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Inositol oxygenase (EC 1.13.99.1) (Aldehyde reductase-like 6) (Kidney-specific protein 32) (Myo-inositol oxygenase) (MI oxygenase) (Renal-specific oxidoreductase)

 MIOX_HUMAN              Reviewed;         285 AA.
Q9UGB7; Q05DJ6; Q5S8C9; Q9BZZ1; Q9UHB8;
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 145.
RecName: Full=Inositol oxygenase;
EC=1.13.99.1;
AltName: Full=Aldehyde reductase-like 6;
AltName: Full=Kidney-specific protein 32;
AltName: Full=Myo-inositol oxygenase;
Short=MI oxygenase;
AltName: Full=Renal-specific oxidoreductase;
Name=MIOX; Synonyms=ALDRL6, KSP32, RSOR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Parthasarathy L., Seelan R., Parthasarathy R.;
"Cloning and expression of human myo-inositol oxygenase (MIOX).";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L.,
Spurr N., Sims M., Halsey W., Van Horn S., Mao J., Sathe G.,
Brooks D.;
"Identification of a novel kidney specific gene, KSP32, that is down
regulated in acute ischemic renal failure.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=10944187; DOI=10.1073/pnas.160266197;
Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K.,
Kanwar Y.S.;
"Identification of a renal-specific oxido-reductase in newborn
diabetic mice.";
Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15504367; DOI=10.1016/j.bbrc.2004.09.209;
Arner R.J., Prabhu K.S., Reddy C.C.;
"Molecular cloning, expression, and characterization of myo-inositol
oxygenase from mouse, rat, and human kidney.";
Biochem. Biophys. Res. Commun. 324:1386-1392(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285 IN COMPLEX WITH IRON
AND MYO-INOSOSE-1, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF
LYS-127.
PubMed=18364358; DOI=10.1074/jbc.M800348200;
Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M.,
Graslund S., Graslund A., Hallberg B.M.;
"Structural and biophysical characterization of human myo-inositol
oxygenase.";
J. Biol. Chem. 283:15209-15216(2008).
-!- CATALYTIC ACTIVITY: Myo-inositol + O(2) = D-glucuronate + H(2)O.
{ECO:0000269|PubMed:18364358}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:18364358};
Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:18364358};
-!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
glucuronate; D-glucuronate from myo-inositol: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UGB7-1; Sequence=Displayed;
Name=2;
IsoId=Q9UGB7-2; Sequence=VSP_041667, VSP_041668;
-!- TISSUE SPECIFICITY: Kidney specific.
-!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
{ECO:0000305}.
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EMBL; AY064416; AAL47192.1; -; mRNA.
EMBL; AF230095; AAK00766.1; -; mRNA.
EMBL; AF197129; AAF25204.1; -; mRNA.
EMBL; AY738258; AAV65816.1; -; mRNA.
EMBL; AK000576; BAA91266.1; -; mRNA.
EMBL; CR456478; CAG30364.1; -; mRNA.
EMBL; AL096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471138; EAW73547.1; -; Genomic_DNA.
EMBL; BC012025; AAH12025.1; -; mRNA.
EMBL; BC073848; AAH73848.1; -; mRNA.
CCDS; CCDS14092.1; -. [Q9UGB7-1]
RefSeq; NP_060054.4; NM_017584.5. [Q9UGB7-1]
UniGene; Hs.129227; -.
PDB; 2IBN; X-ray; 1.50 A; A/B=38-285.
PDBsum; 2IBN; -.
ProteinModelPortal; Q9UGB7; -.
SMR; Q9UGB7; -.
BioGrid; 120733; 2.
STRING; 9606.ENSP00000216075; -.
iPTMnet; Q9UGB7; -.
PhosphoSitePlus; Q9UGB7; -.
BioMuta; MIOX; -.
PaxDb; Q9UGB7; -.
PeptideAtlas; Q9UGB7; -.
PRIDE; Q9UGB7; -.
ProteomicsDB; 84204; -.
ProteomicsDB; 84205; -. [Q9UGB7-2]
TopDownProteomics; Q9UGB7-1; -. [Q9UGB7-1]
DNASU; 55586; -.
Ensembl; ENST00000216075; ENSP00000216075; ENSG00000100253. [Q9UGB7-1]
Ensembl; ENST00000395733; ENSP00000379082; ENSG00000100253. [Q9UGB7-2]
GeneID; 55586; -.
KEGG; hsa:55586; -.
UCSC; uc003bll.2; human. [Q9UGB7-1]
CTD; 55586; -.
DisGeNET; 55586; -.
EuPathDB; HostDB:ENSG00000100253.12; -.
GeneCards; MIOX; -.
HGNC; HGNC:14522; MIOX.
HPA; HPA039451; -.
HPA; HPA039562; -.
MIM; 606774; gene.
neXtProt; NX_Q9UGB7; -.
OpenTargets; ENSG00000100253; -.
PharmGKB; PA24716; -.
eggNOG; KOG1573; Eukaryota.
eggNOG; ENOG410XQ4J; LUCA.
