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Q9UGB7 (MIOX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol oxygenase

EC=1.13.99.1
Alternative name(s):
Aldehyde reductase-like 6
Kidney-specific protein 32
Myo-inositol oxygenase
Short name=MI oxygenase
Renal-specific oxidoreductase
Gene names
Name:MIOX
Synonyms:ALDRL6, KSP32, RSOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Myo-inositol + O2 = D-glucuronate + H2O. Ref.10

Cofactor

Binds 2 iron ions per subunit. Ref.10

Pathway

Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Kidney specific.

Sequence similarities

Belongs to the myo-inositol oxygenase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UGB7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UGB7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     114-231: DWFHLVGLLH...FYPWHTGRDY → VPNLPCPSPS...QAAALLPGAH
     232-285: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Inositol oxygenase
PRO_0000079148

Regions

Region85 – 873Substrate binding
Region141 – 1422Substrate binding
Region220 – 2212Substrate binding

Sites

Metal binding981Iron 1
Metal binding1231Iron 1
Metal binding1241Iron 1
Metal binding1241Iron 2
Metal binding1941Iron 2
Metal binding2201Iron 2
Metal binding2531Iron 1
Binding site291Substrate By similarity
Binding site1271Substrate

Natural variations

Alternative sequence114 – 231118DWFHL…TGRDY → VPNLPCPSPSQTGSTSSGSC TTWGRSWPCSGSPSGLSSAT PSPSDAVRRPPWFSATPPSR TTLTSRILDTAQSSGCISPT VGSTGSSCPGAMMQVRPLHQ VPGPAGRGQAAALLPGAH in isoform 2.
VSP_041667
Alternative sequence232 – 28554Missing in isoform 2.
VSP_041668

Experimental info

Mutagenesis1271K → S: Strongly reduced enzyme activity. Ref.10
Sequence conflict41T → D in AAF25204. Ref.3
Sequence conflict1991Y → F in AAK00766. Ref.2
Sequence conflict219 – 2213FHS → VHF in AAK00766. Ref.2
Sequence conflict2821I → T in AAF25204. Ref.3

Secondary structure

........................................... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: ED70B197FF267B2B

FASTA28533,010
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4C63EF35422491AF
Show »

FASTA23124,516

References

« Hide 'large scale' references
[1]"Cloning and expression of human myo-inositol oxygenase (MIOX)."
Parthasarathy L., Seelan R., Parthasarathy R.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification of a novel kidney specific gene, KSP32, that is down regulated in acute ischemic renal failure."
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.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"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] (ISOFORM 1).
Tissue: Kidney.
[4]"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] (ISOFORM 1).
Tissue: Kidney.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"A genome annotation-driven approach to cloning the human ORFeome."
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.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"The DNA sequence of human chromosome 22."
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. expand/collapse author list , 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.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORMS 1 AND 2).
Tissue: Colon and Kidney.
[10]"Structural and biophysical characterization of human myo-inositol oxygenase."
Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M., Graslund S., Graslund A., Hallberg B.M.
J. Biol. Chem. 283:15209-15216(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285 IN COMPLEX WITH IRON AND MYO-INOSOSE-1, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF LYS-127.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY064416 mRNA. Translation: AAL47192.1.
AF230095 mRNA. Translation: AAK00766.1.
AF197129 mRNA. Translation: AAF25204.1.
AY738258 mRNA. Translation: AAV65816.1.
AK000576 mRNA. Translation: BAA91266.1.
CR456478 mRNA. Translation: CAG30364.1.
AL096767 Genomic DNA. Translation: CAB63064.1.
AL096767 Genomic DNA. Translation: CAO03465.1.
CH471138 Genomic DNA. Translation: EAW73547.1.
BC012025 mRNA. Translation: AAH12025.1.
BC073848 mRNA. Translation: AAH73848.1.
CCDSCCDS14092.1. [Q9UGB7-1]
RefSeqNP_060054.4. NM_017584.5. [Q9UGB7-1]
UniGeneHs.129227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IBNX-ray1.50A/B38-285[»]
ProteinModelPortalQ9UGB7.
SMRQ9UGB7. Positions 37-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000216075.

PTM databases

PhosphoSiteQ9UGB7.

Proteomic databases

PaxDbQ9UGB7.
PRIDEQ9UGB7.

Protocols and materials databases

DNASU55586.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216075; ENSP00000216075; ENSG00000100253. [Q9UGB7-1]
ENST00000395733; ENSP00000379082; ENSG00000100253. [Q9UGB7-2]
GeneID55586.
KEGGhsa:55586.
UCSCuc003bll.1. human. [Q9UGB7-1]
uc003bln.1. human. [Q9UGB7-2]

Organism-specific databases

CTD55586.
GeneCardsGC22P050925.
HGNCHGNC:14522. MIOX.
HPAHPA039451.
HPA039562.
MIM606774. gene.
neXtProtNX_Q9UGB7.
PharmGKBPA24716.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG135479.
HOGENOMHOG000163182.
HOVERGENHBG039556.
InParanoidQ9UGB7.
KOK00469.
OMANFYREQH.
OrthoDBEOG7DZ8KD.
PhylomeDBQ9UGB7.
TreeFamTF300089.

Enzyme and pathway databases

BRENDA1.13.99.1. 2681.
SABIO-RKQ9UGB7.
UniPathwayUPA00111; UER00527.

Gene expression databases

BgeeQ9UGB7.
CleanExHS_MIOX.
GenevestigatorQ9UGB7.

Family and domain databases

InterProIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERPTHR12588. PTHR12588. 1 hit.
PfamPF05153. DUF706. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMIOX. human.
EvolutionaryTraceQ9UGB7.
GenomeRNAi55586.
NextBio60104.
PROQ9UGB7.
SOURCESearch...

Entry information

Entry nameMIOX_HUMAN
AccessionPrimary (citable) accession number: Q9UGB7
Secondary accession number(s): Q05DJ6 expand/collapse secondary AC list , Q5S8C9, Q9BZZ1, Q9UHB8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM