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Q7Z4W1

- DCXR_HUMAN

UniProt

Q7Z4W1 - DCXR_HUMAN

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Protein
L-xylulose reductase
Gene
DCXR
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 1361Substrate
Active sitei149 – 1491Proton acceptor
Binding sitei153 – 1531NADP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 4030NADP
Add
BLAST

GO - Molecular functioni

  1. L-xylulose reductase (NADP+) activity Source: UniProtKB
  2. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. D-xylose metabolic process Source: UniProtKB-KW
  2. NADP metabolic process Source: Ensembl
  3. glucose metabolic process Source: UniProtKB
  4. oxidation-reduction process Source: UniProtKB
  5. protein homotetramerization Source: UniProtKB
  6. 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
Sperm surface protein P34H
Gene namesi
Name:DCXR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:18985. DCXR.

Subcellular locationi

Membrane; Peripheral membrane protein By similarity
Note: Probably recruited to membranes via an interaction with phosphatidylinositol By similarity.

GO - Cellular componenti

  1. brush border Source: Ensembl
  2. cytoplasmic microtubule Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB-SubCell
  5. microvillus Source: Ensembl
  6. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Pentosuria (PNTSU) [MIM:260800]: An inborn error of metabolism characterized by excessive urinary excretion of L-xylulose.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244L-xylulose reductase
PRO_0000054554Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

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

ArrayExpressiQ7Z4W1.
BgeeiQ7Z4W1.
CleanExiHS_DCXR.
GenevestigatoriQ7Z4W1.

Organism-specific databases

HPAiHPA023371.
HPA023863.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi119357. 4 interactions.
IntActiQ7Z4W1. 2 interactions.
STRINGi9606.ENSP00000303356.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ7Z4W1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
HOVERGENiHBG105069.
InParanoidiQ7Z4W1.
KOiK03331.
OMAiPHKAKAM.
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

MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE    50
CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF 100
DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC 150
STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM 200
LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC 244
Length:244
Mass (Da):25,913
Last modified:July 19, 2004 - v2
Checksum:iF82B7A178D46EAA5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → A in AAP97273. 1 Publication
Sequence conflicti239 – 2391G → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi50400451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11799.1.
RefSeqi NP_001182147.1. NM_001195218.1.
NP_057370.1. NM_016286.3.
UniGenei Hs.9857.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PR9 X-ray 1.96 A/B 1-244 [» ]
1WNT X-ray 2.30 A/B/C/D 1-244 [» ]
3D3W X-ray 1.87 A/B 1-244 [» ]
ProteinModelPortali Q7Z4W1.
SMRi Q7Z4W1. Positions 1-244.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119357. 4 interactions.
IntActi Q7Z4W1. 2 interactions.
STRINGi 9606.ENSP00000303356.

Chemistry

ChEMBLi CHEMBL2314.

PTM databases

PhosphoSitei Q7Z4W1.

Polymorphism databases

DMDMi 50400451.

2D gel databases

REPRODUCTION-2DPAGE IPI00448095.

Proteomic databases

MaxQBi Q7Z4W1.
PaxDbi Q7Z4W1.
PRIDEi Q7Z4W1.

Protocols and materials databases

DNASUi 51181.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306869 ; ENSP00000303356 ; ENSG00000169738 .
GeneIDi 51181.
KEGGi hsa:51181.
UCSCi uc002kdg.3. human.

Organism-specific databases

CTDi 51181.
GeneCardsi GC17M079993.
HGNCi HGNC:18985. DCXR.
HPAi HPA023371.
HPA023863.
MIMi 260800. phenotype.
608347. gene.
neXtProti NX_Q7Z4W1.
Orphaneti 2843. Pentosuria.
PharmGKBi PA38772.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1028.
HOVERGENi HBG105069.
InParanoidi Q7Z4W1.
KOi K03331.
OMAi PHKAKAM.
PhylomeDBi Q7Z4W1.
TreeFami TF313841.

Enzyme and pathway databases

BRENDAi 1.1.1.10. 2681.
SABIO-RK Q7Z4W1.

Miscellaneous databases

ChiTaRSi DCXR. human.
EvolutionaryTracei Q7Z4W1.
GenomeRNAii 51181.
NextBioi 54147.
PROi Q7Z4W1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7Z4W1.
Bgeei Q7Z4W1.
CleanExi HS_DCXR.
Genevestigatori Q7Z4W1.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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).
  15. "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: September 3, 2014
This is version 114 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

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