Full text data of DCXR
DCXR
[Confidence: low (only semi-automatic identification from reviews)]
L-xylulose reductase; XR; 1.1.1.10 (Carbonyl reductase II; Dicarbonyl/L-xylulose reductase; Kidney dicarbonyl reductase; kiDCR; Sperm surface protein P34H)
L-xylulose reductase; XR; 1.1.1.10 (Carbonyl reductase II; Dicarbonyl/L-xylulose reductase; Kidney dicarbonyl reductase; kiDCR; Sperm surface protein P34H)
UniProt
Q7Z4W1
ID DCXR_HUMAN Reviewed; 244 AA.
AC Q7Z4W1; Q9BTZ3; Q9UHY9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2004, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=L-xylulose reductase;
DE Short=XR;
DE EC=1.1.1.10;
DE AltName: Full=Carbonyl reductase II;
DE AltName: Full=Dicarbonyl/L-xylulose reductase;
DE AltName: Full=Kidney dicarbonyl reductase;
DE Short=kiDCR;
DE AltName: Full=Sperm surface protein P34H;
GN Name=DCXR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Epididymis;
RX PubMed=10385429; DOI=10.1210/en.140.7.3318;
RA Legare C., Gaudreault C., St Jacques S., Sullivan R.;
RT "P34H sperm protein is preferentially expressed by the human corpus
RT epididymidis.";
RL Endocrinology 140:3318-3327(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, AND
RP INVOLVEMENT IN PENTOSURIA.
RX PubMed=11882650; DOI=10.1074/jbc.M110703200;
RA Nakagawa J., Ishikura S., Asami J., Isaji T., Usami N., Hara A.,
RA Sakurai T., Tsuritani K., Oda K., Takahashi M., Yoshimoto M.,
RA Otsuka N., Kitamura K.;
RT "Molecular characterization of mammalian dicarbonyl/L-xylulose
RT reductase and its localization in kidney.";
RL J. Biol. Chem. 277:17883-17891(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis, Liver, and Testis;
RX PubMed=12680326;
RA Xia X.Y., Xu X.F., Gao Y., Huang Y.F.;
RT "Molecular cloning of human sperm surface protein P34H gene and semi-
RT quantitative analysis of its expression in testis and epididymidis.";
RL Zhonghua Nan Ke Xue 9:24-27(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Huang C., Li Y., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Zhang C.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Q., Yu L., Zhao S.Y.;
RT "Cloning and characterization of a new human cDNA of carbonyl
RT reductase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP POSSIBLE INVOLVEMENT IN PENTOSURIA.
RX PubMed=4392213; DOI=10.1056/NEJM197004162821604;
RA Wang Y.M., Van Eys J.;
RT "The enzymatic defect in essential pentosuria.";
RL N. Engl. J. Med. 282:892-896(1970).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
RX PubMed=12136162; DOI=10.1107/S0907444902008156;
RA El-Kabbani O., Chung R.P.-T., Ishikura S., Usami N., Nakagawa J.,
RA Hara A.;
RT "Crystallization and preliminary crystallographic analysis of human L-
RT xylulose reductase.";
RL Acta Crystallogr. D 58:1379-1380(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH NADP AND
RP SUBSTRATE, AND MUTAGENESIS OF ASN-107.
RX PubMed=15103634; DOI=10.1002/prot.20047;
RA El-Kabbani O., Ishikura S., Darmanin C., Carbone V., Chung R.P.-T.,
RA Usami N., Hara A.;
RT "Crystal structure of human L-xylulose reductase holoenzyme: probing
RT the role of Asn107 with site-directed mutagenesis.";
RL Proteins 55:724-732(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of several
CC pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-
CC xylulose. Participates in the uronate cycle of glucose metabolism.
CC May play a role in the water absorption and cellular
CC osmoregulation in the proximal renal tubules by producing xylitol,
CC an osmolyte, thereby preventing osmolytic stress from occurring in
CC the renal tubules.
