ID   DCXR_BOVIN              Reviewed;         244 AA.
AC   Q1JP75;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Note=Probably recruited to membranes via an
CC       interaction with phosphatidylinositol (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; BT025479; ABF57435.1; -; mRNA.
DR   IPI; IPI00685459; -.
DR   RefSeq; NP_001069359.1; -.
DR   RefSeq; XP_001250628.1; -.
DR   UniGene; Bt.3200; -.
DR   SMR; Q1JP75; 1-243.
DR   Ensembl; ENSBTAG00000008747; Bos taurus.
DR   GeneID; 526937; -.
DR   GeneID; 782391; -.
DR   KEGG; bta:526937; -.
DR   KEGG; bta:782391; -.
DR   HOVERGEN; Q1JP75; -.
DR   BRENDA; 1.1.1.10; 251.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glucose metabolism; Membrane; NADP;
KW   Oxidoreductase; Phosphoprotein; Xylose metabolism.
FT   CHAIN         1    244       L-xylulose reductase.
FT                                /FTId=PRO_0000259351.
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).
SQ   SEQUENCE   244 AA;  25650 MW;  DFDB13119181BA6E CRC64;
     MDLRLAGRRA LVTGAGKGIG RSIVKALHAA GARVVAVSRT QADLDSLVRE CPGVETVCVD
     LADWEATEQA LGGVGPVDLL VNNAAVAFLQ PFLEVTKEAY DMSFSVNLRA VIQVSQIVAR
     GLIARGAPGV IVNVSSQASQ RGLTNHSVYC STKGALDTLT KVMAVELGPH KIRVNAVNPT
     VVMTPMGQAA WSDPQKAKAM LDRIPLGRFA EVENVVDTIL FLLSDRSSMT TGSTVPVDGG
     FLAT
//