B3GN6_MOUSE
ID B3GN6_MOUSE Reviewed; 391 AA.
AC Q3USF0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase;
DE EC=2.4.1.147;
DE AltName: Full=Core 3 synthase;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6;
DE Short=BGnT-6;
DE Short=Beta-1,3-Gn-T6;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 6;
DE Short=Beta3Gn-T6;
GN Name=B3gnt6;
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 [LARGE SCALE MRNA].
RC TISSUE=Salivary 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-391.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the
CC core 3 structure of the O-glycan, an important precursor in the
CC biosynthesis of mucin-type glycoproteins. Plays an important role in
CC the synthesis of mucin-type O-glycans in digestive organs.
CC {ECO:0000250|UniProtKB:Q6ZMB0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-
CC (1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:46880, Rhea:RHEA-COMP:11689, Rhea:RHEA-
CC COMP:11692, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:87075, ChEBI:CHEBI:87080; EC=2.4.1.147;
CC Evidence={ECO:0000250|UniProtKB:Q6ZMB0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-
CC (1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:46884, Rhea:RHEA-COMP:11691, Rhea:RHEA-
CC COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:53604, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:87079; EC=2.4.1.147;
CC Evidence={ECO:0000250|UniProtKB:Q6ZMB0};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; BC039789; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK140429; BAE24383.1; -; mRNA.
DR CCDS; CCDS40027.1; -.
DR RefSeq; NP_001074636.1; NM_001081167.1.
DR AlphaFoldDB; Q3USF0; -.
DR SMR; Q3USF0; -.
DR BioGRID; 234871; 1.
DR STRING; 10090.ENSMUSP00000095879; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q3USF0; 2 sites.
DR PhosphoSitePlus; Q3USF0; -.
DR PaxDb; Q3USF0; -.
DR PeptideAtlas; Q3USF0; -.
DR PRIDE; Q3USF0; -.
DR ProteomicsDB; 277149; -.
DR Antibodypedia; 31219; 102 antibodies from 24 providers.
DR Ensembl; ENSMUST00000098278; ENSMUSP00000095879; ENSMUSG00000074004.
DR GeneID; 272411; -.
DR KEGG; mmu:272411; -.
DR UCSC; uc009ikf.1; mouse.
DR CTD; 192134; -.
DR MGI; MGI:3039603; B3gnt6.
DR VEuPathDB; HostDB:ENSMUSG00000074004; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000163174; -.
DR HOGENOM; CLU_036849_5_3_1; -.
DR InParanoid; Q3USF0; -.
DR OMA; MWKALHN; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q3USF0; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.147; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 272411; 2 hits in 74 CRISPR screens.
DR ChiTaRS; B4gat1; mouse.
DR PRO; PR:Q3USF0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3USF0; protein.
DR Bgee; ENSMUSG00000074004; Expressed in submandibular gland and 8 other tissues.
DR Genevisible; Q3USF0; MM.
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:0106328; F:acetylgalactosaminyl-O-glycosyl-seryl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106327; F:acetylgalactosaminyl-O-glycosyl-threonyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008378; F:galactosyltransferase activity; ISO:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..391
FT /note="Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-
FT 1,3-N-acetylglucosaminyltransferase"
FT /id="PRO_0000289219"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..391
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 133
FT /note="R -> G (in Ref. 2; BAE24383)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="P -> A (in Ref. 2; BAE24383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43951 MW; 23F4488941447A1A CRC64;
MALPSSRRFK SPTTLAFFLV GVTLVVLNQW FLQEHRQEKA KGPVATRRSL AAVVQRSPLF
QVPPCVANAS ANLLTGFQLL PARIQDFLRY RHCRRFPQLW DAPPKCAGPR GVFLLLAVKS
SPAHYERREL IRRTWGQERS YSGRQVLRLF LVGTSPPEEA AREPQLADLL SLEAREYGDV
LQWDFSDTFL NLTLKHLHLL DWTAEHCPGV SFLLSCDDDV FVHTANVLSF LEVQSPEHHL
FTGQLMVGSV PVRESGSKYF VPPQIFPGVA YPAYCSGGGF LLSRYTVRNL RSAAHHVPLF
PIDDAYMGMC LQQAGLAPSS HQGIRPFGVQ LPNVQRLSLD PCMYRELLLV HRFAPYEMLL
MWKALHNPAL HCSHKQVAGS PTAGEQNPDA H
