Q7Z4W1 · DCXR_HUMAN
- ProteinL-xylulose reductase
- GeneDCXR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
- NADP+ + xylitol = H+ + L-xylulose + NADPH
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | brush border | |
Cellular Component | cytoplasmic microtubule | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | microvillus | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | carbonyl reductase (NADPH) activity | |
Molecular Function | identical protein binding | |
Molecular Function | L-xylulose reductase (NADPH) activity | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor | |
Biological Process | D-xylose metabolic process | |
Biological Process | glucose metabolic process | |
Biological Process | glucuronate catabolic process to xylulose 5-phosphate | |
Biological Process | NADP metabolic process | |
Biological Process | positive regulation of reactive oxygen species metabolic process | |
Biological Process | xylulose metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-xylulose reductase
- EC number
- Short namesXR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7Z4W1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: Probably recruited to membranes via an interaction with phosphatidylinositol.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pentosuria (PNTSU)
- Note
- DescriptionAn inborn error of metabolism characterized by excessive urinary excretion of L-xylulose.
- See alsoMIM:260800
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 107 | Loss of function. Probably due to defects in formation of the active site and binding of coenzyme. | ||||
Sequence: N → L or D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 318 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000054554 | 1-244 | UniProt | L-xylulose reductase | |||
Sequence: MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVDLGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVARGLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGGFWAC | |||||||
Modified residue | 21 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 46 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
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.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7Z4W1 | DCXR Q7Z4W1 | 5 | EBI-1044712, EBI-1044712 | |
BINARY | Q7Z4W1 | GLRX2 Q9NS18 | 3 | EBI-1044712, EBI-12102178 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length244
- Mass (Da)25,913
- Last updated2004-07-19 v2
- ChecksumF82B7A178D46EAA5
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 118 | in Ref. 5; AAP97273 | ||||
Sequence: V → A | ||||||
Sequence conflict | 239 | in Ref. 1 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB013846 EMBL· GenBank· DDBJ | BAB64299.1 EMBL· GenBank· DDBJ | mRNA | ||
AF515623 EMBL· GenBank· DDBJ | AAN59786.1 EMBL· GenBank· DDBJ | mRNA | ||
AF515624 EMBL· GenBank· DDBJ | AAO15991.1 EMBL· GenBank· DDBJ | mRNA | ||
AF515625 EMBL· GenBank· DDBJ | AAM54026.1 EMBL· GenBank· DDBJ | mRNA | ||
AF113123 EMBL· GenBank· DDBJ | AAF14864.1 EMBL· GenBank· DDBJ | mRNA | ||
AF139841 EMBL· GenBank· DDBJ | AAP97273.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006881 EMBL· GenBank· DDBJ | AAP35527.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001470 EMBL· GenBank· DDBJ | AAH01470.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003018 EMBL· GenBank· DDBJ | AAH03018.1 EMBL· GenBank· DDBJ | mRNA |