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L-xylulose reductase (XR) (EC 1.1.1.10) (Dicarbonyl/L-xylulose reductase) (Sperm antigen P26h)

 DCXR_MESAU              Reviewed;         244 AA.
Q91XV4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
20-JUN-2018, entry version 85.
RecName: Full=L-xylulose reductase;
Short=XR;
EC=1.1.1.10;
AltName: Full=Dicarbonyl/L-xylulose reductase;
AltName: Full=Sperm antigen P26h;
Name=DCXR;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-169; 172-184 AND
199-223, HOMOTETRAMERIZATION, AND TISSUE SPECIFICITY.
PubMed=11306103; DOI=10.1016/S0009-2797(00)00315-X;
Ishikura S., Isaji T., Usami N., Kitahara K., Nakagawa J., Hara A.;
"Molecular cloning, expression and tissue distribution of hamster
diacetyl reductase. Identity with L-xylulose reductase.";
Chem. Biol. Interact. 130:879-889(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
STRAIN=Syrian; TISSUE=Liver;
PubMed=11882650; DOI=10.1074/jbc.M110703200;
Nakagawa J., Ishikura S., Asami J., Isaji T., Usami N., Hara A.,
Sakurai T., Tsuritani K., Oda K., Takahashi M., Yoshimoto M.,
Otsuka N., Kitamura K.;
"Molecular characterization of mammalian dicarbonyl/L-xylulose
reductase and its localization in kidney.";
J. Biol. Chem. 277:17883-17891(2002).
[3]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9890754;
DOI=10.1002/(SICI)1098-2795(199902)52:2<225::AID-MRD14>3.0.CO;2-M;
Legare C., Berube B., Boue F., Lefievre L., Morales C.R., El-Alfy M.,
Sullivan R.;
"Hamster sperm antigen P26h is a phosphatidylinositol-anchored
protein.";
Mol. Reprod. Dev. 52:225-233(1999).
-!- FUNCTION: Catalyzes the NADPH-dependent reduction of several
pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-
xylulose. Participates in the uronate cycle of glucose metabolism.
May play a role in the water absorption and cellular
osmoregulation in the proximal renal tubules by producing xylitol,
an osmolyte, thereby preventing osmolytic stress from occurring in
the renal tubules.
-!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH.
{ECO:0000269|PubMed:11882650}.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9890754};
Peripheral membrane protein {ECO:0000269|PubMed:9890754}.
Cytoplasmic vesicle, secretory vesicle, acrosome
{ECO:0000269|PubMed:9890754}. Note=Probably recruited to membranes
via an interaction with phosphatidylinositol. During epididymal
transit, it accumulates on the acrosomal cap of spermatozoa.
-!- TISSUE SPECIFICITY: Highly expressed in kidney and liver.
Expressed in epididymis. Weakly expressed in brain, heart, lung,
spleen and testis. {ECO:0000269|PubMed:11306103,
ECO:0000269|PubMed:11882650, ECO:0000269|PubMed:9890754}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; AB045204; BAB61727.1; -; mRNA.
RefSeq; NP_001268340.1; NM_001281411.1.
ProteinModelPortal; Q91XV4; -.
SMR; Q91XV4; -.
GeneID; 101835313; -.
CTD; 51181; -.
HOVERGEN; HBG105069; -.
OrthoDB; EOG091G0GV2; -.
BioCyc; MetaCyc:MONOMER-13240; -.
BRENDA; 1.1.1.10; 3239.
SABIO-RK; Q91XV4; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005903; C:brush border; IEA:Ensembl.
GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0044105; F:L-xylulose reductase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:Ensembl.
GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0005997; P:xylulose metabolic process; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Acetylation; Carbohydrate metabolism; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Glucose metabolism;
Membrane; Methylation; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome; Xylose metabolism.
CHAIN 1 244 L-xylulose reductase.
/FTId=PRO_0000054555.
NP_BIND 11 39 NADP. {ECO:0000250}.
ACT_SITE 149 149 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
ACT_SITE 153 153 {ECO:0000250}.
BINDING 136 136 Substrate. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q7Z4W1}.
MOD_RES 21 21 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q7Z4W1}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z4W1}.
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


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