Reviewed, UniProtKB/Swiss-Prot Q91X52 (DCXR_MOUSE)

Names and origin

Protein names

Recommended name:
    L-xylulose reductase
      Short name=XR
    EC=1.1.1.10
Alternative name(s):
    Dicarbonyl/L-xylulose reductase

Gene names

Name:

Dcxr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (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 structure	Homotetramer.
Subcellular location	Membrane; Peripheral membrane proteinBy 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.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Xylose metabolism
Cellular component	Cell membrane Membrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW NADP metabolic process Ref.1 Inferred from direct assay. Source: MGI glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW xylulose metabolic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell brush border Ref.1 Inferred from direct assay. Source: MGI microvillus Ref.1 Inferred from direct assay. Source: MGI
Molecular function	L-xylulose reductase activity Inferred from electronic annotation. Source: EC protein binding Ref.1 Inferred from physical interaction. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	L-xylulose reductase		PRO_0000054556
Regions
	Nucleotide binding	11 – 39	29	NADP By similarity
Sites
	Active site	149	1	Proton acceptor By similarity
	Active site	153	1	By similarity
	Binding site	136	1	Substrate By similarity
Amino acid modifications
	Modified residue	149	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	127	1	V → N in AAH12247. Ref.3
	Sequence conflict	133 – 135	3	NVS → KKY in AAH12247. Ref.3
	Sequence conflict	157 – 158	2	DM → FL in AAH12247. Ref.3
	Sequence conflict	162	1	M → R in AAH12247. Ref.3
	Sequence conflict	172	1	I → S in AAH12247. Ref.3
	Sequence conflict	184	1	T → R in AAH12247. Ref.3
	Sequence conflict	202 – 203	2	DR → ES in AAH12247. Ref.3
	Sequence conflict	224	1	S → G in BAB23131. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q91X52-1 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 9701111544053820	FASTA	244	25,746
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney." 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. J. Biol. Chem. 277:17883-17891(2002) [PubMed: 11882650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Kidney.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Embryo and Pancreas.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D89656 mRNA. Translation: BAB88678.1. AK004023 mRNA. Translation: BAB23131.1. AK007627 mRNA. Translation: BAB25146.1. AK153521 mRNA. Translation: BAE32063.1. BC012247 mRNA. Translation: AAH12247.1.
RefSeq	NP_080704.2.
UniGene	Mm.231091
3D structure databases
HSSP	HSSP built from PDB template 1CYD based on UniProtKB P08074.
SMR	Q91X52. Positions 1-243.
ModBase	Search...
PTM databases
PhosphoSite	Q91X52.
2-D gel databases
REPRODUCTION-2DPAGE	Q91X52.
Genome annotation databases
Ensembl	ENSMUSG00000039450. Mus musculus. [Contig view]
GeneID	67880.
KEGG	mmu:67880.
Organism-specific databases
MGI	MGI:1915130. Dcxr.
Phylogenomic databases
HOGENOM	Q91X52.
HOVERGEN	Q91X52.
Gene expression databases
ArrayExpress	Q91X52.
CleanEx	MM_DCXR.
GermOnline	ENSMUSG00000039450. Mus musculus.
Family and domain databases
InterPro	IPR002198. DHase_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DHase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	325821.
SOURCE	Search...

Entry information

Entry name

DCXR_MOUSE

Accession

Primary (citable) accession number: Q91X52
Secondary accession number(s): Q3U5L5, Q9D129, Q9D8W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)