MIOX_MOUSE
ID MIOX_MOUSE Reviewed; 285 AA.
AC Q9QXN5; Q5S8D0; Q91WQ8;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inositol oxygenase;
DE EC=1.13.99.1;
DE AltName: Full=Aldehyde reductase-like 6;
DE AltName: Full=Myo-inositol oxygenase;
DE Short=MI oxygenase;
DE AltName: Full=Renal-specific oxidoreductase;
GN Name=Miox; Synonyms=Aldrl6, Rsor;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10944187; DOI=10.1073/pnas.160266197;
RA Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K.,
RA Kanwar Y.S.;
RT "Identification of a renal-specific oxido-reductase in newborn diabetic
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=15504367; DOI=10.1016/j.bbrc.2004.09.209;
RA Arner R.J., Prabhu K.S., Reddy C.C.;
RT "Molecular cloning, expression, and characterization of myo-inositol
RT oxygenase from mouse, rat, and human kidney.";
RL Biochem. Biophys. Res. Commun. 324:1386-1392(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND
RP MYO-INOSITOL, AND COFACTOR.
RX PubMed=17012379; DOI=10.1073/pnas.0605143103;
RA Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., Loomes K.M.,
RA Baker E.N.;
RT "Crystal structure of a substrate complex of myo-inositol oxygenase, a di-
RT iron oxygenase with a key role in inositol metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15032-15037(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND
RP MYO-INOSITOL, AND COFACTOR.
RX PubMed=18364358; DOI=10.1074/jbc.m800348200;
RA Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M.,
RA Graslund S., Graslund A., Hallberg B.M.;
RT "Structural and biophysical characterization of human myo-inositol
RT oxygenase.";
RL J. Biol. Chem. 283:15209-15216(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol + O2 = D-glucuronate + H(+) + H2O;
CC Xref=Rhea:RHEA:23696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17268, ChEBI:CHEBI:58720;
CC EC=1.13.99.1;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:17012379, ECO:0000269|PubMed:18364358};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:17012379,
CC ECO:0000269|PubMed:18364358};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Kidney specific. Renal proximal tubules.
CC {ECO:0000269|PubMed:10944187}.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000305}.
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DR EMBL; AF197127; AAF25202.1; -; mRNA.
DR EMBL; AY738257; AAV65815.1; -; mRNA.
DR EMBL; BC013543; AAH13543.1; -; mRNA.
DR CCDS; CCDS27745.1; -.
DR RefSeq; NP_064361.2; NM_019977.2.
DR PDB; 2HUO; X-ray; 2.00 A; A=1-285.
DR PDB; 3BXD; X-ray; 2.00 A; A=1-285.
DR PDBsum; 2HUO; -.
DR PDBsum; 3BXD; -.
DR AlphaFoldDB; Q9QXN5; -.
DR SMR; Q9QXN5; -.
DR STRING; 10090.ENSMUSP00000023282; -.
DR iPTMnet; Q9QXN5; -.
DR PhosphoSitePlus; Q9QXN5; -.
DR REPRODUCTION-2DPAGE; Q9QXN5; -.
DR jPOST; Q9QXN5; -.
DR MaxQB; Q9QXN5; -.
DR PaxDb; Q9QXN5; -.
DR PeptideAtlas; Q9QXN5; -.
DR PRIDE; Q9QXN5; -.
DR ProteomicsDB; 295612; -.
DR Antibodypedia; 53923; 312 antibodies from 21 providers.
DR DNASU; 56727; -.
DR Ensembl; ENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613.
DR GeneID; 56727; -.
DR KEGG; mmu:56727; -.
DR UCSC; uc007xgc.1; mouse.
DR CTD; 55586; -.
DR MGI; MGI:1891725; Miox.
DR VEuPathDB; HostDB:ENSMUSG00000022613; -.
DR eggNOG; KOG1573; Eukaryota.
DR GeneTree; ENSGT00390000016211; -.
DR HOGENOM; CLU_050259_1_0_1; -.
DR InParanoid; Q9QXN5; -.
DR OMA; RYNTKYG; -.
DR OrthoDB; 1436589at2759; -.
DR PhylomeDB; Q9QXN5; -.
DR TreeFam; TF300089; -.
DR BRENDA; 1.13.99.1; 3474.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; Q9QXN5; -.
DR UniPathway; UPA00111; UER00527.
DR BioGRID-ORCS; 56727; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Miox; mouse.
DR EvolutionaryTrace; Q9QXN5; -.
DR PRO; PR:Q9QXN5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QXN5; protein.
DR Bgee; ENSMUSG00000022613; Expressed in right kidney and 54 other tissues.
DR ExpressionAtlas; Q9QXN5; baseline and differential.
DR Genevisible; Q9QXN5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR GO; GO:0050113; F:inositol oxygenase activity; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:MGI.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:UniProtKB.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; ISS:UniProtKB.
DR GO; GO:0019310; P:inositol catabolic process; ISS:UniProtKB.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR007828; Inositol_oxygenase.
DR PANTHER; PTHR12588; PTHR12588; 1.
DR Pfam; PF05153; MIOX; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..285
FT /note="Inositol oxygenase"
FT /id="PRO_0000079149"
FT BINDING 29
FT /ligand="substrate"
FT BINDING 85..88
FT /ligand="substrate"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 127
FT /ligand="substrate"
FT BINDING 141..142
FT /ligand="substrate"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 220..221
FT /ligand="substrate"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17012379,
FT ECO:0000269|PubMed:18364358"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN4"
FT CONFLICT 65
FT /note="S -> G (in Ref. 1; AAF25202)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2HUO"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2HUO"
FT TURN 155..159
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2HUO"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2HUO"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:2HUO"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:2HUO"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:2HUO"
SQ SEQUENCE 285 AA; 33164 MW; C6877BFF2B60D1A7 CRC64;
MKVDVGPDPS LVYRPDVDPE MAKSKDSFRN YTSGPLLDRV FTTYKLMHTH QTVDFVSRKR
IQYGSFSYKK MTIMEAVGML DDLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
LLHDLGKIMA LWGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ
PHCGLENVLM SWGHDEYLYQ MMKFNKFSLP SEAFYMIRFH SFYPWHTGGD YRQLCSQQDL
DMLPWVQEFN KFDLYTKCPD LPDVESLRPY YQGLIDKYCP GTLSW