CC -!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity). Note=Probably recruited to membranes via an
CC interaction with phosphatidylinositol (By similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and
CC epididymis. In the epididymis, it is mainly expressed in the
CC proximal and distal sections of the corpus region. Weakly or not
CC expressed in brain, lung, heart, spleen and testis.
CC -!- DISEASE: Note=The enzyme defect in pentosuria has been shown to
CC involve L-xylulose reductase. Essential pentosuria is an inborn
CC error of metabolism characterized by the excessive urinary
CC excretion of the pentose L-xylulose.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB013846; BAB64299.1; -; mRNA.
DR EMBL; AF515623; AAN59786.1; -; mRNA.
DR EMBL; AF515624; AAO15991.1; -; mRNA.
DR EMBL; AF515625; AAM54026.1; -; mRNA.
DR EMBL; AF113123; AAF14864.1; -; mRNA.
DR EMBL; AF139841; AAP97273.1; -; mRNA.
DR EMBL; BT006881; AAP35527.1; -; mRNA.
DR EMBL; BC001470; AAH01470.1; -; mRNA.
DR EMBL; BC003018; AAH03018.1; -; mRNA.
DR RefSeq; NP_001182147.1; NM_001195218.1.
DR RefSeq; NP_057370.1; NM_016286.3.
DR UniGene; Hs.9857; -.
DR PDB; 1PR9; X-ray; 1.96 A; A/B=1-244.
DR PDB; 1WNT; X-ray; 2.30 A; A/B/C/D=1-244.
DR PDB; 3D3W; X-ray; 1.87 A; A/B=1-244.
DR PDBsum; 1PR9; -.
DR PDBsum; 1WNT; -.
DR PDBsum; 3D3W; -.
DR ProteinModelPortal; Q7Z4W1; -.
DR SMR; Q7Z4W1; 1-244.
DR IntAct; Q7Z4W1; 2.
DR STRING; 9606.ENSP00000303356; -.
DR ChEMBL; CHEMBL2314; -.
DR PhosphoSite; Q7Z4W1; -.
DR DMDM; 50400451; -.
DR REPRODUCTION-2DPAGE; IPI00448095; -.
DR PaxDb; Q7Z4W1; -.
DR PRIDE; Q7Z4W1; -.
DR DNASU; 51181; -.
DR Ensembl; ENST00000306869; ENSP00000303356; ENSG00000169738.
DR GeneID; 51181; -.
DR KEGG; hsa:51181; -.
DR UCSC; uc002kdg.3; human.
DR CTD; 51181; -.
DR GeneCards; GC17M079993; -.
DR HGNC; HGNC:18985; DCXR.
DR HPA; HPA023371; -.
DR HPA; HPA023863; -.
DR MIM; 608347; gene.
DR neXtProt; NX_Q7Z4W1; -.
DR Orphanet; 2843; Pentosuria.
DR PharmGKB; PA38772; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG105069; -.
DR InParanoid; Q7Z4W1; -.
DR KO; K03331; -.
DR OMA; QRAITNH; -.
DR PhylomeDB; Q7Z4W1; -.
DR BRENDA; 1.1.1.10; 2681.
DR SABIO-RK; Q7Z4W1; -.
DR ChiTaRS; DCXR; human.
DR EvolutionaryTrace; Q7Z4W1; -.
DR GenomeRNAi; 51181; -.
DR NextBio; 54147; -.
DR PRO; PR:Q7Z4W1; -.
DR ArrayExpress; Q7Z4W1; -.
DR Bgee; Q7Z4W1; -.
DR CleanEx; HS_DCXR; -.
DR Genevestigator; Q7Z4W1; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0005997; P:xylulose metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome;
KW Direct protein sequencing; Glucose metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Xylose metabolism.
FT CHAIN 1 244 L-xylulose reductase.
FT /FTId=PRO_0000054554.
FT NP_BIND 11 40 NADP.
