ID UGDH_MOUSE Reviewed; 493 AA. AC O70475; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JUN-2009, entry version 72. DE RecName: Full=UDP-glucose 6-dehydrogenase; DE Short=UDP-Glc dehydrogenase; DE Short=UDP-GlcDH; DE Short=UDPGDH; DE EC=1.1.1.22; GN Name=Ugdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98411308; PubMed=9737970; DOI=10.1074/jbc.273.39.25117; RA Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.; RT "Molecular cloning and characterization of the human and mouse UDP- RT glucose dehydrogenase genes."; RL J. Biol. Chem. 273:25117-25124(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473 AND THR-474, AND RP MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS RP SPECTROMETRY. RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans; CC hyaluronan, chondroitin sulfate, and heparan sulfate. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP- CC glucuronate + 2 NADH. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronic acid CC biosynthesis; UDP-glucuronic acid from UDP-glucose: step 1/1. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF061017; AAC36096.1; -; mRNA. DR EMBL; BC006749; AAH06749.1; -; mRNA. DR IPI; IPI00118344; -. DR RefSeq; NP_033492.1; -. DR UniGene; Mm.344831; -. DR PhosphoSite; O70475; -. DR PRIDE; O70475; -. DR Ensembl; ENSMUSG00000029201; Mus musculus. DR GeneID; 22235; -. DR KEGG; mmu:22235; -. DR MGI; MGI:1306785; Ugdh. DR HOGENOM; O70475; -. DR HOVERGEN; O70475; -. DR OMA; O70475; QMCPEIR. DR BRENDA; 1.1.1.22; 244. DR NextBio; 302285; -. DR ArrayExpress; O70475; -. DR Bgee; O70475; -. DR CleanEx; MM_UGDH; -. DR GermOnline; ENSMUSG00000029201; Mus musculus. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:EC. DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR017476; Nucleotide_sugar_DH. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR014028; UDP-Glc/GDP-Man_DH_dimer-bd. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1. DR PANTHER; PTHR11374; UDPG_MGDP_DH_Creg; 1. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. PE 1: Evidence at protein level; KW NAD; Oxidoreductase; Phosphoprotein. FT CHAIN 1 493 UDP-glucose 6-dehydrogenase. FT /FTId=PRO_0000074061. FT NP_BIND 6 23 NAD (By similarity). FT REGION 162 165 Substrate binding (By similarity). FT ACT_SITE 276 276 Nucleophile (By similarity). FT BINDING 36 36 NAD (By similarity). FT BINDING 41 41 NAD (By similarity). FT BINDING 93 93 NAD (By similarity). FT BINDING 131 131 NAD; via amide nitrogen (By similarity). FT BINDING 165 165 NAD (By similarity). FT BINDING 220 220 Substrate (By similarity). FT BINDING 273 273 Substrate; via amide nitrogen (By FT similarity). FT BINDING 279 279 NAD (By similarity). FT BINDING 339 339 Substrate (By similarity). FT BINDING 346 346 NAD (By similarity). FT MOD_RES 473 473 Phosphotyrosine. FT MOD_RES 474 474 Phosphothreonine. SQ SEQUENCE 493 AA; 54832 MW; C6234F3C1D7480C7 CRC64; MVEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQK AVRALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHS ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK FSLQDPPNKK PKV //