ID B3GN3_MOUSE Reviewed; 372 AA. AC Q5JCS9; Q8R0U2; Q9D7Z2; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 02-SEP-2026, entry version 140. DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3; DE EC=2.4.1.149 {ECO:0000250|UniProtKB:Q9Y2A9}; DE AltName: Full=Core 1 extending beta-1,3-N-acetylglucosaminyltransferase {ECO:0000250|UniProtKB:Q9Y2A9}; DE EC=2.4.1.146 {ECO:0000250|UniProtKB:Q9Y2A9}; DE AltName: Full=Core1-beta3GlcNAcT; DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3; DE Short=BGnT-3; DE Short=Beta-1,3-Gn-T3; DE Short=Beta-1,3-N-acetylglucosaminyltransferase 3; DE Short=Beta3Gn-T3; GN Name=B3gnt3; 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=129/Sv; RA Zhou D., Hennet T.; RT "Mouse beta1,3 N-acetylglucosaminyltransferase-3."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yeh J.-C., Fukuda M.; RT "Core 1 beta-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT)."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Stomach; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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-N-acetylglucosaminyltransferase involved in the CC synthesis of poly-N-acetyllactosamine. Has activity for type 2 CC oligosaccharides. Also acts as a core1-1,3-N- CC acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo CC sialyl Lewis x on extended core1 O-glycans. CC {ECO:0000250|UniProtKB:Q9Y2A9}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl- CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + UDP- CC N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal- CC (1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-threonyl-[protein] + CC UDP + H(+); Xref=Rhea:RHEA:56224, Rhea:RHEA-COMP:14420, Rhea:RHEA- CC COMP:14422, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:139607, ChEBI:CHEBI:139612; EC=2.4.1.146; CC Evidence={ECO:0000250|UniProtKB:Q9Y2A9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl- CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + UDP-N- CC acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal- CC (1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-seryl-[protein] + UDP CC + H(+); Xref=Rhea:RHEA:56220, Rhea:RHEA-COMP:14419, Rhea:RHEA- CC COMP:14421, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:139605, ChEBI:CHEBI:139611; EC=2.4.1.146; CC Evidence={ECO:0000250|UniProtKB:Q9Y2A9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl CC derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D- CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D- CC glucosaminyl derivative + UDP + H(+); Xref=Rhea:RHEA:14389, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:133507, ChEBI:CHEBI:134090; EC=2.4.1.149; CC Evidence={ECO:0000250|UniProtKB:Q9Y2A9}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single- CC pass type II membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=beta 3 CC GlcNAc-T III; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_572"; 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; AY037785; AAK68855.1; -; mRNA. DR EMBL; AY039028; AAK72481.1; -; mRNA. DR EMBL; AK008674; BAB25824.1; -; mRNA. DR EMBL; BC026418; AAH26418.1; -; mRNA. DR CCDS; CCDS22405.1; -. DR RefSeq; NP_082465.3; NM_028189.3. DR RefSeq; XP_006509815.1; XM_006509752.4. DR RefSeq; XP_006509816.1; XM_006509753.4. DR AlphaFoldDB; Q5JCS9; -. DR SMR; Q5JCS9; -. DR BioGRID; 215289; 1. DR FunCoup; Q5JCS9; 292. DR STRING; 10090.ENSMUSP00000034260; -. DR GlyCosmos; Q5JCS9; 3 sites, No reported glycans. DR GlyGen; Q5JCS9; 3 sites, 1 N-linked glycan (1 site). DR PhosphoSitePlus; Q5JCS9; -. DR PaxDb; 10090-ENSMUSP00000034260; -. DR ProteomicsDB; 265189; -. DR Antibodypedia; 14471; 108 antibodies from 25 providers. DR DNASU; 72297; -. DR Ensembl; ENSMUST00000034260.9; ENSMUSP00000034260.8; ENSMUSG00000031803.9. DR GeneID; 72297; -. DR KEGG; mmu:72297; -. DR UCSC; uc009mer.3; mouse. DR AGR; MGI:2152535; -. DR CTD; 10331; -. DR MGI; MGI:2152535; B3gnt3. DR VEuPathDB; HostDB:ENSMUSG00000031803; -. DR eggNOG; KOG2287; Eukaryota. DR GeneTree; ENSGT00940000159134; -. DR HOGENOM; CLU_036849_5_3_1; -. DR InParanoid; Q5JCS9; -. DR OMA; VSYLQGH; -. DR OrthoDB; 2139606at2759; -. DR PhylomeDB; Q5JCS9; -. DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis. DR Reactome; R-MMU-913709; O-linked glycosylation of mucins. DR Reactome; R-MMU-9931295; PD-L1(CD274) glycosylation and translocation to plasma membrane. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 72297; 1 hit in 79 CRISPR screens. DR PRO; PR:Q5JCS9; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q5JCS9; protein. DR Bgee; ENSMUSG00000031803; Expressed in epithelium of stomach and 59 other cell types or tissues. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; ISS:UniProtKB. DR GO; GO:0009101; P:glycoprotein biosynthetic process; IEA:InterPro. DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:UniProtKB. DR FunFam; 3.90.550.50:FF:000009; Hexosyltransferase; 1. DR Gene3D; 3.90.550.50; -; 1. DR InterPro; IPR002659; Glyco_trans_31. DR PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR11214:SF23; N-ACETYLLACTOSAMINIDE BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE 3; 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..372 FT /note="N-acetyllactosaminide beta-1,3-N- FT acetylglucosaminyltransferase 3" FT /id="PRO_0000219173" FT TOPO_DOM 1..10 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 11..31 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 32..372 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 31..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 64 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 256 FT /note="A -> T (in Ref. 4; AAH26418)" FT /evidence="ECO:0000305" FT CONFLICT 283 FT /note="L -> I (in Ref. 1; AAK68855 and 3; BAB25824)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="I -> V (in Ref. 1; AAK68855 and 3; BAB25824)" FT /evidence="ECO:0000305" SQ SEQUENCE 372 AA; 42586 MW; 484771C8054DE265 CRC64; MRLPRQSPYE ILLLVLVALL VLLLLLTSKS PPSCSAPERS KEPEDNPGWA TGHPRTHPAR CRANLSVSSH PDFAGLPLHV RDFLFYRHCR DFPVLREPRV TKCAEPVFLL LAIKSSPANY GRRQMLRTTW ARERRVRGAP LRRLFLVGSD RDPQQARKYN RLLELEAQKY GDILQWDFHD SFFNLTLKQV LFLEWQLTYC TNASFVLNGD DDVFAHTDNM VTYLQDHDPD QHLFVGHLIQ NVGPIRVPWS KYFIPALVMA EDRYPPYCGG GGFLLSRFTV AALRRAARVL PMFPIDDVFL GMCLQQQGLA PGTHSGVRTA GVFPPSPRVS SFDPCFYRDL LLVHRFLPFE MLLMWDALNQ PQLLCGRQSP AY //