FT ACT_SITE 149 149 Proton acceptor.
FT BINDING 136 136 Substrate.
FT BINDING 153 153 NADP.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 107 107 N->L,D: Loss of function. Probably due to
FT defects in formation of the active site
FT and binding of coenzyme.
FT CONFLICT 118 118 V -> A (in Ref. 5; AAP97273).
FT CONFLICT 239 239 G -> R (in Ref. 1).
FT STRAND 9 14
FT HELIX 18 29
FT STRAND 33 39
FT HELIX 41 50
FT STRAND 55 58
FT HELIX 64 71
FT STRAND 79 82
FT HELIX 92 94
FT HELIX 97 107
FT HELIX 109 125
FT STRAND 129 134
FT HELIX 137 139
FT HELIX 147 167
FT HELIX 168 170
FT STRAND 172 179
FT HELIX 185 188
FT HELIX 194 201
FT HELIX 212 223
FT HELIX 225 227
FT STRAND 234 238
FT HELIX 241 243
SQ SEQUENCE 244 AA; 25913 MW; F82B7A178D46EAA5 CRC64;
MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD
LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR
GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT
VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG
FWAC
//
ID DCXR_HUMAN Reviewed; 244 AA.
AC Q7Z4W1; Q9BTZ3; Q9UHY9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2004, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=L-xylulose reductase;
DE Short=XR;
DE EC=1.1.1.10;
DE AltName: Full=Carbonyl reductase II;
DE AltName: Full=Dicarbonyl/L-xylulose reductase;
DE AltName: Full=Kidney dicarbonyl reductase;
DE Short=kiDCR;
DE AltName: Full=Sperm surface protein P34H;
GN Name=DCXR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Epididymis;
RX PubMed=10385429; DOI=10.1210/en.140.7.3318;
RA Legare C., Gaudreault C., St Jacques S., Sullivan R.;
RT "P34H sperm protein is preferentially expressed by the human corpus
RT epididymidis.";
RL Endocrinology 140:3318-3327(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, AND
RP INVOLVEMENT IN PENTOSURIA.
RX PubMed=11882650; DOI=10.1074/jbc.M110703200;
RA Nakagawa J., Ishikura S., Asami J., Isaji T., Usami N., Hara A.,
RA Sakurai T., Tsuritani K., Oda K., Takahashi M., Yoshimoto M.,
RA Otsuka N., Kitamura K.;
RT "Molecular characterization of mammalian dicarbonyl/L-xylulose
RT reductase and its localization in kidney.";
RL J. Biol. Chem. 277:17883-17891(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis, Liver, and Testis;
RX PubMed=12680326;
RA Xia X.Y., Xu X.F., Gao Y., Huang Y.F.;
RT "Molecular cloning of human sperm surface protein P34H gene and semi-
RT quantitative analysis of its expression in testis and epididymidis.";
RL Zhonghua Nan Ke Xue 9:24-27(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Huang C., Li Y., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Zhang C.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Q., Yu L., Zhao S.Y.;
RT "Cloning and characterization of a new human cDNA of carbonyl
RT reductase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP POSSIBLE INVOLVEMENT IN PENTOSURIA.
RX PubMed=4392213; DOI=10.1056/NEJM197004162821604;
RA Wang Y.M., Van Eys J.;
RT "The enzymatic defect in essential pentosuria.";
RL N. Engl. J. Med. 282:892-896(1970).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
RX PubMed=12136162; DOI=10.1107/S0907444902008156;
RA El-Kabbani O., Chung R.P.-T., Ishikura S., Usami N., Nakagawa J.,
RA Hara A.;
RT "Crystallization and preliminary crystallographic analysis of human L-
RT xylulose reductase.";
RL Acta Crystallogr. D 58:1379-1380(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH NADP AND
RP SUBSTRATE, AND MUTAGENESIS OF ASN-107.