GeneTree; ENSGT00390000016211; -.
HOGENOM; HOG000163182; -.
HOVERGEN; HBG039556; -.
InParanoid; Q9UGB7; -.
KO; K00469; -.
OMA; HEKQTVA; -.
OrthoDB; EOG091G0FIX; -.
PhylomeDB; Q9UGB7; -.
TreeFam; TF300089; -.
BRENDA; 1.13.99.1; 2681.
Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RK; Q9UGB7; -.
UniPathway; UPA00111; UER00527.
ChiTaRS; MIOX; human.
EvolutionaryTrace; Q9UGB7; -.
GenomeRNAi; 55586; -.
PRO; PR:Q9UGB7; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100253; -.
CleanEx; HS_MIOX; -.
ExpressionAtlas; Q9UGB7; baseline and differential.
Genevisible; Q9UGB7; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016234; C:inclusion body; ISS:UniProtKB.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
GO; GO:0050113; F:inositol oxygenase activity; IDA:UniProtKB.
GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:Ensembl.
GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; ISS:UniProtKB.
GO; GO:0019310; P:inositol catabolic process; IDA:UniProtKB.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
InterPro; IPR007828; Inositol_oxygenase.
PANTHER; PTHR12588; PTHR12588; 1.
Pfam; PF05153; MIOX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
Reference proteome.
CHAIN 1 285 Inositol oxygenase.
/FTId=PRO_0000079148.
REGION 85 87 Substrate binding.
REGION 141 142 Substrate binding.
REGION 220 221 Substrate binding.
METAL 98 98 Iron 1. {ECO:0000269|PubMed:18364358}.
METAL 123 123 Iron 1. {ECO:0000269|PubMed:18364358}.
METAL 124 124 Iron 1. {ECO:0000269|PubMed:18364358}.
METAL 124 124 Iron 2. {ECO:0000269|PubMed:18364358}.
METAL 194 194 Iron 2. {ECO:0000269|PubMed:18364358}.
METAL 220 220 Iron 2. {ECO:0000269|PubMed:18364358}.
METAL 253 253 Iron 1. {ECO:0000269|PubMed:18364358}.
BINDING 29 29 Substrate. {ECO:0000250}.
BINDING 127 127 Substrate.
MOD_RES 33 33 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXN4}.
VAR_SEQ 114 231 DWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASV
VFCDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHD
EYMYQVMKFNKFSLPPEAFYMIRFHSFYPWHTGRDY -> V
PNLPCPSPSQTGSTSSGSCTTWGRSWPCSGSPSGLSSATPS
PSDAVRRPPWFSATPPSRTTLTSRILDTAQSSGCISPTVGS
TGSSCPGAMMQVRPLHQVPGPAGRGQAAALLPGAH (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041667.
VAR_SEQ 232 285 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041668.
MUTAGEN 127 127 K->S: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:18364358}.
CONFLICT 4 4 T -> D (in Ref. 3; AAF25204).
{ECO:0000305}.
CONFLICT 199 199 Y -> F (in Ref. 2; AAK00766).
{ECO:0000305}.
CONFLICT 219 221 FHS -> VHF (in Ref. 2; AAK00766).
{ECO:0000305}.
CONFLICT 282 282 I -> T (in Ref. 3; AAF25204).
{ECO:0000305}.
HELIX 38 50 {ECO:0000244|PDB:2IBN}.
HELIX 53 63 {ECO:0000244|PDB:2IBN}.
STRAND 68 71 {ECO:0000244|PDB:2IBN}.
HELIX 73 79 {ECO:0000244|PDB:2IBN}.
HELIX 80 82 {ECO:0000244|PDB:2IBN}.
HELIX 95 109 {ECO:0000244|PDB:2IBN}.
HELIX 114 122 {ECO:0000244|PDB:2IBN}.
HELIX 125 127 {ECO:0000244|PDB:2IBN}.
HELIX 128 131 {ECO:0000244|PDB:2IBN}.
HELIX 136 138 {ECO:0000244|PDB:2IBN}.
STRAND 145 148 {ECO:0000244|PDB:2IBN}.
HELIX 157 160 {ECO:0000244|PDB:2IBN}.
HELIX 165 168 {ECO:0000244|PDB:2IBN}.
TURN 170 172 {ECO:0000244|PDB:2IBN}.
STRAND 173 176 {ECO:0000244|PDB:2IBN}.
HELIX 185 187 {ECO:0000244|PDB:2IBN}.
HELIX 194 205 {ECO:0000244|PDB:2IBN}.
HELIX 211 219 {ECO:0000244|PDB:2IBN}.
HELIX 223 226 {ECO:0000244|PDB:2IBN}.
TURN 232 234 {ECO:0000244|PDB:2IBN}.
HELIX 237 253 {ECO:0000244|PDB:2IBN}.
HELIX 264 278 {ECO:0000244|PDB:2IBN}.
STRAND 283 285 {ECO:0000244|PDB:2IBN}.
SEQUENCE 285 AA; 33010 MW; ED70B197FF267B2B CRC64;
MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH
AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ
PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL
AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW


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