[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.273.39.25117; PubMed=9737970 [NCBI, ExPASy, EBI, Israel, Japan] Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.; "Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes."; J. Biol. Chem. 273:25117-25124(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473 AND THR-474, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).

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

AF061017; AAC36096.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006749; AAH06749.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_033492.1; -.

UniGene

Mm.344831

3D structure databases

ModBase

O70475.

PTM databases

PhosphoSite

O70475; -.

Organism-specific databases

MGI

MGI:1306785; Ugdh.

Gene expression databases

ArrayExpress

O70475; -.

CleanEx

MM_UGDH; -.

GermOnline

ENSMUSG00000029201; Mus musculus.

Ontologies

GO:0001702;	Biological process: gastrulation with mouth forming second (inferred from mutant phenotype from MGI).
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.

BLOCKS

O70475.

Genome annotation databases

Ensembl

ENSMUSG00000029201; Mus musculus. [Contig view]

GeneID

22235; -.

KEGG

mmu:22235; -.

Phylogenomic databases

HOGENOM

O70475; -.

HOVERGEN

O70475; -.

Other

Ugdh; Mus musculus.

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_0000074061`
`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.`
`MOD_RES`	`474 474`		`Phosphothreonine.`

Sequence information

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

Molecular weight: 54832 Da [This is the MW of the unprocessed precursor]

CRC64: C6234F3C1D7480C7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVEIKKICCI GAGYVGGPTC SVIAHMCPEI 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 
GGDETPEGQK AVRALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD 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 KMLKPAFIFD GRRVLDGLHS ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK 

       490 
FSLQDPPNKK PKV

O70475 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