RX PubMed=15103634; DOI=10.1002/prot.20047;
RA El-Kabbani O., Ishikura S., Darmanin C., Carbone V., Chung R.P.-T.,
RA Usami N., Hara A.;
RT "Crystal structure of human L-xylulose reductase holoenzyme: probing
RT the role of Asn107 with site-directed mutagenesis.";
RL Proteins 55:724-732(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of several
CC pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-
CC xylulose. Participates in the uronate cycle of glucose metabolism.
CC May play a role in the water absorption and cellular
CC osmoregulation in the proximal renal tubules by producing xylitol,
CC an osmolyte, thereby preventing osmolytic stress from occurring in
CC the renal tubules.
CC -!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity). Note=Probably recruited to membranes via an
CC interaction with phosphatidylinositol (By similarity).
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and
CC epididymis. In the epididymis, it is mainly expressed in the
CC proximal and distal sections of the corpus region. Weakly or not
CC expressed in brain, lung, heart, spleen and testis.
CC -!- DISEASE: Note=The enzyme defect in pentosuria has been shown to
CC involve L-xylulose reductase. Essential pentosuria is an inborn
CC error of metabolism characterized by the excessive urinary
CC excretion of the pentose L-xylulose.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB013846; BAB64299.1; -; mRNA.
DR EMBL; AF515623; AAN59786.1; -; mRNA.
DR EMBL; AF515624; AAO15991.1; -; mRNA.
DR EMBL; AF515625; AAM54026.1; -; mRNA.
DR EMBL; AF113123; AAF14864.1; -; mRNA.
DR EMBL; AF139841; AAP97273.1; -; mRNA.
DR EMBL; BT006881; AAP35527.1; -; mRNA.
DR EMBL; BC001470; AAH01470.1; -; mRNA.
DR EMBL; BC003018; AAH03018.1; -; mRNA.
DR RefSeq; NP_001182147.1; NM_001195218.1.
DR RefSeq; NP_057370.1; NM_016286.3.
DR UniGene; Hs.9857; -.
DR PDB; 1PR9; X-ray; 1.96 A; A/B=1-244.
DR PDB; 1WNT; X-ray; 2.30 A; A/B/C/D=1-244.
DR PDB; 3D3W; X-ray; 1.87 A; A/B=1-244.
DR PDBsum; 1PR9; -.
DR PDBsum; 1WNT; -.
DR PDBsum; 3D3W; -.
DR ProteinModelPortal; Q7Z4W1; -.
DR SMR; Q7Z4W1; 1-244.
DR IntAct; Q7Z4W1; 2.
DR STRING; 9606.ENSP00000303356; -.
DR ChEMBL; CHEMBL2314; -.
DR PhosphoSite; Q7Z4W1; -.
DR DMDM; 50400451; -.
DR REPRODUCTION-2DPAGE; IPI00448095; -.
DR PaxDb; Q7Z4W1; -.
DR PRIDE; Q7Z4W1; -.
DR DNASU; 51181; -.
DR Ensembl; ENST00000306869; ENSP00000303356; ENSG00000169738.
DR GeneID; 51181; -.
DR KEGG; hsa:51181; -.
DR UCSC; uc002kdg.3; human.
DR CTD; 51181; -.
DR GeneCards; GC17M079993; -.
DR HGNC; HGNC:18985; DCXR.
DR HPA; HPA023371; -.
DR HPA; HPA023863; -.
DR MIM; 608347; gene.
DR neXtProt; NX_Q7Z4W1; -.
DR Orphanet; 2843; Pentosuria.
DR PharmGKB; PA38772; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG105069; -.
DR InParanoid; Q7Z4W1; -.
DR KO; K03331; -.
DR OMA; QRAITNH; -.
DR PhylomeDB; Q7Z4W1; -.
DR BRENDA; 1.1.1.10; 2681.
DR SABIO-RK; Q7Z4W1; -.
DR ChiTaRS; DCXR; human.
DR EvolutionaryTrace; Q7Z4W1; -.
