B3GT6_MOUSE
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 03-AUG-2022, entry version 138.
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";
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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 GlyGen; Q91Z92; 1 site.
DR PhosphoSitePlus; Q91Z92; -.
DR EPD; Q91Z92; -.
DR MaxQB; Q91Z92; -.
DR PaxDb; Q91Z92; -.
DR PeptideAtlas; Q91Z92; -.
DR PRIDE; Q91Z92; -.
DR ProteomicsDB; 277098; -.
DR Antibodypedia; 26175; 163 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 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; 640360at2759; -.
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 75 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; ISO: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:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:MGI.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
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:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 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
