NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
STRAIN=Hartley;
TISSUE=Liver;
DOI=10.1074/jbc.M110703200; PubMed=11882650 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

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.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By similarity). Note=Probably recruited to membranes via an interaction with phosphatidylinositol (By similarity).
TISSUE SPECIFICITY: Highly expressed in kidney and liver. Expressed in epididymis. Expressed at intermediate level in lung. Weakly expressed in brain, heart, spleen and testis.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB061720; BAB64341.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08074; 1CYD. [HSSP ENTRY / PDB]

SMR

Q920N9; 1-243.

ModBase

Q920N9.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

BLOCKS

Q920N9.

Phylogenomic databases

HOVERGEN

Q920N9; -.

Other

ProtoNet

Q920N9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Glucose metabolism; Membrane; NADP; Oxidoreductase; Phosphoprotein; Xylose metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 244`	`244`	`L-xylulose reductase.`	`PRO_0000054553`
`NP_BIND`	`11 39`	`29`	`NADP (By similarity).`
`ACT_SITE`	`149 149`		`Proton acceptor (By similarity).`
`ACT_SITE`	`153 153`		`By similarity.`
`BINDING`	`136 136`		`Substrate (By similarity).`
`MOD_RES`	`149 149`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 25750 Da [This is the MW of the unprocessed precursor]

CRC64: C7AE9AE263C59B5A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD 

        70         80         90        100        110        120 
LADWEATEQA LSNVGPADLL VNNAAVALLQ PFLEVTKEAC VTSFNVNLRA VIQVSQIVAK 

       130        140        150        160        170        180 
GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALYMLT KMMALELGPH KIRVNAVNPT 

       190        200        210        220        230        240 
VVMTPMGRTN WSDPHKAKAM LDRIPLGKFA EVENVVDTIL FLLSNRSGMT TGSTLPVDGG 


FLAT

Q920N9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools