B3GN3_MOUSE
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 03-AUG-2022, entry version 122.
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=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 H(+) + UDP; 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] +
CC H(+) + UDP; 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 + H(+) + UDP; 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";
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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_006509752.3.
DR RefSeq; XP_006509816.1; XM_006509753.3.
DR AlphaFoldDB; Q5JCS9; -.
DR SMR; Q5JCS9; -.
DR STRING; 10090.ENSMUSP00000034260; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q5JCS9; 3 sites.
DR PhosphoSitePlus; Q5JCS9; -.
DR MaxQB; Q5JCS9; -.
DR PaxDb; Q5JCS9; -.
DR PRIDE; Q5JCS9; -.
DR ProteomicsDB; 265189; -.
DR Antibodypedia; 14471; 106 antibodies from 23 providers.
DR DNASU; 72297; -.
DR Ensembl; ENSMUST00000034260; ENSMUSP00000034260; ENSMUSG00000031803.
DR GeneID; 72297; -.
DR KEGG; mmu:72297; -.
DR UCSC; uc009mer.3; mouse.
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; YCAGGGF; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q5JCS9; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 72297; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q5JCS9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q5JCS9; protein.
DR Bgee; ENSMUSG00000031803; Expressed in epithelium of stomach and 57 other tissues.
DR Genevisible; Q5JCS9; 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:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:UniProtKB.
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..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
