Reviewed, UniProtKB/Swiss-Prot Q91XV4 (DCXR_MESAU)

Names and origin

Protein names

Recommended name:
    L-xylulose reductase
      Short name=XR
    EC=1.1.1.10
Alternative name(s):
    Dicarbonyl/L-xylulose reductase
    Sperm antigen P26h

Gene names

Name:

DCXR

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	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.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Xylose metabolism
Cellular component	Membrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	D-xylose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	acrosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-xylulose reductase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	L-xylulose reductase		PRO_0000054555
Regions
	Nucleotide binding	11 – 39	29	NADP By similarity
Sites
	Active site	149	1	Proton acceptor By similarity
	Active site	153	1	By similarity
	Binding site	136	1	Substrate By similarity
Amino acid modifications
	Modified residue	149	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91XV4-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 76F7EC25BAA56D01	FASTA	244	25,675
	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

References

[1]	"Molecular cloning, expression and tissue distribution of hamster diacetyl reductase. Identity with L-xylulose reductase." Ishikura S., Isaji T., Usami N., Kitahara K., Nakagawa J., Hara A. Chem. Biol. Interact. 130:879-889(2001) [PubMed: 11306103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-169; 172-184 AND 199-223, HOMOTETRAMERIZATION, TISSUE SPECIFICITY.
[2]	"Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney." 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. J. Biol. Chem. 277:17883-17891(2002) [PubMed: 11882650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY. Strain: Syrian. Tissue: Liver.
[3]	"Hamster sperm antigen P26h is a phosphatidylinositol-anchored protein." Legare C., Berube B., Boue F., Lefievre L., Morales C.R., El-Alfy M., Sullivan R. Mol. Reprod. Dev. 52:225-233(1999) [PubMed: 9890754] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB045204 mRNA. Translation: BAB61727.1.
3D structure databases
HSSP	HSSP built from PDB template 1CYD based on UniProtKB P08074.
SMR	Q91XV4. Positions 1-241.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q91XV4.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13240.
Family and domain databases
InterPro	IPR002198. DHase_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DHase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCXR_MESAU

Accession

Primary (citable) accession number: Q91XV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 1, 2001
Last modified:	November 25, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)