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Reviewed, UniProtKB/Swiss-Prot Q7Z4W1 (DCXR_HUMAN)

Last modified November 4, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
    Kidney dicarbonyl reductase
      Short name=kiDCR
    Carbonyl reductase II
    Sperm surface protein P34H
Gene names
Name: DCXR
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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, liver and epididymis. In the epididymis, it is mainly expressed in the proximal and distal sections of the corpus region. Weakly or not expressed in brain, lung, heart, spleen and testis.

Involvement in disease

Defects in DCXR are a cause of pentosuria [MIM:260800]; also called L-xylulosuria or xylitol dehydrogenase deficiency. Pentosuria is an inborn error of carbohydrate metabolism, characterized by the excessive urinary excretion of the sugar xylitol.

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
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244L-xylulose reductase
PRO_0000054554

Regions

Nucleotide binding11 – 4030NADP

Sites

Active site1491Proton acceptor
Binding site1361Substrate
Binding site1531NADP

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue1491Phosphotyrosine

Experimental info

Mutagenesis1071N → L or D: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme
Sequence conflict1181V → A in AAP97273. Ref.5
Sequence conflict2391G → R Ref.1

Secondary structure

.......................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7Z4W1-1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: F82B7A178D46EAA5

FASTA24425,913
        10         20         30         40         50         60 
MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD 

        70         80         90        100        110        120 
LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR 

       130        140        150        160        170        180 
GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT 

       190        200        210        220        230        240 
VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG 


FWAC 

« Hide

References

« Hide 'large scale' references
[1]"P34H sperm protein is preferentially expressed by the human corpus epididymidis."
Legare C., Gaudreault C., St Jacques S., Sullivan R.
Endocrinology 140:3318-3327(1999) [PubMed: 10385429] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Epididymis.
[2]"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, INVOLVEMENT IN PENTOSURIA.
[3]"Molecular cloning of human sperm surface protein P34H gene and semi-quantitative analysis of its expression in testis and epididymidis."
Xia X.Y., Xu X.F., Gao Y., Huang Y.F.
Zhonghua Nan Ke Xue 9:24-27(2003) [PubMed: 12680326] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epididymis, Liver and Testis.
[4]"A novel gene expressed in the human adrenal gland."
Huang C., Li Y., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Zhang C., Han Z., Wang Y., Chen Z., Fu G.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.
[5]"Cloning and characterization of a new human cDNA of carbonyl reductase."
Liu Q., Yu L., Zhao S.Y.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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].
Tissue: Lung and Placenta.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1.
Tissue: Platelet.
[9]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, MASS SPECTROMETRY.
[10]"Crystallization and preliminary crystallographic analysis of human L-xylulose reductase."
El-Kabbani O., Chung R.P.-T., Ishikura S., Usami N., Nakagawa J., Hara A.
Acta Crystallogr. D 58:1379-1380(2002) [PubMed: 12136162] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
[11]"Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis."
El-Kabbani O., Ishikura S., Darmanin C., Carbone V., Chung R.P.-T., Usami N., Hara A.
Proteins 55:724-732(2004) [PubMed: 15103634] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE, MUTAGENESIS OF ASN-107.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB013846 mRNA. Translation: BAB64299.1.
AF515623 mRNA. Translation: AAN59786.1.
AF515624 mRNA. Translation: AAO15991.1.
AF515625 mRNA. Translation: AAM54026.1.
AF113123 mRNA. Translation: AAF14864.1.
AF139841 mRNA. Translation: AAP97273.1.
BT006881 mRNA. Translation: AAP35527.1.
BC001470 mRNA. Translation: AAH01470.1.
BC003018 mRNA. Translation: AAH03018.1.
RefSeqNP_057370.1.
UniGeneHs.9857

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PR9X-ray1.96A/B1-244[»]
1WNTX-ray2.30A/B/C/D1-244[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ7Z4W1.

PTM databases

PhosphoSiteQ7Z4W1.

2-D gel databases

REPRODUCTION-2DPAGEIPI00448095.

Genome annotation databases

EnsemblENSG00000169738. Homo sapiens. [Contig view]
GeneID51181.
KEGGhsa:51181.

Organism-specific databases

H-InvDBHIX0014266.
HGNCHGNC:18985. DCXR.
MIM260800. phenotype.
608347. gene.
PharmGKBPA38772.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ7Z4W1.
HOVERGENQ7Z4W1.

Gene expression databases

ArrayExpressQ7Z4W1.
CleanExHS_DCXR.
GermOnlineENSG00000169738. Homo sapiens.

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...

Other Resources

NextBio54147.
SOURCESearch...

Entry information

Entry nameDCXR_HUMAN
AccessionPrimary (citable) accession number: Q7Z4W1
Secondary accession number(s): Q9BTZ3, Q9UHY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: November 4, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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