MIOX_RAT
ID MIOX_RAT Reviewed; 285 AA.
AC Q9QXN4; Q5S8C8; Q68G06; Q99PN7;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inositol oxygenase;
DE EC=1.13.99.1;
DE AltName: Full=Aldehyde reductase-like 6;
DE AltName: Full=Kidney-specific protein 32;
DE AltName: Full=Myo-inositol oxygenase;
DE Short=MI oxygenase;
DE AltName: Full=Renal-specific oxidoreductase;
GN Name=Miox; Synonyms=Aldrl6, Ksp32, Rsor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
RA Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L., Spurr N.,
RA Sims M., Halsey W., Van Horn S., Mao J., Sathe G., Brooks D.;
RT "Identification of a novel kidney specific gene, KSP32, that is down
RT regulated in acute ischemic renal failure.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Long Evans; 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
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.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000305}.
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DR EMBL; AF197128; AAF25203.1; -; mRNA.
DR EMBL; AF230096; AAK00767.1; -; mRNA.
DR EMBL; AY738259; AAV65817.1; -; mRNA.
DR EMBL; BC078840; AAH78840.1; -; mRNA.
DR RefSeq; NP_665714.2; NM_145771.2.
DR AlphaFoldDB; Q9QXN4; -.
DR SMR; Q9QXN4; -.
DR STRING; 10116.ENSRNOP00000011941; -.
DR iPTMnet; Q9QXN4; -.
DR PhosphoSitePlus; Q9QXN4; -.
DR PaxDb; Q9QXN4; -.
DR PRIDE; Q9QXN4; -.
DR DNASU; 252899; -.
DR Ensembl; ENSRNOT00000011941; ENSRNOP00000011941; ENSRNOG00000008694.
DR GeneID; 252899; -.
DR KEGG; rno:252899; -.
DR CTD; 55586; -.
DR RGD; 628739; Miox.
DR eggNOG; KOG1573; Eukaryota.
DR GeneTree; ENSGT00390000016211; -.
DR HOGENOM; CLU_050259_1_0_1; -.
DR InParanoid; Q9QXN4; -.
DR OrthoDB; 1436589at2759; -.
DR PhylomeDB; Q9QXN4; -.
DR TreeFam; TF300089; -.
DR BRENDA; 1.13.99.1; 5301.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; Q9QXN4; -.
DR UniPathway; UPA00111; UER00527.
DR PRO; PR:Q9QXN4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Genevisible; Q9QXN4; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS: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; IDA:RGD.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; ISO:RGD.
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 Cytoplasm; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Inositol oxygenase"
FT /id="PRO_0000079152"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220..221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 4..5
FT /note="DL -> TV (in Ref. 2; AAK00767)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="M -> V (in Ref. 2; AAK00767)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..26
FT /note="SKG -> DKA (in Ref. 2; AAK00767)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="M -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="M -> V (in Ref. 3; AAV65817)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..61
FT /note="RKRI -> SKHA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> T (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 33185 MW; F34A26521979AE89 CRC64;
MKVDLGPDPS LVYRPDVDPE MAKSKGSFRN YTSGPLLDRV FTTYKLMHTH QTVDFVMRKR
IQFGSFSYKK MTVMEAVDML DDLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
LLHDLGKILA LWGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ
PHCGLENVLM SWGHDEYLYQ MMKFNKFSLP SEAFYMVRFH SFYPWHTGGD YRQLCSQQDL
DMLPWVQEFN KFDLYTKCPD LPEVKSLRPY YQGLIDKYCP GILSW