DR GenomeRNAi; 51181; -.
DR NextBio; 54147; -.
DR PRO; PR:Q7Z4W1; -.
DR ArrayExpress; Q7Z4W1; -.
DR Bgee; Q7Z4W1; -.
DR CleanEx; HS_DCXR; -.
DR Genevestigator; Q7Z4W1; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0005997; P:xylulose metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome;
KW Direct protein sequencing; Glucose metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Xylose metabolism.
FT CHAIN 1 244 L-xylulose reductase.
FT /FTId=PRO_0000054554.
FT NP_BIND 11 40 NADP.
FT ACT_SITE 149 149 Proton acceptor.
FT BINDING 136 136 Substrate.
FT BINDING 153 153 NADP.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 107 107 N->L,D: Loss of function. Probably due to
FT defects in formation of the active site
FT and binding of coenzyme.
FT CONFLICT 118 118 V -> A (in Ref. 5; AAP97273).
FT CONFLICT 239 239 G -> R (in Ref. 1).
FT STRAND 9 14
FT HELIX 18 29
FT STRAND 33 39
FT HELIX 41 50
FT STRAND 55 58
FT HELIX 64 71
FT STRAND 79 82
FT HELIX 92 94
FT HELIX 97 107
FT HELIX 109 125
FT STRAND 129 134
FT HELIX 137 139
FT HELIX 147 167
FT HELIX 168 170
FT STRAND 172 179
FT HELIX 185 188
FT HELIX 194 201
FT HELIX 212 223
FT HELIX 225 227
FT STRAND 234 238
FT HELIX 241 243
SQ SEQUENCE 244 AA; 25913 MW; F82B7A178D46EAA5 CRC64;
MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD
LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR
GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT
VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG
FWAC
//
MIM
608347
*RECORD*
*FIELD* NO
608347
*FIELD* TI
*608347 DICARBONYL/L-XYLULOSE REDUCTASE; DCXR
;;CARBONYL REDUCTASE 2;;
DICARBONYL REDUCTASE;;
read moreDIACETYL REDUCTASE;;
L-XYLULOSE REDUCTASE;;
P34H
*FIELD* TX
DESCRIPTION
DCXR is an enzyme that has both diacetyl reductase (EC 1.1.1.5) and
L-xylulose reductase (EC 1.1.1.10) activities (Nakagawa et al., 2002).
CLONING
Using hamster P26h as probe, Legare et al. (1999) cloned DCXR, which
they designated P34H, from a human epididymis cDNA library. The deduced
244-amino acid protein has a calculated molecular mass of 26 kD. It
contains 3 N-glycosylation sites in the C-terminal region. DCXR shares
65% amino acid identity with hamster P26h and 71% similarity with pig
lung tetrameric carbonyl reductase. Northern blot analysis detected a
transcript of about 0.9 kb expressed at a high level in epididymis and
at a low level in testis. Expression was high in corpus, moderate in
caput, and low in cauda epididymis. Expression was also detected at low
levels in liver, pancreas, muscle, and lung. In situ hybridization
revealed expression predominantly in the proximal and distal sections of
the corpus epididymis, with staining restricted to the principal cells
of the epididymal epithelium.
Nakagawa et al. (2002) cloned Dcxr from a mouse glomeruli- and renal
tubule-enriched kidney cDNA library. The deduced 244-amino acid protein
has a calculated molecular mass of 25.7 kD. Using the mouse sequence as
probe, followed by RT-PCR and RACE, Nakagawa et al. (2002) cloned DCXR
from a human kidney cDNA library. The deduced protein contains 2
N-terminal consensus sequences for short-chain dehydrogenase/reductase
enzymes and several conserved residues for coenzyme binding, catalysis,
and subunit interaction. RT-PCR detected expression in all tissues
examined, with highest levels in kidney and epididymis.
