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Protein

L-xylulose reductase

Gene

DCXR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Xylitol + NADP+ = L-xylulose + NADPH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361Substrate1 Publication
Active sitei149 – 1491Proton acceptor
Binding sitei153 – 1531NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 4030NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  • L-xylulose reductase (NADP+) activity Source: UniProtKB
  • oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB

GO - Biological processi

  • D-xylose metabolic process Source: UniProtKB-KW
  • glucose metabolic process Source: UniProtKB
  • NADP metabolic process Source: Ensembl
  • oxidation-reduction process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • xylulose metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Xylose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.10. 2681.
SABIO-RKQ7Z4W1.

Names & Taxonomyi

Protein namesi
Recommended name:
L-xylulose reductase (EC:1.1.1.10)
Short name:
XR
Alternative name(s):
Carbonyl reductase II
Dicarbonyl/L-xylulose reductase
Kidney dicarbonyl reductase
Short name:
kiDCR
Short chain dehydrogenase/reductase family 20C member 1
Sperm surface protein P34H
Gene namesi
Name:DCXR
Synonyms:SDR20C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:18985. DCXR.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: Ensembl
  • cytoplasmic microtubule Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
  • microvillus Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Pentosuria (PNTSU)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn inborn error of metabolism characterized by excessive urinary excretion of L-xylulose.

See also OMIM:260800

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071N → L or D: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme. 1 Publication

Organism-specific databases

MIMi260800. phenotype.
Orphaneti2843. Pentosuria.
PharmGKBiPA38772.

Polymorphism and mutation databases

BioMutaiDCXR.
DMDMi50400451.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244L-xylulose reductasePRO_0000054554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei46 – 461Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7Z4W1.
PaxDbiQ7Z4W1.
PRIDEiQ7Z4W1.

2D gel databases

REPRODUCTION-2DPAGEIPI00448095.

PTM databases

PhosphoSiteiQ7Z4W1.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ7Z4W1.
CleanExiHS_DCXR.
ExpressionAtlasiQ7Z4W1. baseline and differential.
GenevisibleiQ7Z4W1. HS.

Organism-specific databases

HPAiHPA023371.
HPA023863.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi119357. 8 interactions.
IntActiQ7Z4W1. 2 interactions.
STRINGi9606.ENSP00000303356.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 397Combined sources
Helixi41 – 5010Combined sources
Beta strandi55 – 584Combined sources
Helixi64 – 718Combined sources
Beta strandi79 – 824Combined sources
Helixi92 – 943Combined sources
Helixi97 – 10711Combined sources
Helixi109 – 12517Combined sources
Beta strandi129 – 1346Combined sources
Helixi137 – 1393Combined sources
Helixi147 – 16721Combined sources
Helixi168 – 1703Combined sources
Beta strandi172 – 1798Combined sources
Helixi185 – 1884Combined sources
Helixi194 – 2018Combined sources
Helixi212 – 22312Combined sources
Helixi225 – 2273Combined sources
Beta strandi234 – 2385Combined sources
Helixi241 – 2433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PR9X-ray1.96A/B1-244[»]
1WNTX-ray2.30A/B/C/D1-244[»]
3D3WX-ray1.87A/B1-244[»]
ProteinModelPortaliQ7Z4W1.
SMRiQ7Z4W1. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z4W1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105069.
InParanoidiQ7Z4W1.
KOiK03331.
OMAiKANHESW.
PhylomeDBiQ7Z4W1.
TreeFamiTF313841.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z4W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE
60 70 80 90 100
CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF
110 120 130 140 150
DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC
160 170 180 190 200
STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM
210 220 230 240
LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC
Length:244
Mass (Da):25,913
Last modified:July 19, 2004 - v2
Checksum:iF82B7A178D46EAA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → A in AAP97273 (Ref. 5) Curated
Sequence conflicti239 – 2391G → R (PubMed:10385429).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11799.1.
RefSeqiNP_001182147.1. NM_001195218.1.
NP_057370.1. NM_016286.3.
UniGeneiHs.9857.

Genome annotation databases

EnsembliENST00000306869; ENSP00000303356; ENSG00000169738.
GeneIDi51181.
KEGGihsa:51181.
UCSCiuc002kdg.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11799.1.
RefSeqiNP_001182147.1. NM_001195218.1.
NP_057370.1. NM_016286.3.
UniGeneiHs.9857.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PR9X-ray1.96A/B1-244[»]
1WNTX-ray2.30A/B/C/D1-244[»]
3D3WX-ray1.87A/B1-244[»]
ProteinModelPortaliQ7Z4W1.
SMRiQ7Z4W1. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119357. 8 interactions.
IntActiQ7Z4W1. 2 interactions.
STRINGi9606.ENSP00000303356.

Chemistry

ChEMBLiCHEMBL2314.

PTM databases

PhosphoSiteiQ7Z4W1.

Polymorphism and mutation databases

BioMutaiDCXR.
DMDMi50400451.

2D gel databases

REPRODUCTION-2DPAGEIPI00448095.

Proteomic databases

MaxQBiQ7Z4W1.
PaxDbiQ7Z4W1.
PRIDEiQ7Z4W1.

Protocols and materials databases

DNASUi51181.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306869; ENSP00000303356; ENSG00000169738.
GeneIDi51181.
KEGGihsa:51181.
UCSCiuc002kdg.3. human.

Organism-specific databases

CTDi51181.
GeneCardsiGC17M079993.
HGNCiHGNC:18985. DCXR.
HPAiHPA023371.
HPA023863.
MIMi260800. phenotype.
608347. gene.
neXtProtiNX_Q7Z4W1.
Orphaneti2843. Pentosuria.
PharmGKBiPA38772.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105069.
InParanoidiQ7Z4W1.
KOiK03331.
OMAiKANHESW.
PhylomeDBiQ7Z4W1.
TreeFamiTF313841.

Enzyme and pathway databases

BRENDAi1.1.1.10. 2681.
SABIO-RKQ7Z4W1.

Miscellaneous databases

ChiTaRSiDCXR. human.
EvolutionaryTraceiQ7Z4W1.
GenomeRNAii51181.
NextBioi54147.
PROiQ7Z4W1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z4W1.
CleanExiHS_DCXR.
ExpressionAtlasiQ7Z4W1. baseline and differential.
GenevisibleiQ7Z4W1. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 PNTSU.
  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 PNTSU.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: INVOLVEMENT IN PNTSU.
  12. "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].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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).
  16. "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.

Entry informationi

Entry nameiDCXR_HUMAN
AccessioniPrimary (citable) accession number: Q7Z4W1
Secondary accession number(s): Q9BTZ3, Q9UHY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: June 24, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.