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Reviewed, UniProtKB/Swiss-Prot Q920N9 (DCXR_CAVPO)

Last modified November 25, 2008. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-xylulose reductase
      Short name=XR
    EC=1.1.1.10
Alternative name(s):
    Dicarbonyl/L-xylulose reductase
    Protein P26h
Gene names
Name: DCXR
Synonyms: GLB
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. Note= Probably recruited to membranes via an interaction with phosphatidylinositol By similarity.

Tissue specificity

Highly expressed in kidney and liver. Expressed in epididymis. Expressed at intermediate level in lung. Weakly expressed in brain, heart, spleen and testis.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords

   Biological processCarbohydrate metabolism
Glucose metabolism
Xylose metabolism
   Cellular componentMembrane
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processD-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 componentmembrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-xylulose reductase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244L-xylulose reductase
PRO_0000054553

Regions

Nucleotide binding11 – 3929NADP By similarity

Sites

Active site1491Proton acceptor By similarity
Active site1531 By similarity
Binding site1361Substrate By similarity

Amino acid modifications

Modified residue1491Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q920N9-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C7AE9AE263C59B5A

FASTA24425,750
        10         20         30         40         50         60 
MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD 

        70         80         90        100        110        120 
LADWEATEQA LSNVGPADLL VNNAAVALLQ PFLEVTKEAC VTSFNVNLRA VIQVSQIVAK 

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

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


FLAT 

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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.
Strain: Hartley.
Tissue: Liver.

Cross-references

Sequence databases

AB061720 mRNA. Translation: BAB64341.1.

3D structure databases

HSSPHSSP built from PDB template 1CYD based on UniProtKB P08074.
SMRQ920N9. Positions 1-243.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ920N9.

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCXR_CAVPO
AccessionPrimary (citable) accession number: Q920N9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: November 25, 2008
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents