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UniProtKB/Swiss-Prot entry Q9UGB7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MIOX_HUMAN
Primary accession number Q9UGB7
Secondary accession numbers Q5S8C9 Q9BZZ1 Q9UHB8
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
Name and origin of the protein
Protein name Inositol oxygenase
Synonyms EC 1.13.99.1
Myo-inositol oxygenase
MI oxygenase
Aldehyde reductase-like 6
Renal-specific oxidoreductase
Kidney-specific protein 32
Gene name
Name: MIOX
Synonyms: ALDRL6, KSP32, RSOR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
TISSUE=Kidney;
DOI=10.1073/pnas.160266197; PubMed=10944187 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Kidney;
DOI=10.1016/j.bbrc.2004.09.209; PubMed=15504367 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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:RESEARCH84.1-RESEARCH84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285.
Structural genomics consortium (SGC);
"Terminal substrate binding to the myo-inositol oxygenase di-iron cluster.";
Submitted (OCT-2006) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY064416; AAL47192.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF230095; AAK00766.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF197129; AAF25204.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY738258; AAV65816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000576; BAA91266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456478; CAG30364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL096767; CAB63064.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073848; AAH73848.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060054.4; -.
UniGene Hs.129227
3D structure databases
PDB
2IBN; X-ray; 1.50 A; A/B=38-285.[ExPASy / RCSB / EBI]
PDBsum 2IBN; -.
ModBase Q9UGB7.
Organism-specific databases
H-InvDB HIX0023329; -.
HGNC HGNC:14522; MIOX.
GenAtlas MIOX.
MIM 606774; gene. [NCBI / EBI]
PharmGKB PA24716; -.
GeneCards Q9UGB7.
Gene expression databases
ArrayExpress Q9UGB7; -.
CleanEx HS_MIOX; -.
GermOnline ENSG00000100253; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0016234; Cellular component: inclusion body (inferred from sequence or structural similarity from UniProtKB).
GO:0004033; Molecular function: aldo-keto reductase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0016701; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen (inferred from sequence or structural similarity from UniProtKB).
GO:0019310; Biological process: inositol catabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007828; DUF706.
Graphical view of domain structure.
PANTHER PTHR12588; DUF706; 1.
Pfam PF05153; DUF706; 1.
Pfam graphical view of domain structure.
BLOCKS Q9UGB7.
Genome annotation databases
Ensembl ENSG00000100253; Homo sapiens. [Contig view]
GeneID 55586; -.
KEGG hsa:55586; -.
NMPDR fig|9606.3.peg.21978; -.
Phylogenomic databases
HOGENOM Q9UGB7; -.
HOVERGEN Q9UGB7; -.
Other
LinkHub Q9UGB7; -.
SOURCE MIOX; Homo sapiens.
ProtoNet Q9UGB7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   285  285     Inositol oxygenase. PRO_0000079148
METAL   98    98        Iron 1 (By similarity). 
METAL   123   123        Iron 1 (By similarity). 
METAL   124   124        Iron 1 (By similarity). 
METAL   124   124        Iron 2 (By similarity). 
METAL   194   194        Iron 2 (By similarity). 
METAL   220   220        Iron 2 (By similarity). 
METAL   253   253        Iron 1 (By similarity). 
CONFLICT   4     4        T -> D (in Ref. 3; AAF25204). 
CONFLICT   199   199        Y -> F (in Ref. 2; AAK00766). 
CONFLICT   219   221        FHS -> VHF (in Ref. 2; AAK00766). 
CONFLICT   282   282        I -> T (in Ref. 3; AAF25204). 
HELIX   38    50  13      
HELIX   53    63  11      
STRAND   68    71  4      
HELIX   73    79  7      
HELIX   80    82  3      
HELIX   95   109  15      
HELIX   114   122  9      
HELIX   125   127  3      
HELIX   128   131  4      
HELIX   136   138  3      
STRAND   145   148  4      
HELIX   157   160  4      
HELIX   165   168  4      
TURN   170   172  3      
STRAND   173   176  4      
HELIX   185   187  3      
HELIX   194   205  12      
HELIX   211   219  9      
HELIX   223   226  4      
TURN   232   234  3      
HELIX   237   253  17      
HELIX   264   278  15      
Sequence information
Length: 285 AA [This is the length of the unprocessed precursor] Molecular weight: 33010 Da [This is the MW of the unprocessed precursor] CRC64: ED70B197FF267B2B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH 

        70         80         90        100        110        120 
AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG 

       130        140        150        160        170        180 
LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ 

       190        200        210        220        230        240 
PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL 

       250        260        270        280 
AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW 

Q9UGB7 in FASTA format

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