Q9UGB7 (MIOX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol catabolic process Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB inclusion body Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	NADP binding Inferred from electronic annotation. Source: Compara aldo-keto reductase (NADP) activity Inferred from sequence or structural similarity. Source: UniProtKB ferric iron binding Inferred from direct assay Ref.10. Source: UniProtKB inositol oxygenase activity Inferred from direct assay Ref.10. Source: UniProtKB oxidoreductase activity, acting on NAD(P)H Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Inositol oxygenase

PRO_0000079148

Regions

Region

85 – 87

3

Substrate binding

Region

141 – 142

2

Substrate binding

Region

220 – 221

2

Substrate binding

Sites

Metal binding

98

1

Iron 1

Metal binding

123

1

Iron 1

Metal binding

124

1

Iron 1

Metal binding

124

1

Iron 2

Metal binding

194

1

Iron 2

Metal binding

220

1

Iron 2

Metal binding

253

1

Iron 1

Binding site

29

1

Substrate By similarity

Binding site

127

1

Substrate

Natural variations

Alternative sequence

114 – 231

118

DWFHL…TGRDY → VPNLPCPSPSQTGSTSSGSC TTWGRSWPCSGSPSGLSSAT PSPSDAVRRPPWFSATPPSR TTLTSRILDTAQSSGCISPT VGSTGSSCPGAMMQVRPLHQ VPGPAGRGQAAALLPGAH in isoform 2.

VSP_041667

Alternative sequence

232 – 285

54

Missing in isoform 2.

VSP_041668

Experimental info

Mutagenesis

127

1

K → S: Strongly reduced enzyme activity. Ref.10

Sequence conflict

4

1

T → D in AAF25204. Ref.3

Sequence conflict

199

1

Y → F in AAK00766. Ref.2

Sequence conflict

219 – 221

3

FHS → VHF in AAK00766. Ref.2

Sequence conflict

282

1

I → T in AAF25204. Ref.3

Secondary structure

1

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285

Helix Strand Turn

Details...

Helix

38 – 50

13

Helix

53 – 63

11

Beta 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

Beta strand

145 – 148

4

Helix

157 – 160

4

Helix

165 – 168

4

Turn

170 – 172

3

Beta 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

Beta strand

283 – 285

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: ED70B197FF267B2B	FASTA	285	33,010
	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
	Isoform 2 [UniParc]. Checksum: 4C63EF35422491AF	FASTA	231	24,516
	10 20 30 40 50 60 MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH 70 80 90 100 110 120 AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKVPNLPCP 130 140 150 160 170 180 SPSQTGSTSS GSCTTWGRSW PCSGSPSGLS SATPSPSDAV RRPPWFSATP PSRTTLTSRI 190 200 210 220 230 LDTAQSSGCI SPTVGSTGSS CPGAMMQVRP LHQVPGPAGR GQAAALLPGA H

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00099088.
IPI00807628.

RefSeq

NP_060054.4. NM_017584.5.

UniGene

Hs.129227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IBN	X-ray	1.50	A/B	38-285	[»]

ProteinModelPortal

Q9UGB7.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000216075.

PTM databases

PhosphoSite

Q9UGB7.

Polymorphism databases

DMDM

28380090.

Proteomic databases

PaxDb

Q9UGB7.

PRIDE

Q9UGB7.

Protocols and materials databases

DNASU

55586.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216075; ENSP00000216075; ENSG00000100253.
ENST00000395733; ENSP00000379082; ENSG00000100253.

GeneID

55586.

KEGG

hsa:55586.

UCSC

uc003bll.1. human.
uc003bln.1. human.

Organism-specific databases

CTD

55586.

GeneCards

GC22P050925.

HGNC

HGNC:14522. MIOX.

MIM

606774. gene.

neXtProt

NX_Q9UGB7.

PharmGKB

PA24716.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG135479.

HOGENOM

HOG000163182.

HOVERGEN

HBG039556.

InParanoid

Q9UGB7.

KO

K00469.

OMA

YDVESER.

OrthoDB

EOG454902.

PhylomeDB

Q9UGB7.

Enzyme and pathway databases

BRENDA

1.13.99.1. 2681.

SABIO-RK

Q9UGB7.

UniPathway

UPA00111; UER00527.

Gene expression databases

ArrayExpress

Q9UGB7.

Bgee

Q9UGB7.

CleanEx

HS_MIOX.

Genevestigator

Q9UGB7.

GermOnline

ENSG00000100253. Homo sapiens.

Family and domain databases

InterPro

IPR007828. Inositol_oxygenase.
[Graphical view]

PANTHER

PTHR12588. PTHR12588. 1 hit.

Pfam

PF05153. DUF706. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MIOX. human.

EvolutionaryTrace

Q9UGB7.

GenomeRNAi

55586.

NextBio

60104.

SOURCE

Search...

Entry information

Entry name

MIOX_HUMAN

Accession

Primary (citable) accession number: Q9UGB7
Secondary accession number(s): Q05DJ6 , Q5S8C9, Q9BZZ1, Q9UHB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.