ID B3GT6_MOUSE STANDARD; PRT; 325 AA. AC Q91Z92; Q8CC93; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 05-SEP-2006, entry version 33. DE Beta-1,3-galactosyltransferase 6 (EC 2.4.1.134) (Beta 3GalT6) DE (Galactosylxylosylprotein 3-beta-galactosyltransferase) (UDP- DE Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6) DE (Galactosyltransferase II) (GAG GalTII). 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. 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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: Chondroitin sulfate and heparan sulfate synthesis. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi membrane; single-pass CC type II membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. 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 UniGene; Mm.347395; -. DR Ensembl; ENSMUSG00000050796; Mus musculus. DR MGI; MGI:2152819; B3galt6. DR ArrayExpress; Q91Z92; -. DR GO; GO:0005797; C:Golgi medial cisterna; IDA. DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta...; IDA. DR GO; GO:0006024; P:glycosaminoglycan biosynthesis; IDA. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR002659; Glyco_trans_31. DR PANTHER; PTHR11214; Glyco_trans_31; 1. DR Pfam; PF01762; Galactosyl_T; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; KW Membrane; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 325 Beta-1,3-galactosyltransferase 6. FT /FTId=PRO_0000219169. FT TOPO_DOM 1 11 Cytoplasmic (Potential). FT TRANSMEM 12 30 Signal-anchor for type II membrane FT 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 //