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UniProtKB/Swiss-Prot entry Q7Z4W1


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

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Entry information
Entry name DCXR_HUMAN
Primary accession number Q7Z4W1
Secondary accession numbers Q9BTZ3 Q9UHY9
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on July 19, 2004 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 53)
Name and origin of the protein
Protein name L-xylulose reductase
Synonyms XR
EC 1.1.1.10
Dicarbonyl/L-xylulose reductase
Kidney dicarbonyl reductase
kiDCR
Carbonyl reductase II
Sperm surface protein P34H
Gene name
Name: DCXR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Epididymis;
DOI=10.1210/en.140.7.3318; PubMed=10385429 [NCBI, ExPASy, EBI, Israel, Japan]
Legare C., Gaudreault C., St Jacques S., Sullivan R.;
"P34H sperm protein is preferentially expressed by the human corpus epididymidis.";
Endocrinology 140:3318-3327(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, AND INVOLVEMENT IN PENTOSURIA.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epididymis, Liver, and Testis;
PubMed=12680326 [NCBI, ExPASy, EBI, Israel, Japan]
Xia X.Y., Xu X.F., Gao Y., Huang Y.F.;
"Molecular cloning of human sperm surface protein P34H gene and semi-quantitative analysis of its expression in testis and epididymidis.";
Zhonghua Nan Ke Xue 9:24-27(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=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.;
"A novel gene expressed in the human adrenal gland.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Liu Q., Yu L., Zhao S.Y.;
"Cloning and characterization of a new human cDNA of carbonyl reductase.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[10]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
DOI=10.1107/S0907444902008156; PubMed=12136162 [NCBI, ExPASy, EBI, Israel, Japan]
El-Kabbani O., Chung R.P.-T., Ishikura S., Usami N., Nakagawa J., Hara A.;
"Crystallization and preliminary crystallographic analysis of human L-xylulose reductase.";
Acta Crystallogr. D 58:1379-1380(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE, AND MUTAGENESIS OF ASN-107.
DOI=10.1002/prot.20047; PubMed=15103634 [NCBI, ExPASy, EBI, Israel, Japan]
El-Kabbani O., Ishikura S., Darmanin C., Carbone V., Chung R.P.-T., Usami N., Hara A.;
"Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis.";
Proteins 55:724-732(2004).
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, 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.
  • 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.
  • 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
AB013846; BAB64299.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515623; AAN59786.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515624; AAO15991.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515625; AAM54026.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF113123; AAF14864.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF139841; AAP97273.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006881; AAP35527.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001470; AAH01470.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003018; AAH03018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057370.1; -.
UniGene Hs.9857
3D structure databases
PDB
1PR9; X-ray; 1.96 A; A/B=1-244.[ExPASy / RCSB / EBI]
1WNT; X-ray; 2.30 A; A/B/C/D=1-244.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PR9; -.
1WNT; -.
ModBase Q7Z4W1.
PTM databases
PhosphoSite Q7Z4W1; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00448095; -.
Organism-specific databases
H-InvDB HIX0014266; -.
HGNC HGNC:18985; DCXR.
GenAtlas DCXR.
MIM 260800; phenotype. [NCBI / EBI]
608347; gene. [NCBI / EBI]
PharmGKB PA38772; -.
GeneCards Q7Z4W1.
Gene expression databases
ArrayExpress Q7Z4W1; -.
CleanEx HS_DCXR; -.
GermOnline ENSG00000169738; Homo sapiens.
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.
BLOCKS Q7Z4W1.
Genome annotation databases
Ensembl ENSG00000169738; Homo sapiens. [Contig view]
GeneID 51181; -.
KEGG hsa:51181; -.
Phylogenomic databases
HOGENOM Q7Z4W1; -.
HOVERGEN Q7Z4W1; -.
Other
SOURCE DCXR; Homo sapiens.
ProtoNet Q7Z4W1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Carbohydrate metabolism; Direct protein sequencing; 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_0000054554
NP_BIND   11    40  30     NADP. 
ACT_SITE   149   149        Proton acceptor. 
BINDING   136   136        Substrate. 
BINDING   153   153        NADP. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   149   149        Phosphotyrosine. 
MUTAGEN   107   107        N->L,D: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme. 
CONFLICT   118   118        V -> A (in Ref. 5; AAP97273). 
CONFLICT   239   239        G -> R (in Ref. 1). 
STRAND   9    14  6      
HELIX   18    29  12      
STRAND   33    39  7      
HELIX   41    50  10      
STRAND   55    58  4      
HELIX   64    71  8      
STRAND   79    82  4      
HELIX   92    94  3      
HELIX   97   107  11      
HELIX   109   125  17      
STRAND   129   134  6      
HELIX   137   139  3      
HELIX   147   167  21      
HELIX   168   170  3      
STRAND   172   179  8      
HELIX   185   188  4      
HELIX   194   201  8      
HELIX   212   223  12      
HELIX   225   227  3      
STRAND   234   238  5      
HELIX   241   243  3      
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 25913 Da [This is the MW of the unprocessed precursor] CRC64: F82B7A178D46EAA5 [This is a checksum on the sequence]
        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 

Q7Z4W1 in FASTA format

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