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Q7Z4W1

- DCXR_HUMAN

UniProt

Q7Z4W1 - DCXR_HUMAN

Protein

L-xylulose reductase

Gene

DCXR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    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

    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: UniProt
    4. membrane Source: UniProtKB-SubCell
    5. microvillus Source: Ensembl
    6. nucleus Source: UniProt

    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

    ArrayExpressiQ7Z4W1.
    BgeeiQ7Z4W1.
    CleanExiHS_DCXR.
    GenevestigatoriQ7Z4W1.

    Organism-specific databases

    HPAiHPA023371.
    HPA023863.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi119357. 4 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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 115 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