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UniProtKB/Swiss-Prot entry Q920P0

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

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Entry information
Entry name DCXR_RAT
Primary accession number Q920P0
Secondary accession numbers None
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
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
Synonyms: Glb
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
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]
 MUTAGENESIS OF SER-136; GLN-137; LEU-143; HIS-146; TYR-149; LYS-153; ASN-190 AND TRP-191.
DOI=10.1016/S0009-2797(02)00217-X; PubMed=12604240 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikura S., Isaji T., Usami N., Nakagawa J., El-Kabbani O., Hara A.;
"Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis.";
Chem. Biol. Interact. 143:543-550(2003).
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). 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.
  • 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
AB061719; BAB64340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_599214.1; -.
UniGene Rn.177518
3D structure databases
HSSP P08074; 1CYD. [HSSP ENTRY / PDB]
SMR Q920P0; 1-243.
ModBase Q920P0.
Organism-specific databases
RGD 620031; Dcxr.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0050038; Molecular function: L-xylulose reductase activity (inferred from electronic annotation from EC).
GO:0042732; Biological process: D-xylose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006006; Biological process: glucose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet Q920P0.
Genome annotation databases
GeneID 171408; -.
KEGG rno:171408; -.
Phylogenomic databases
HOVERGEN Q920P0; -.
Other
NextBio 622280; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Glucose metabolism; Membrane; NADP; Oxidoreductase; Phosphoprotein; Xylose metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   244  244     L-xylulose reductase. PRO_0000054557
NP_BIND   11    39  29     NADP (By similarity). 
ACT_SITE   149   149        Proton acceptor. 
ACT_SITE   153   153         
BINDING   136   136        Substrate (By similarity). 
MOD_RES   149   149        Phosphotyrosine (By similarity). 
MUTAGEN   136   136        S->A: Loss of activity. 
MUTAGEN   137   137        Q->M: Slightly reduced activity. Loss of activity for sugars; when associated with F-143 and L-146. 
MUTAGEN   143   143        L->F: Slightly reduced activity. Loss of activity for sugars; when associated with M-137 and L-146. 
MUTAGEN   146   146        H->L: Slightly reduced activity. Loss of activity for sugars; when associated with M-137; F-143 and L-146. 
MUTAGEN   149   149        Y->F: Loss of activity. 
MUTAGEN   153   153        K->M: Loss of activity. 
MUTAGEN   190   190        N->V: Slightly reduced activity. Loss of activity for sugars; when associated with S-191. 
MUTAGEN   191   191        W->F: Slightly reduced activity. 
MUTAGEN   191   191        W->S: Slightly reduced activity. Loss of activity for sugars; when associated with V-190. 
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 25720 Da [This is the MW of the unprocessed precursor] CRC64: 7BAEE7E7BB404057 [This is a checksum on the sequence] 
        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
Q920P0 in FASTA format

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