinModelPortali Q9QXN5.
    SMRi Q9QXN5. Positions 28-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QXN5. 1 interaction.
    MINTi MINT-4102022.

    PTM databases

    PhosphoSitei Q9QXN5.

    2D gel databases

    REPRODUCTION-2DPAGE Q9QXN5.

    Proteomic databases

    MaxQBi Q9QXN5.
    PaxDbi Q9QXN5.
    PRIDEi Q9QXN5.

    Protocols and materials databases

    DNASUi 56727.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023282 ; ENSMUSP00000023282 ; ENSMUSG00000022613 .
    GeneIDi 56727.
    KEGGi mmu:56727.
    UCSCi uc007xgc.1. mouse.

    Organism-specific databases

    CTDi 55586.
    MGIi MGI:1891725. Miox.

    Phylogenomic databases

    eggNOGi NOG135479.
    GeneTreei ENSGT00390000016211.
    HOGENOMi HOG000163182.
    HOVERGENi HBG039556.
    InParanoidi Q9QXN5.
    KOi K00469.
    OMAi NFYREQH.
    OrthoDBi EOG7DZ8KD.
    PhylomeDBi Q9QXN5.
    TreeFami TF300089.

    Enzyme and pathway databases

    UniPathwayi UPA00111 ; UER00527 .
    BRENDAi 1.13.99.1. 3474.
    SABIO-RK Q9QXN5.

    Miscellaneous databases

    EvolutionaryTracei Q9QXN5.
    NextBioi 313210.
    PROi Q9QXN5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QXN5.
    CleanExi MM_MIOX.
    Genevestigatori Q9QXN5.

    Family and domain databases

    InterProi IPR018170. Aldo/ket_reductase_CS.
    IPR007828. Inositol_oxygenase.
    [Graphical view ]
    PANTHERi PTHR12588. PTHR12588. 1 hit.
    Pfami PF05153. DUF706. 1 hit.
    [Graphical view ]
    PROSITEi PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a renal-specific oxido-reductase in newborn diabetic mice."
      Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., Kanwar Y.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Kidney.
    2. "Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney."
      Arner R.J., Prabhu K.S., Reddy C.C.
      Biochem. Biophys. Res. Commun. 324:1386-1392(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Kidney.
    3. "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: Kidney.
    4. "Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism."
      Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., Loomes K.M., Baker E.N.
      Proc. Natl. Acad. Sci. U.S.A. 103:15032-15037(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND MYO-INOSITOL, COFACTOR.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND MYO-INOSITOL, COFACTOR.

    Entry informationi

    Entry nameiMIOX_MOUSE
    AccessioniPrimary (citable) accession number: Q9QXN5
    Secondary accession number(s): Q5S8D0, Q91WQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3