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   03-AUG-2022, entry version 112.
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; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   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 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 (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Probably recruited to membranes via an
CC       interaction with phosphatidylinositol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT025479; ABF57435.1; -; mRNA.
DR   RefSeq; NP_001069359.1; NM_001075891.1.
DR   AlphaFoldDB; Q1JP75; -.
DR   SMR; Q1JP75; -.
DR   PaxDb; Q1JP75; -.
DR   PeptideAtlas; Q1JP75; -.
DR   PRIDE; Q1JP75; -.
DR   Ensembl; ENSBTAT00000085766; ENSBTAP00000071030; ENSBTAG00000051698.
DR   GeneID; 526937; -.
DR   KEGG; bta:526937; -.
DR   CTD; 51181; -.
DR   VEuPathDB; HostDB:ENSBTAG00000051698; -.
DR   eggNOG; KOG1207; Eukaryota.
DR   GeneTree; ENSGT00940000154873; -.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q1JP75; -.
DR   OMA; EILVGWQ; -.
DR   OrthoDB; 1051625at2759; -.
DR   TreeFam; TF313841; -.
DR   Reactome; R-BTA-5661270; Formation of xylulose-5-phosphate.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000051698; Expressed in cortex of kidney and 94 other tissues.
DR   ExpressionAtlas; Q1JP75; baseline.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Carbohydrate metabolism; Glucose metabolism; Membrane;
KW   Methylation; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Xylose metabolism.
FT   CHAIN           1..244
FT                   /note="L-xylulose reductase"
FT                   /id="PRO_0000259351"
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   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
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