DCXR_MOUSE
ID DCXR_MOUSE Reviewed; 244 AA.
AC Q91X52; Q3U5L5; Q9D129; Q9D8W1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=L-xylulose reductase;
DE Short=XR;
DE EC=1.1.1.10;
DE AltName: Full=Dicarbonyl/L-xylulose reductase;
GN Name=Dcxr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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., Otsuka N.,
RA Kitamura K.;
RT "Molecular characterization of mammalian dicarbonyl/L-xylulose reductase
RT and its localization in kidney.";
RL J. Biol. Chem. 277:17883-17891(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of several pentoses,
CC tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose.
CC Participates in the uronate cycle of glucose metabolism. May play a
CC role in the water absorption and cellular osmoregulation in the
CC proximal renal tubules by producing xylitol, an osmolyte, thereby
CC preventing osmolytic stress from occurring in the renal tubules.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + xylitol = H(+) + L-xylulose + NADPH;
CC Xref=Rhea:RHEA:17025, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.10;
CC Evidence={ECO:0000269|PubMed:11882650};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Apical cell membrane
CC {ECO:0000269|PubMed:11882650}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11882650}. Note=Probably recruited to membranes via
CC an interaction with phosphatidylinositol (By similarity). In kidney, it
CC is localized in the brush border membranes of proximal tubular cells.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and epididymis.
CC Expressed at intermediate level in lung. Weakly or not expressed in
CC brain, heart, spleen and testis. {ECO:0000269|PubMed:11882650}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; D89656; BAB88678.1; -; mRNA.
DR EMBL; AK004023; BAB23131.1; -; mRNA.
DR EMBL; AK007627; BAB25146.1; -; mRNA.
DR EMBL; AK153521; BAE32063.1; -; mRNA.
DR EMBL; BC012247; AAH12247.1; -; mRNA.
DR CCDS; CCDS25755.1; -.
DR RefSeq; NP_080704.2; NM_026428.2.
DR AlphaFoldDB; Q91X52; -.
DR SMR; Q91X52; -.
DR STRING; 10090.ENSMUSP00000026144; -.
DR iPTMnet; Q91X52; -.
DR PhosphoSitePlus; Q91X52; -.
DR SwissPalm; Q91X52; -.
DR REPRODUCTION-2DPAGE; Q91X52; -.
DR EPD; Q91X52; -.
DR jPOST; Q91X52; -.
DR MaxQB; Q91X52; -.
DR PaxDb; Q91X52; -.
DR PeptideAtlas; Q91X52; -.
DR PRIDE; Q91X52; -.
DR ProteomicsDB; 279318; -.
DR Antibodypedia; 19868; 351 antibodies from 33 providers.
DR DNASU; 67880; -.
DR Ensembl; ENSMUST00000026144; ENSMUSP00000026144; ENSMUSG00000039450.
DR GeneID; 67880; -.
DR KEGG; mmu:67880; -.
DR UCSC; uc007muh.1; mouse.
DR CTD; 51181; -.
DR MGI; MGI:1915130; Dcxr.
DR VEuPathDB; HostDB:ENSMUSG00000039450; -.
DR eggNOG; KOG1207; Eukaryota.
DR GeneTree; ENSGT00940000154873; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q91X52; -.
DR OMA; GICEFKE; -.
DR OrthoDB; 1051625at2759; -.
DR PhylomeDB; Q91X52; -.
DR TreeFam; TF313841; -.
DR BRENDA; 1.1.1.10; 3474.
DR Reactome; R-MMU-5661270; Formation of xylulose-5-phosphate.
DR SABIO-RK; Q91X52; -.
DR BioGRID-ORCS; 67880; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dcxr; mouse.
DR PRO; PR:Q91X52; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91X52; protein.
DR Bgee; ENSMUSG00000039450; Expressed in right kidney and 218 other tissues.
DR ExpressionAtlas; Q91X52; baseline and differential.
DR Genevisible; Q91X52; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IDA:MGI.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; ISO:MGI.
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:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IDA:MGI.
DR GO; GO:0006739; P:NADP metabolic process; IDA:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0005997; P:xylulose metabolic process; IDA:MGI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cell membrane; Glucose metabolism;
KW Membrane; Methylation; NADP; Oxidoreductase; Reference proteome;
KW Xylose metabolism.
FT CHAIN 1..244
FT /note="L-xylulose reductase"
FT /id="PRO_0000054556"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT BINDING 11..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT MOD_RES 21
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT CONFLICT 127
FT /note="V -> N (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..135
FT /note="NVS -> KKY (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="DM -> FL (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="M -> R (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="I -> S (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="T -> R (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="DR -> ES (in Ref. 3; AAH12247)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> G (in Ref. 2; BAB23131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 25746 MW; 9701111544053820 CRC64;
MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD
LADWEATEQA LSNVGPVDLL VNNAAVALLQ PFLEVTKEAC DTSFNVNLRA VIQVSQIVAK
GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALDMLT KMMALELGPH KIRVNAVNPT
VVMTPMGRTN WSDPHKAKAM LDRIPLGKFA EVENVVDTIL FLLSNRSGMT TGSTLPVDGG
FLAT
