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 28-JUN-2023, entry version 143. DE RecName: Full=Beta-1,3-galactosyltransferase 6 {ECO:0000305|PubMed:11551958}; DE Short=Beta-1,3-GalTase 6; DE Short=Beta3Gal-T6; DE Short=Beta3GalT6 {ECO:0000303|PubMed:11551958}; DE EC=2.4.1.134 {ECO:0000250|UniProtKB:Q96L58}; 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX 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 1,3- RT 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from CC UDP-galactose to substrates with a terminal beta-linked galactose CC residue. Has a preference for galactose-beta-1,4-xylose that is found CC in the linker region of glycosaminoglycans, such as heparan sulfate and CC chondroitin sulfate. Has no activity towards substrates with terminal CC glucosamine or galactosamine residues. {ECO:0000250|UniProtKB:Q96L58}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl- CC [protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)- CC beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + CC UDP; Xref=Rhea:RHEA:11780, Rhea:RHEA-COMP:12570, Rhea:RHEA- CC COMP:12571, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, CC ChEBI:CHEBI:132088, ChEBI:CHEBI:132090; EC=2.4.1.134; CC Evidence={ECO:0000250|UniProtKB:Q96L58}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11781; CC Evidence={ECO:0000250|UniProtKB:Q96L58}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q96L58}; CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis. CC {ECO:0000250|UniProtKB:Q96L58}. CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. CC {ECO:0000250|UniProtKB:Q96L58}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000250|UniProtKB:Q96L58}; Single-pass type II membrane protein CC {ECO:0000250|UniProtKB:Q96L58}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; 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 CCDS; CCDS19053.1; -. DR RefSeq; NP_536693.1; NM_080445.4. DR AlphaFoldDB; Q91Z92; -. DR SMR; Q91Z92; -. DR BioGRID; 228237; 1. DR STRING; 10090.ENSMUSP00000057521; -. DR CAZy; GT31; Glycosyltransferase Family 31. DR GlyCosmos; Q91Z92; 1 site, No reported glycans. DR GlyGen; Q91Z92; 1 site. DR PhosphoSitePlus; Q91Z92; -. DR EPD; Q91Z92; -. DR MaxQB; Q91Z92; -. DR PaxDb; Q91Z92; -. DR PeptideAtlas; Q91Z92; -. DR ProteomicsDB; 277098; -. DR Antibodypedia; 26175; 176 antibodies from 26 providers. DR DNASU; 117592; -. DR Ensembl; ENSMUST00000052185; ENSMUSP00000057521; ENSMUSG00000050796. DR GeneID; 117592; -. DR KEGG; mmu:117592; -. DR UCSC; uc008wfq.1; mouse. DR AGR; MGI:2152819; -. DR CTD; 126792; -. DR MGI; MGI:2152819; B3galt6. DR VEuPathDB; HostDB:ENSMUSG00000050796; -. DR eggNOG; KOG2288; Eukaryota. DR GeneTree; ENSGT00940000162229; -. DR HOGENOM; CLU_046589_0_0_1; -. DR InParanoid; Q91Z92; -. DR OMA; HVYRWHD; -. DR OrthoDB; 357901at2759; -. DR PhylomeDB; Q91Z92; -. DR TreeFam; TF314311; -. DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis. DR UniPathway; UPA00755; -. DR UniPathway; UPA00756; -. DR BioGRID-ORCS; 117592; 5 hits in 80 CRISPR screens. DR ChiTaRS; B3gnt2; mouse. DR PRO; PR:Q91Z92; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q91Z92; protein. DR Bgee; ENSMUSG00000050796; Expressed in optic fissure and 201 other tissues. DR Genevisible; Q91Z92; MM. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosyltransferase activity; IDA:MGI. DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISO:MGI. DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:MGI. DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central. DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.90.550.50; -; 1. DR InterPro; IPR002659; Glyco_trans_31. DR PANTHER; PTHR11214:SF3; BETA-1,3-GALACTOSYLTRANSFERASE 6; 1. DR PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR Pfam; PF01762; Galactosyl_T; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..325 FT /note="Beta-1,3-galactosyltransferase 6" FT /id="PRO_0000219169" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 12..30 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 31..325 FT /note="Lumenal" FT /evidence="ECO:0000255" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" 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 //