ID   DCXR_CAVPO              Reviewed;         244 AA.
AC   Q920N9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=L-xylulose reductase;
DE            Short=XR;
DE            EC=1.1.1.10;
DE   AltName: Full=Dicarbonyl/L-xylulose reductase;
DE   AltName: Full=Protein P26h;
GN   Name=DCXR; Synonyms=GLB;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=Hartley; TISSUE=Liver;
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).
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}. Note=Probably recruited to membranes via an
CC       interaction with phosphatidylinositol. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney and liver. Expressed in
CC       epididymis. Expressed at intermediate level in lung. Weakly expressed
CC       in 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; AB061720; BAB64341.1; -; mRNA.
DR   RefSeq; NP_001166413.1; NM_001172942.1.
DR   AlphaFoldDB; Q920N9; -.
DR   SMR; Q920N9; -.
DR   GeneID; 100712804; -.
DR   CTD; 51181; -.
DR   InParanoid; Q920N9; -.
DR   BRENDA; 1.1.1.10; 1225.
DR   SABIO-RK; Q920N9; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
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:0005997; P:xylulose metabolic process; IDA:UniProtKB.
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; Reference proteome; Xylose metabolism.
FT   CHAIN           1..244
FT                   /note="L-xylulose reductase"
FT                   /id="PRO_0000054553"
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"
SQ   SEQUENCE   244 AA;  25750 MW;  C7AE9AE263C59B5A CRC64;
     MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD
     LADWEATEQA LSNVGPADLL VNNAAVALLQ PFLEVTKEAC VTSFNVNLRA VIQVSQIVAK
     GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALYMLT KMMALELGPH KIRVNAVNPT
     VVMTPMGRTN WSDPHKAKAM LDRIPLGKFA EVENVVDTIL FLLSNRSGMT TGSTLPVDGG
     FLAT