ID B3GT6_MOUSE Reviewed; 325 AA. AC Q91Z92; Q8CC93; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 05-OCT-2010, entry version 69. DE RecName: Full=Beta-1,3-galactosyltransferase 6; DE Short=Beta-1,3-GalTase 6; DE Short=Beta3Gal-T6; DE Short=Beta3GalT6; DE EC=2.4.1.134; DE AltName: Full=GAG GalTII; DE AltName: Full=Galactosyltransferase II; DE AltName: Full=Galactosylxylosylprotein 3-beta-galactosyltransferase; DE AltName: Full=UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6; GN Name=B3galt6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX MEDLINE=21611170; PubMed=11551958; DOI=10.1074/jbc.M107339200; RA Bai X., Zhou D., Brown J.R., Crawford B.E., Hennet T., Esko J.D.; RT "Biosynthesis of the linkage region of glycosaminoglycans: cloning and RT activity of galactosyltransferase II, the sixth member of the beta RT 1,3-galactosyltransferase family (beta 3GalT6)."; RL J. Biol. Chem. 276:48189-48195(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cecum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; 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). CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose CC from UDP-galactose to substrates with a terminal beta-linked CC galactose residue. Has a preference for galactose-beta-1,4-xylose CC that is found in the linker region of glycosaminoglycans, such as CC heparan sulfate and chondroitin sulfate. Has no activity towards CC substrates with terminal glucosamine or galactosamine residues (By CC similarity). CC -!- CATALYTIC ACTIVITY: UDP-galactose + 4-beta-D-galactosyl-O-beta-D- CC xylosylprotein = UDP + 3-beta-D-galactosyl-4-beta-D-galactosyl-O- CC beta-D-xylosylprotein. CC -!- COFACTOR: Manganese (By similarity). CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis. CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type CC II membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; CC Note=b3GalT6; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_459"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY050569; AAL11441.1; -; mRNA. DR EMBL; AK033608; BAC28387.1; -; mRNA. DR EMBL; AK078083; BAC37119.1; -; mRNA. DR EMBL; AK090344; BAC41178.1; -; mRNA. DR EMBL; BC082998; AAH82998.1; -; mRNA. DR IPI; IPI00130692; -. DR RefSeq; NP_536693.1; -. DR RefSeq; XP_913883.2; -. DR UniGene; Mm.347395; -. DR UniGene; Mm.440185; -. DR ProteinModelPortal; Q91Z92; -. DR CAZy; GT31; Glycosyltransferase Family 31. DR PRIDE; Q91Z92; -. DR Ensembl; ENSMUST00000052185; ENSMUSP00000057521; ENSMUSG00000050796. DR GeneID; 117592; -. DR GeneID; 634148; -. DR KEGG; mmu:117592; -. DR KEGG; mmu:634148; -. DR UCSC; uc008wfq.1; mouse. DR CTD; 117592; -. DR MGI; MGI:2152819; B3galt6. DR eggNOG; maNOG18450; -. DR HOGENOM; HBG714704; -. DR HOVERGEN; HBG050652; -. DR InParanoid; Q91Z92; -. DR OMA; KSRGCNN; -. DR OrthoDB; EOG9K0T7V; -. DR BRENDA; 2.4.1.134; 244. DR NextBio; 369698; -. DR ArrayExpress; Q91Z92; -. DR Bgee; Q91Z92; -. DR Genevestigator; Q91Z92; -. DR GermOnline; ENSMUSG00000050796; Mus musculus. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosylt...; IEA:EC. DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta...; IDA:MGI. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:MGI. DR GO; GO:0006486; P:protein amino acid glycosylation; IEA:InterPro. DR InterPro; IPR002659; Glyco_trans_31. DR PANTHER; PTHR11214; Glyco_trans_31; 1. DR Pfam; PF01762; Galactosyl_T; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; KW Membrane; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 325 Beta-1,3-galactosyltransferase 6. FT /FTId=PRO_0000219169. FT TOPO_DOM 1 11 Cytoplasmic (Potential). FT TRANSMEM 12 30 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 31 325 Lumenal (Potential). FT CARBOHYD 127 127 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 325 AA; 37021 MW; 971D2C00528169A2 CRC64; MKVFRRAWRH RVALGLGGLA FCGTTLLYLA RCASEGETPS ASGAARPRAK AFLAVLVASA PRAVERRTAV RSTWLAPERR GGPEDVWARF AVGTGGLGSE ERRALELEQA QHGDLLLLPA LRDAYENLTA KVLAMLTWLD ERVDFEFVLK ADDDSFARLD AILVDLRARE PARRRRLYWG FFSGRGRVKP GGRWREAAWQ LCDYYLPYAL GGGYVLSADL VHYLRLSREY LRAWHSEDVS LGTWLAPVDV QREHDPRFDT EYKSRGCNNQ YLVTHKQSPE DMLEKQQMLL HEGRLCKHEV QLRLSYVYDW SAPPSQCCQR KEGVP //