Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7Z4W1

- DCXR_HUMAN

UniProt

Q7Z4W1 - DCXR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 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

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

GO - Biological processi

  1. D-xylose metabolic process Source: UniProtKB-KW
  2. glucose metabolic process Source: UniProtKB
  3. NADP metabolic process Source: Ensembl
  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 By similarity; 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: UniProtKB
  4. membrane Source: UniProtKB-KW
  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.3 Publications
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 reductasePRO_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

BgeeiQ7Z4W1.
CleanExiHS_DCXR.
ExpressionAtlasiQ7Z4W1. baseline and differential.
GenevestigatoriQ7Z4W1.

Organism-specific databases

HPAiHPA023371.
HPA023863.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi119357. 6 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.
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

        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. 1 PublicationCurated
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.

Polymorphism databases

DMDMi50400451.

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 .
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119357. 6 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.
GeneTreei ENSGT00760000118868.
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

Bgeei Q7Z4W1.
CleanExi HS_DCXR.
ExpressionAtlasi Q7Z4W1. baseline and differential.
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: November 26, 2014
This is version 117 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