[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Liver; Kobayashi T., Yokota H., Yuasa A.; "cDNA cloning of rat UDP-glucose dehydrogenase."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr0503073; PubMed=16396499 [NCBI, ExPASy, EBI, Israel, Japan] Moser K., White F.M.; "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; J. Proteome Res. 5:98-104(2006).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS SPECTROMETRY. TISSUE=Kidney; DOI=10.1073/pnas.0600895103; PubMed=16641100 [NCBI, ExPASy, EBI, Israel, Japan] Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).

Comments

FUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.
CATALYTIC ACTIVITY: UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH.
PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1 .
SUBUNIT: Homohexamer (By similarity).
SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase 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

AB013732; BAA28215.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_112615.1; -.

UniGene

Rn.3967

3D structure databases

ModBase

O70199.

PTM databases

PhosphoSite

O70199; -.

Organism-specific databases

RGD

621879; Ugdh.

Gene expression databases

ArrayExpress

O70199; -.

GermOnline

ENSRNOG00000002643; Rattus norvegicus.

Ontologies

GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0003979;	Molecular function: UDP-glucose 6-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.

PANTHER

PTHR11374; UDPG_MGDP_DH_Creg; 1.

Pfam

PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.

Proteomics databases

PRIDE

O70199; -.

Genome annotation databases

Ensembl

ENSRNOG00000002643; Rattus norvegicus. [Contig view]

GeneID

83472; -.

KEGG

rno:83472; -.

Phylogenomic databases

HOVERGEN

O70199; -.

Other

615885; -.

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

Keywords

NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 493`	`493`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074062`
`NP_BIND`	`6 23`	`18`	`NAD (By similarity).`
`REGION`	`162 165`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`276 276`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`41 41`		`NAD (By similarity).`
`BINDING`	`93 93`		`NAD (By similarity).`
`BINDING`	`131 131`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`165 165`		`NAD (By similarity).`
`BINDING`	`220 220`		`Substrate (By similarity).`
`BINDING`	`273 273`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`279 279`		`NAD (By similarity).`
`BINDING`	`339 339`		`Substrate (By similarity).`
`BINDING`	`346 346`		`NAD (By similarity).`
`MOD_RES`	`473 473`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`474 474`		`Phosphothreonine.`

Sequence information

Length: 493 AA [This is the length of the unprocessed precursor]

Molecular weight: 54892 Da [This is the MW of the unprocessed precursor]

CRC64: F435D1F9AC8307EF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEIKKICCI GAGYVGGPTC SVIARMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV 

        70         80         90        100        110        120 
VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS 

       130        140        150        160        170        180 
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI 

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CESTGADVEE VATAIGMDQR IGNKFLKASV GFGGGCFQKD VLNLVYLCEA LNLPEVARYW 

       310        320        330        340        350        360 
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE 

       370        380        390        400        410        420 
GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK RMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK 

       490 
FSLQDPPNKK PKV

O70199 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