DCXR_MESAU
ID DCXR_MESAU Reviewed; 244 AA.
AC Q91XV4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Sperm antigen P26h;
GN Name=DCXR;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-169; 172-184 AND
RP 199-223, HOMOTETRAMERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11306103; DOI=10.1016/s0009-2797(00)00315-x;
RA Ishikura S., Isaji T., Usami N., Kitahara K., Nakagawa J., Hara A.;
RT "Molecular cloning, expression and tissue distribution of hamster diacetyl
RT reductase. Identity with L-xylulose reductase.";
RL Chem. Biol. Interact. 130:879-889(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Syrian; 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).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9890754;
RX DOI=10.1002/(sici)1098-2795(199902)52:2<225::aid-mrd14>3.0.co;2-m;
RA Legare C., Berube B., Boue F., Lefievre L., Morales C.R., El-Alfy M.,
RA Sullivan R.;
RT "Hamster sperm antigen P26h is a phosphatidylinositol-anchored protein.";
RL Mol. Reprod. Dev. 52:225-233(1999).
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:0000269|PubMed:9890754}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9890754}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome {ECO:0000269|PubMed:9890754}. Note=Probably
CC recruited to membranes via an interaction with phosphatidylinositol.
CC During epididymal transit, it accumulates on the acrosomal cap of
CC spermatozoa.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and liver. Expressed in
CC epididymis. Weakly expressed in brain, heart, lung, spleen and testis.
CC {ECO:0000269|PubMed:11306103, ECO:0000269|PubMed:11882650,
CC ECO:0000269|PubMed:9890754}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB045204; BAB61727.1; -; mRNA.
DR RefSeq; NP_001268340.1; NM_001281411.1.
DR AlphaFoldDB; Q91XV4; -.
DR SMR; Q91XV4; -.
DR STRING; 10036.XP_005069850.1; -.
DR GeneID; 101835313; -.
DR CTD; 51181; -.
DR eggNOG; KOG1207; Eukaryota.
DR OrthoDB; 1051625at2759; -.
DR BioCyc; MetaCyc:MON-13240; -.
DR BRENDA; 1.1.1.10; 3239.
DR SABIO-RK; Q91XV4; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
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; Cytoplasmic vesicle;
KW Direct protein sequencing; Glucose metabolism; Membrane; Methylation; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Xylose metabolism.
FT CHAIN 1..244
FT /note="L-xylulose reductase"
FT /id="PRO_0000054555"
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; 25675 MW; 76F7EC25BAA56D01 CRC64;
MDLGLAGRRA LVTGAGKGIG RSTVLALQAA GAHVVAVSRT QADLDSLVSE CPGVETVCVD
LADWEATEQA LSSVGPVDLL VNNAAVALLQ PFLEVTKEAF DMSFNVNLRA VIQVSQIVAR
GMIARGAPGA IVNVSSQASQ RALANHSVYC STKGALDMLT KMMALELGPH KIRVNAVNPT
VVMTSMGRTN WSDPHKAKVM LDRIPLGKFA EVENVVDAIL FLLSHRSNMT TGSTLPVDGG
FLVT
