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UniProtKB/Swiss-Prot entry Q91X52


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

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Entry information
Entry name DCXR_MOUSE
Primary accession number Q91X52
Secondary accession numbers Q3U5L5 Q9D129 Q9D8W1
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on July 19, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name L-xylulose reductase
Synonyms XR
EC 1.1.1.10
Dicarbonyl/L-xylulose reductase
Gene name
Name: Dcxr
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6;
TISSUE=Kidney;
DOI=10.1074/jbc.M110703200; PubMed=11882650 [NCBI, ExPASy, EBI, Israel, Japan]
Nakagawa J., Ishikura S., Asami J., Isaji T., Usami N., Hara A., Sakurai T., Tsuritani K., Oda K., Takahashi M., Yoshimoto M., Otsuka N., Kitamura K.;
"Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney.";
J. Biol. Chem. 277:17883-17891(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Embryo, and Pancreas;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Salivary gland;
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).
Comments
  • FUNCTION: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
  • CATALYTIC ACTIVITY: Xylitol + NADP+ = L-xylulose + NADPH.
  • SUBUNIT: Homotetramer.
  • SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By similarity). Apical cell membrane; Peripheral membrane protein. Note=Probably recruited to membranes via an interaction with phosphatidylinositol (By similarity). In kidney, it is localized in the brush border membranes of proximal tubular cells.
  • TISSUE SPECIFICITY: Highly expressed in kidney, liver and epididymis. Expressed at intermediate level in lung. Weakly or not expressed in brain, heart, spleen and testis.
  • SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.
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
D89656; BAB88678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004023; BAB23131.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007627; BAB25146.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153521; BAE32063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012247; AAH12247.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_080704.2; -.
UniGene Mm.231091
3D structure databases
HSSP P08074; 1CYD. [HSSP ENTRY / PDB]
SMR Q91X52; 1-243.
ModBase Q91X52.
PTM databases
PhosphoSite Q91X52; -.
2D gel databases
REPRODUCTION-2DPAGE Q91X52; -.
Organism-specific databases
MGI MGI:1915130; Dcxr.
Gene expression databases
ArrayExpress Q91X52; -.
CleanEx MM_DCXR; -.
GermOnline ENSMUSG00000039450; Mus musculus.
Ontologies
GO
GO:0005903; Cellular component: brush border (inferred from direct assay from MGI).
GO:0005902; Cellular component: microvillus (inferred from direct assay from MGI).
GO:0016614; Molecular function: oxidoreductase activity, acting on CH-OH group of donors (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0006739; Biological process: NADP metabolic process (inferred from direct assay from MGI).
GO:0005997; Biological process: xylulose metabolic process (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
BLOCKS Q91X52.
Genome annotation databases
Ensembl ENSMUSG00000039450; Mus musculus. [Contig view]
GeneID 67880; -.
KEGG mmu:67880; -.
Phylogenomic databases
HOGENOM Q91X52; -.
HOVERGEN Q91X52; -.
Other
SOURCE Dcxr; Mus musculus.
ProtoNet Q91X52.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Cell membrane; Glucose metabolism; Membrane; NADP; Oxidoreductase; Xylose metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   244  244     L-xylulose reductase. PRO_0000054556
NP_BIND   11    39  29     NADP (By similarity). 
ACT_SITE   149   149        Proton acceptor (By similarity). 
ACT_SITE   153   153        By similarity. 
BINDING   136   136        Substrate (By similarity). 
CONFLICT   127   127        V -> N (in Ref. 3; AAH12247). 
CONFLICT   133   135        NVS -> KKY (in Ref. 3; AAH12247). 
CONFLICT   157   158        DM -> FL (in Ref. 3; AAH12247). 
CONFLICT   162   162        M -> R (in Ref. 3; AAH12247). 
CONFLICT   172   172        I -> S (in Ref. 3; AAH12247). 
CONFLICT   184   184        T -> R (in Ref. 3; AAH12247). 
CONFLICT   202   203        DR -> ES (in Ref. 3; AAH12247). 
CONFLICT   224   224        S -> G (in Ref. 2; BAB23131). 
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 25746 Da [This is the MW of the unprocessed precursor] CRC64: 9701111544053820 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD 

        70         80         90        100        110        120 
LADWEATEQA LSNVGPVDLL VNNAAVALLQ PFLEVTKEAC DTSFNVNLRA VIQVSQIVAK 

       130        140        150        160        170        180 
GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALDMLT KMMALELGPH KIRVNAVNPT 

       190        200        210        220        230        240 
VVMTPMGRTN WSDPHKAKAM LDRIPLGKFA EVENVVDTIL FLLSNRSGMT TGSTLPVDGG 


FLAT 

Q91X52 in FASTA format

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