GENE FUNCTION
Nakagawa et al. (2002) assayed purified recombinant human DCXR and
purified recombinant Dcxr cloned from 4 mammalian species. All DCXRs
functioned as homotetramers with NADPH-linked reductase activities for
alpha-dicarbonyl compounds, and they also catalyzed the oxidoreduction
between xylitol and L-xylulose. The DCXRs were competitively inhibited
by n-butyric acid. The diacetyl reductase activity of DCXR showed pH
dependence, with decreased activity when the pH increased from 5.8 to
9.0; about 40% maximum activity was found at pH 7.0. The substrate
specificities and kinetic constants of DCXRs for dicarbonyl compounds
and sugars were similar to those of mammalian diacetyl reductase and
L-xylulose reductase, respectively. Nakagawa et al. (2002) noted that
deficiency of L-xylulose reductase can result in pentosuria (260800).
Lane (1985) found that the red blood cells of normal individuals contain
2 L-xylulose reductase enzymes, 1 major and 1 minor. The red blood cells
from pentosurics have only 1 of these. The residual enzyme has
characteristics of the minor enzyme, which led Lane (1985) to conclude
that homozygosity for the pentosuria gene leads to loss of function of
the major enzyme.
El-Kabbani et al. (2004) studied the crystal structure of the human
L-xylulose reductase holoenzyme and, with site-directed mutagenesis,
found that the asparagine residue at codon 107 plays a critical role in
coenzyme binding rather than in the catalytic mechanism.
MAPPING
The International Radiation Mapping Consortium mapped the DCXR gene to
chromosome 17 (TMAP SHGC-31983).
*FIELD* RF
1. El-Kabbani, O.; Ishikura, S.; Darmanin, C.; Carbone, V.; Chung,
R. P.-T.; Usami, N.; Hara, A.: Crystal structure of human L-xylulose
reductase holoenzyme: probing the role of asn107 with site-directed
mutagenesis. Proteins 55: 724-732, 2004.
2. Lane, A. B.: On the nature of L-xylulose reductase deficiency
in essential pentosuria. Biochem. Genet. 23: 61-72, 1985.
3. Legare, C.; Gaudreault, C.; St-Jacques, S.; Sullivan, R.: P34H
sperm protein is preferentially expressed by the human corpus epididymidis
(sic). Endocrinology 140: 3318-3327, 1999.
4. 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.: Molecular characterization of mammalian
dicarbonyl/L-xylulose reductase and its localization in kidney. J.
Biol. Chem. 277: 17883-17891, 2002.
*FIELD* CN
Victor A. McKusick - updated: 3/17/2005
Victor A. McKusick - updated: 3/15/2005
*FIELD* CD
Patricia A. Hartz: 12/17/2003
*FIELD* ED
carol: 07/09/2009
tkritzer: 3/28/2005
terry: 3/17/2005
tkritzer: 3/16/2005
terry: 3/15/2005
mgross: 12/17/2003
*RECORD*
*FIELD* NO
608347
*FIELD* TI
*608347 DICARBONYL/L-XYLULOSE REDUCTASE; DCXR
;;CARBONYL REDUCTASE 2;;
DICARBONYL REDUCTASE;;
read moreDIACETYL REDUCTASE;;
L-XYLULOSE REDUCTASE;;
P34H
*FIELD* TX
DESCRIPTION
DCXR is an enzyme that has both diacetyl reductase (EC 1.1.1.5) and
L-xylulose reductase (EC 1.1.1.10) activities (Nakagawa et al., 2002).
CLONING
Using hamster P26h as probe, Legare et al. (1999) cloned DCXR, which
they designated P34H, from a human epididymis cDNA library. The deduced
244-amino acid protein has a calculated molecular mass of 26 kD. It
contains 3 N-glycosylation sites in the C-terminal region. DCXR shares
65% amino acid identity with hamster P26h and 71% similarity with pig
lung tetrameric carbonyl reductase. Northern blot analysis detected a
transcript of about 0.9 kb expressed at a high level in epididymis and
at a low level in testis. Expression was high in corpus, moderate in
caput, and low in cauda epididymis. Expression was also detected at low
levels in liver, pancreas, muscle, and lung. In situ hybridization
revealed expression predominantly in the proximal and distal sections of
the corpus epididymis, with staining restricted to the principal cells
of the epididymal epithelium.
