DCXR_RAT
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 03-AUG-2022, entry version 128.
DE RecName: Full=L-xylulose reductase;
DE Short=XR;
DE EC=1.1.1.10 {ECO:0000269|PubMed:11882650, ECO:0000269|PubMed:12604240, ECO:0000269|PubMed:21477590};
DE AltName: Full=Dicarbonyl/L-xylulose reductase;
GN Name=Dcxr; Synonyms=Glb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC 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., 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).
RN [2]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-136; GLN-137; LEU-143; HIS-146;
RP TYR-149; LYS-153; 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 recognition of
RT L-xylulose reductase by site-directed mutagenesis.";
RL Chem. Biol. Interact. 143:543-550(2003).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21477590; DOI=10.1016/j.febslet.2011.03.062;
RA Son L.T., Ko K.M., Cho J.H., Singaravelu G., Chatterjee I., Choi T.W.,
RA Song H.O., Yu J.R., Park B.J., Lee S.K., Ahnn J.;
RT "DHS-21, a dicarbonyl/L-xylulose reductase (DCXR) ortholog, regulates
RT longevity and reproduction in Caenorhabditis elegans.";
RL FEBS Lett. 585:1310-1316(2011).
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, ECO:0000269|PubMed:12604240,
CC ECO:0000269|PubMed:21477590};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for L-xylulose (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21477590};
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. Weakly or not
CC expressed in brain, heart, lung, spleen, epididymis and testis.
CC {ECO:0000269|PubMed:11882650}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB061719; BAB64340.1; -; mRNA.
DR RefSeq; NP_599214.1; NM_134387.1.
DR RefSeq; XP_008766687.1; XM_008768465.2.
DR AlphaFoldDB; Q920P0; -.
DR SMR; Q920P0; -.
DR IntAct; Q920P0; 1.
DR STRING; 10116.ENSRNOP00000064161; -.
DR iPTMnet; Q920P0; -.
DR PhosphoSitePlus; Q920P0; -.
DR PaxDb; Q920P0; -.
DR PRIDE; Q920P0; -.
DR GeneID; 171408; -.
DR KEGG; rno:171408; -.
DR CTD; 51181; -.
DR RGD; 620031; Dcxr.
DR eggNOG; KOG1207; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q920P0; -.
DR OMA; GICEFKE; -.
DR OrthoDB; 1051625at2759; -.
DR PhylomeDB; Q920P0; -.
DR BRENDA; 1.1.1.10; 5301.
DR Reactome; R-RNO-5661270; Formation of xylulose-5-phosphate.
DR SABIO-RK; Q920P0; -.
DR PRO; PR:Q920P0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000050315; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; Q920P0; baseline and differential.
DR Genevisible; Q920P0; RN.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; ISO:RGD.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; ISO:RGD.
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:0006739; P:NADP metabolic process; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
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 1: Evidence at protein 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_0000054557"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT ACT_SITE 153
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"
FT MUTAGEN 136
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 137
FT /note="Q->M: Slightly reduced activity. Loss of activity
FT for sugars; when associated with F-143 and L-146."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 143
FT /note="L->F: Slightly reduced activity. Loss of activity
FT for sugars; when associated with M-137 and L-146."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 146
FT /note="H->L: Slightly reduced activity. Loss of activity
FT for sugars; when associated with M-137; F-143 and L-146."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 149
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 153
FT /note="K->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 190
FT /note="N->V: Slightly reduced activity. Loss of activity
FT for sugars; when associated with S-191."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 191
FT /note="W->F: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:12604240"
FT MUTAGEN 191
FT /note="W->S: Slightly reduced activity. Loss of activity
FT for sugars; when associated with V-190."
FT /evidence="ECO:0000269|PubMed:12604240"
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
