Reviewed, UniProtKB/Swiss-Prot Q920P0 (DCXR_RAT)

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
Synonyms:	Glb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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. Note= Probably recruited to membranes via an interaction with phosphatidylinositol By similarity.
Tissue specificity	Highly expressed in kidney and liver. Weakly or not expressed in brain, heart, lung, spleen, epididymis 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	Membrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-xylulose reductase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
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_0000054557
Regions
	Nucleotide binding	11 – 39	29	NADP By similarity
Sites
	Active site	149	1	Proton acceptor
	Active site	153	1
	Binding site	136	1	Substrate By similarity
Amino acid modifications
	Modified residue	149	1	Phosphotyrosine By similarity
Experimental info
	Mutagenesis	136	1	S → A: Loss of activity
	Mutagenesis	137	1	Q → M: Slightly reduced activity. Loss of activity for sugars; when associated with F-143 and L-146
	Mutagenesis	143	1	L → F: Slightly reduced activity. Loss of activity for sugars; when associated with M-137 and L-146
	Mutagenesis	146	1	H → L: Slightly reduced activity. Loss of activity for sugars; when associated with M-137; F-143 and L-146
	Mutagenesis	149	1	Y → F: Loss of activity
	Mutagenesis	153	1	K → M: Loss of activity
	Mutagenesis	190	1	N → V: Slightly reduced activity. Loss of activity for sugars; when associated with S-191
	Mutagenesis	191	1	W → F: Slightly reduced activity
	Mutagenesis	191	1	W → S: Slightly reduced activity. Loss of activity for sugars; when associated with V-190

Sequences

	Sequence		Length	Mass (Da)
	Q920P0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 7BAEE7E7BB404057	FASTA	244	25,720
	10 20 30 40 50 60 MDLGLAGRRA LVTGAGKGIG RSTVLALQAA GAQVVAVSRT REDLDSLVRE CPGVEPVCVD 70 80 90 100 110 120 LADWEATEQA LSNVGPVDLL VNNAAVATLQ PFLEVTKEAC DTSFNVNFRA VVQVSQIVAR 130 140 150 160 170 180 GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALDMLT KVMALELGPH KIRVNAVNPT 190 200 210 220 230 240 VVMTPMGRAN WSDPHKAKVM LDRIPLGKFA EVENVVDTIL FLLSNRSSMT TGSALPVDGG FLAT

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, TISSUE SPECIFICITY.
[2]	"Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis." Ishikura S., Isaji T., Usami N., Nakagawa J., El-Kabbani O., Hara A. Chem. Biol. Interact. 143:543-550(2003) [PubMed: 12604240] [Abstract] Cited for: MUTAGENESIS OF SER-136; GLN-137; LEU-143; HIS-146; TYR-149; LYS-153; ASN-190 AND TRP-191.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB061719 mRNA. Translation: BAB64340.1.
RefSeq	NP_599214.1.
UniGene	Rn.177518
3D structure databases
HSSP	HSSP built from PDB template 1CYD based on UniProtKB P08074.
SMR	Q920P0. Positions 1-243.
ModBase	Search...
Genome annotation databases
GeneID	171408.
KEGG	rno:171408.
Organism-specific databases
RGD	620031. Dcxr.
Phylogenomic databases
HOVERGEN	Q920P0.
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	622280.

Entry information

Entry name

DCXR_RAT

Accession

Primary (citable) accession number: Q920P0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 1, 2001
Last modified:	November 25, 2008
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)