Nakagawa et al. (2002) cloned Dcxr from a mouse glomeruli- and renal
tubule-enriched kidney cDNA library. The deduced 244-amino acid protein
has a calculated molecular mass of 25.7 kD. Using the mouse sequence as
probe, followed by RT-PCR and RACE, Nakagawa et al. (2002) cloned DCXR
from a human kidney cDNA library. The deduced protein contains 2
N-terminal consensus sequences for short-chain dehydrogenase/reductase
enzymes and several conserved residues for coenzyme binding, catalysis,
and subunit interaction. RT-PCR detected expression in all tissues
examined, with highest levels in kidney and epididymis.
GENE FUNCTION
Nakagawa et al. (2002) assayed purified recombinant human DCXR and
purified recombinant Dcxr cloned from 4 mammalian species. All DCXRs
functioned as homotetramers with NADPH-linked reductase activities for
alpha-dicarbonyl compounds, and they also catalyzed the oxidoreduction
between xylitol and L-xylulose. The DCXRs were competitively inhibited
by n-butyric acid. The diacetyl reductase activity of DCXR showed pH
dependence, with decreased activity when the pH increased from 5.8 to
9.0; about 40% maximum activity was found at pH 7.0. The substrate
specificities and kinetic constants of DCXRs for dicarbonyl compounds
and sugars were similar to those of mammalian diacetyl reductase and
L-xylulose reductase, respectively. Nakagawa et al. (2002) noted that
deficiency of L-xylulose reductase can result in pentosuria (260800).
Lane (1985) found that the red blood cells of normal individuals contain
2 L-xylulose reductase enzymes, 1 major and 1 minor. The red blood cells
from pentosurics have only 1 of these. The residual enzyme has
characteristics of the minor enzyme, which led Lane (1985) to conclude
that homozygosity for the pentosuria gene leads to loss of function of
the major enzyme.
El-Kabbani et al. (2004) studied the crystal structure of the human
L-xylulose reductase holoenzyme and, with site-directed mutagenesis,
found that the asparagine residue at codon 107 plays a critical role in
coenzyme binding rather than in the catalytic mechanism.
MAPPING
The International Radiation Mapping Consortium mapped the DCXR gene to
chromosome 17 (TMAP SHGC-31983).
*FIELD* RF
1. El-Kabbani, O.; Ishikura, S.; Darmanin, C.; Carbone, V.; Chung,
R. P.-T.; Usami, N.; Hara, A.: Crystal structure of human L-xylulose
reductase holoenzyme: probing the role of asn107 with site-directed
mutagenesis. Proteins 55: 724-732, 2004.
2. Lane, A. B.: On the nature of L-xylulose reductase deficiency
in essential pentosuria. Biochem. Genet. 23: 61-72, 1985.
3. Legare, C.; Gaudreault, C.; St-Jacques, S.; Sullivan, R.: P34H
sperm protein is preferentially expressed by the human corpus epididymidis
(sic). Endocrinology 140: 3318-3327, 1999.
4. 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.: Molecular characterization of mammalian
dicarbonyl/L-xylulose reductase and its localization in kidney. J.
Biol. Chem. 277: 17883-17891, 2002.
*FIELD* CN
Victor A. McKusick - updated: 3/17/2005
Victor A. McKusick - updated: 3/15/2005
*FIELD* CD
Patricia A. Hartz: 12/17/2003
*FIELD* ED
carol: 07/09/2009
tkritzer: 3/28/2005
terry: 3/17/2005
tkritzer: 3/16/2005
terry: 3/15/2005
mgross: 12/17/2003