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   25-NOV-2008, entry version 51.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; 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.,
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   [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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(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). Apical cell membrane; Peripheral membrane protein.
CC       Note=Probably recruited to membranes via an interaction with
CC       phosphatidylinositol (By similarity). In kidney, it is localized
CC       in the brush border membranes of proximal tubular cells.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and
CC       epididymis. Expressed at intermediate level in lung. Weakly or not
CC       expressed in brain, heart, spleen and testis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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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   RefSeq; NP_080704.2; -.
DR   UniGene; Mm.231091; -.
DR   HSSP; P08074; 1CYD.
DR   SMR; Q91X52; 1-243.
DR   PhosphoSite; Q91X52; -.
DR   REPRODUCTION-2DPAGE; Q91X52; -.
DR   Ensembl; ENSMUSG00000039450; Mus musculus.
DR   GeneID; 67880; -.
DR   KEGG; mmu:67880; -.
DR   MGI; MGI:1915130; Dcxr.
DR   HOGENOM; Q91X52; -.
DR   HOVERGEN; Q91X52; -.
DR   NextBio; 325821; -.
DR   ArrayExpress; Q91X52; -.
DR   CleanEx; MM_DCXR; -.
DR   GermOnline; ENSMUSG00000039450; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005903; C:brush border; IDA:MGI.
DR   GO; GO:0005902; C:microvillus; IDA:MGI.
DR   GO; GO:0050038; F:L-xylulose reductase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006739; P:NADP metabolic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0005997; P:xylulose metabolic process; IDA:MGI.
DR   InterPro; IPR002198; DHase_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell membrane; Glucose metabolism; Membrane;
KW   NADP; Oxidoreductase; Phosphoprotein; Xylose metabolism.
FT   CHAIN         1    244       L-xylulose reductase.
FT                                /FTId=PRO_0000054556.
FT   NP_BIND      11     39       NADP (By similarity).
FT   ACT_SITE    149    149       Proton acceptor (By similarity).
FT   ACT_SITE    153    153       By similarity.
FT   BINDING     136    136       Substrate (By similarity).
FT   MOD_RES     149    149       Phosphotyrosine (By similarity).
FT   CONFLICT    127    127       V -> N (in Ref. 3; AAH12247).
FT   CONFLICT    133    135       NVS -> KKY (in Ref. 3; AAH12247).
FT   CONFLICT    157    158       DM -> FL (in Ref. 3; AAH12247).
FT   CONFLICT    162    162       M -> R (in Ref. 3; AAH12247).
FT   CONFLICT    172    172       I -> S (in Ref. 3; AAH12247).
FT   CONFLICT    184    184       T -> R (in Ref. 3; AAH12247).
FT   CONFLICT    202    203       DR -> ES (in Ref. 3; AAH12247).
FT   CONFLICT    224    224       S -> G (in Ref. 2; BAB23131).
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
//