ID   DCXR_RAT                Reviewed;         244 AA.
AC   Q920P0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 47.
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; Synonyms=Glb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
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   MUTAGENESIS OF SER-136; GLN-137; LEU-143; HIS-146; TYR-149; LYS-153;
RP   ASN-190 AND TRP-191.
RX   PubMed=12604240; DOI=10.1016/S0009-2797(02)00217-X;
RA   Ishikura S., Isaji T., Usami N., Nakagawa J., El-Kabbani O., Hara A.;
RT   "Identification of amino acid residues involved in substrate
RT   recognition of L-xylulose reductase by site-directed mutagenesis.";
RL   Chem. Biol. Interact. 143:543-550(2003).
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 and liver. Weakly
CC       or not expressed in brain, heart, lung, spleen, epididymis and
CC       testis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AB061719; BAB64340.1; -; mRNA.
DR   IPI; IPI00200794; -.
DR   RefSeq; NP_599214.1; -.
DR   UniGene; Rn.177518; -.
DR   HSSP; P08074; 1CYD.
DR   SMR; Q920P0; 1-243.
DR   PRIDE; Q920P0; -.
DR   GeneID; 171408; -.
DR   KEGG; rno:171408; -.
DR   RGD; 620031; Dcxr.
DR   HOVERGEN; Q920P0; -.
DR   BRENDA; 1.1.1.10; 248.
DR   NextBio; 622280; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0050038; F:L-xylulose reductase activity; IEA:EC.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Membrane; NADP;
KW   Oxidoreductase; Phosphoprotein; Xylose metabolism.
FT   CHAIN         1    244       L-xylulose reductase.
FT                                /FTId=PRO_0000054557.
FT   NP_BIND      11     39       NADP (By similarity).
FT   ACT_SITE    149    149       Proton acceptor.
FT   ACT_SITE    153    153
FT   BINDING     136    136       Substrate (By similarity).
FT   MOD_RES     149    149       Phosphotyrosine (By similarity).
FT   MUTAGEN     136    136       S->A: Loss of activity.
FT   MUTAGEN     137    137       Q->M: Slightly reduced activity. Loss of
FT                                activity for sugars; when associated with
FT                                F-143 and L-146.
FT   MUTAGEN     143    143       L->F: Slightly reduced activity. Loss of
FT                                activity for sugars; when associated with
FT                                M-137 and L-146.
FT   MUTAGEN     146    146       H->L: Slightly reduced activity. Loss of
FT                                activity for sugars; when associated with
FT                                M-137; F-143 and L-146.
FT   MUTAGEN     149    149       Y->F: Loss of activity.
FT   MUTAGEN     153    153       K->M: Loss of activity.
FT   MUTAGEN     190    190       N->V: Slightly reduced activity. Loss of
FT                                activity for sugars; when associated with
FT                                S-191.
FT   MUTAGEN     191    191       W->F: Slightly reduced activity.
FT   MUTAGEN     191    191       W->S: Slightly reduced activity. Loss of
FT                                activity for sugars; when associated with
FT                                V-190.
SQ   SEQUENCE   244 AA;  25720 MW;  7BAEE7E7BB404057 CRC64;
     MDLGLAGRRA LVTGAGKGIG RSTVLALQAA GAQVVAVSRT REDLDSLVRE CPGVEPVCVD
     LADWEATEQA LSNVGPVDLL VNNAAVATLQ PFLEVTKEAC DTSFNVNFRA VVQVSQIVAR
     GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALDMLT KVMALELGPH KIRVNAVNPT
     VVMTPMGRAN WSDPHKAKVM LDRIPLGKFA EVENVVDTIL FLLSNRSSMT TGSALPVDGG
     FLAT
//