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Q7Z4W1 (DCXR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-xylulose reductase

Short name=XR
EC=1.1.1.10
Alternative name(s):
Carbonyl reductase II
Dicarbonyl/L-xylulose reductase
Kidney dicarbonyl reductase
Short name=kiDCR
Sperm surface protein P34H
Gene names
Name:DCXR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
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. Ref.2

Subunit structure

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. Ref.1 Ref.2

Involvement in disease

The enzyme defect in pentosuria has been shown to involve L-xylulose reductase. Essential pentosuria is an inborn error of metabolism characterized by the excessive urinary excretion of the pentose L-xylulose.

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
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

NADP metabolic process

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 19442656. Source: UniProtKB

protein homotetramerization

Inferred from direct assay Ref.2. Source: UniProtKB

xylulose metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentbrush border

Inferred from electronic annotation. Source: Ensembl

cytoplasmic microtubule

Inferred from direct assay PubMed 23264731. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microvillus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionL-xylulose reductase (NADP+) activity

Inferred from direct assay Ref.2. Source: UniProtKB

oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Inferred from direct assay PubMed 19442656. Source: UniProtKB

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 Ref.8 Ref.11 Ref.12

Experimental info

Mutagenesis1071N → L or D: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme. Ref.14
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1.
Tissue: Platelet.
[9]"The enzymatic defect in essential pentosuria."
Wang Y.M., Van Eys J.
N. Engl. J. Med. 282:892-896(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PENTOSURIA.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
[14]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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.
CCDSCCDS11799.1.
RefSeqNP_001182147.1. NM_001195218.1.
NP_057370.1. NM_016286.3.
UniGeneHs.9857.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PR9X-ray1.96A/B1-244[»]
1WNTX-ray2.30A/B/C/D1-244[»]
3D3WX-ray1.87A/B1-244[»]
ProteinModelPortalQ7Z4W1.
SMRQ7Z4W1. Positions 1-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119357. 4 interactions.
IntActQ7Z4W1. 2 interactions.
STRING9606.ENSP00000303356.

Chemistry

ChEMBLCHEMBL2314.

PTM databases

PhosphoSiteQ7Z4W1.

Polymorphism databases

DMDM50400451.

2D gel databases

REPRODUCTION-2DPAGEIPI00448095.

Proteomic databases

MaxQBQ7Z4W1.
PaxDbQ7Z4W1.
PRIDEQ7Z4W1.

Protocols and materials databases

DNASU51181.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306869; ENSP00000303356; ENSG00000169738.
GeneID51181.
KEGGhsa:51181.
UCSCuc002kdg.3. human.

Organism-specific databases

CTD51181.
GeneCardsGC17M079993.
HGNCHGNC:18985. DCXR.
HPAHPA023371.
HPA023863.
MIM608347. gene.
neXtProtNX_Q7Z4W1.
Orphanet2843. Pentosuria.
PharmGKBPA38772.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG105069.
InParanoidQ7Z4W1.
KOK03331.
OMAPHKAKAM.
PhylomeDBQ7Z4W1.
TreeFamTF313841.

Enzyme and pathway databases

BRENDA1.1.1.10. 2681.
SABIO-RKQ7Z4W1.

Gene expression databases

ArrayExpressQ7Z4W1.
BgeeQ7Z4W1.
CleanExHS_DCXR.
GenevestigatorQ7Z4W1.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCXR. human.
EvolutionaryTraceQ7Z4W1.
GenomeRNAi51181.
NextBio54147.
PROQ7Z4W1.
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: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 17

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