[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-169; 172-184 AND 199-223, HOMOTETRAMERIZATION, AND TISSUE SPECIFICITY. DOI=10.1016/S0009-2797(00)00315-X; PubMed=11306103 [NCBI, ExPASy, EBI, Israel, Japan] 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; 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).
[3]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1002/(SICI)1098-2795(199902)52:2<225::AID-MRD14>3.0.CO;2-M; PubMed=9890754 [NCBI, ExPASy, EBI, Israel, Japan] 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).

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. Acrosome. 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.
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

AB045204; BAB61727.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08074; 1CYD. [HSSP ENTRY / PDB]

SMR

Q91XV4; 1-241.

ModBase

Q91XV4.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13240; -.

Ontologies

GO:0001669;	Cellular component: acrosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0050038;	Molecular function: L-xylulose reductase activity (inferred from electronic annotation from EC).
GO:0042732;	Biological process: D-xylose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

Q91XV4.

Phylogenomic databases

HOVERGEN

Q91XV4; -.

Other

UniRef

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

Keywords

Carbohydrate metabolism; Direct protein sequencing; 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_0000054555`
`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: 25675 Da [This is the MW of the unprocessed precursor]

CRC64: 76F7EC25BAA56D01 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLGLAGRRA LVTGAGKGIG RSTVLALQAA GAHVVAVSRT QADLDSLVSE CPGVETVCVD 

        70         80         90        100        110        120 
LADWEATEQA LSSVGPVDLL VNNAAVALLQ PFLEVTKEAF DMSFNVNLRA VIQVSQIVAR 

       130        140        150        160        170        180 
GMIARGAPGA IVNVSSQASQ RALANHSVYC STKGALDMLT KMMALELGPH KIRVNAVNPT 

       190        200        210        220        230        240 
VVMTSMGRTN WSDPHKAKVM LDRIPLGKFA EVENVVDAIL FLLSHRSNMT TGSTLPVDGG 


FLVT

Q91XV4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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