B3GN2_MOUSE
ID B3GN2_MOUSE Reviewed; 397 AA.
AC Q9Z222; Q91V18;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2;
DE EC=2.4.1.149 {ECO:0000250|UniProtKB:Q9NY97};
DE AltName: Full=Beta-1,3-N-acetylglucosaminyltransferase 1;
DE Short=BGnT-1;
DE Short=Beta-1,3-Gn-T1;
DE Short=Beta3Gn-T1;
DE AltName: Full=Beta-1,3-galactosyltransferase 7;
DE Short=Beta-1,3-GalTase 7;
DE Short=Beta3Gal-T7;
DE Short=Beta3GalT7;
DE Short=b3Gal-T7;
DE AltName: Full=Beta-3-Gx-T7;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2;
DE Short=BGnT-2;
DE Short=Beta-1,3-Gn-T2;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 2;
DE Short=Beta3Gn-T2;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7;
GN Name=B3GNT2; Synonyms=B3gnt1, Beta3gnt;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND TISSUE SPECIFICITY.
RC STRAIN=ICR {ECO:0000269|PubMed:9892646};
RC TISSUE=Neonatal brain {ECO:0000269|PubMed:9892646};
RX PubMed=9892646; DOI=10.1073/pnas.96.2.406;
RA Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
RA Vliegenthart J.F.G., Berger E.G., Hennet T.;
RT "A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine
RT synthase activity is structurally related to beta-1,3-
RT galactosyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION.
RA Zhou D., Berger E.G., Hennet T.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAK95359.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C.B17 {ECO:0000312|EMBL:AAK95359.1};
RX PubMed=11511811; DOI=10.1023/a:1010921313314;
RA Egan S., Cohen B., Sarkar M., Ying Y., Cohen S., Singh N., Wang W.,
RA Flock G., Goh T., Schachter H.;
RT "Molecular cloning and expression analysis of a mouse UDP-GlcNAc:Gal(beta1-
RT 4)Glc(NAc)-R beta1,3-N-acetylglucosaminyltransferase homologous to
RT Drosophila melanogaster Brainiac and the beta1,3-galactosyltransferase
RT family.";
RL Glycoconj. J. 17:867-875(2000).
RN [4] {ECO:0000312|EMBL:AAH09075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI {ECO:0000312|EMBL:AAH09075.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH09075.1};
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 [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17890318; DOI=10.1073/pnas.0707426104;
RA Togayachi A., Kozono Y., Ishida H., Abe S., Suzuki N., Tsunoda Y.,
RA Hagiwara K., Kuno A., Ohkura T., Sato N., Sato T., Hirabayashi J.,
RA Ikehara Y., Tachibana K., Narimatsu H.;
RT "Polylactosamine on glycoproteins influences basal levels of lymphocyte and
RT macrophage activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15829-15834(2007).
RN [6]
RP INTERACTION WITH B3GNT8.
RX PubMed=18826941; DOI=10.1074/jbc.m806933200;
RA Seko A., Yamashita K.;
RT "Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by
RT beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-
RT acetyllactosamine chains in differentiated HL-60 cells.";
RL J. Biol. Chem. 283:33094-33100(2008).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=18008318; DOI=10.1002/mrd.20828;
RA Biellmann F., Henion T.R., Burki K., Hennet T.;
RT "Impaired sexual behavior in male mice deficient for the beta1-3 N-
RT acetylglucosaminyltransferase-I gene.";
RL Mol. Reprod. Dev. 75:699-706(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-173.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=23006775; DOI=10.1016/j.mcn.2012.09.003;
RA Henion T.R., Madany P.A., Faden A.A., Schwarting G.A.;
RT "beta3GnT2 null mice exhibit defective accessory olfactory bulb
RT innervation.";
RL Mol. Cell. Neurosci. 52:73-86(2013).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
CC synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and
CC elongation of poly-N-acetyllactosamine chains (PubMed:9892646).
CC Probably constitutes the main polylactosamine synthase
CC (PubMed:17890318). {ECO:0000269|PubMed:17890318,
CC ECO:0000269|PubMed:9892646}.
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:Q9NY97};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9892646};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with B3GNT8; this interaction greatly increases
CC B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity.
CC {ECO:0000269|PubMed:18826941}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, kidney and testis
CC and, to a lesser extent, in liver and skeletal muscle. No expression in
CC spleen. {ECO:0000269|PubMed:9892646}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduced number polylactosamine
CC structures on N-glycans in immunological tissues. B-cells and T-cells
CC proliferate show hyperproliferation (PubMed:17890318). Mice also
CC display defective accessory olfactory bulb innervation
CC (PubMed:23006775). Impaired sexual behaviour. While female mice are
CC fertile, males show a reduced rate of reproduction. Defects cannot be
CC attributed to any physical defect in their reproductive organs,
CC suggesting that the phenotype observed may result from an impaired
CC sexual response to female mating partners.
CC {ECO:0000269|PubMed:17890318, ECO:0000269|PubMed:18008318,
CC ECO:0000269|PubMed:23006775}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
CC -!- CAUTION: There is some conflicting nomenclature, as some groups still
CC name this protein B3gnt1 (PubMed:18008318). The correct and official
CC nomenclature is however B3gnt2. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=MGC32391:
CC hypothetical protein MGC32391/hypothetical protein MGC32391;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_472";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=beta 3
CC GlcNAc-T I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_571";
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DR EMBL; AF092050; AAD09763.2; -; mRNA.
DR EMBL; AY043479; AAK95359.1; -; mRNA.
DR EMBL; BC009075; AAH09075.1; -; mRNA.
DR CCDS; CCDS24471.1; -.
DR RefSeq; NP_001162585.1; NM_001169114.1.
DR RefSeq; NP_058584.3; NM_016888.5.
DR AlphaFoldDB; Q9Z222; -.
DR SMR; Q9Z222; -.
DR IntAct; Q9Z222; 2.
DR STRING; 10090.ENSMUSP00000060247; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9Z222; 6 sites.
DR iPTMnet; Q9Z222; -.
DR PhosphoSitePlus; Q9Z222; -.
DR MaxQB; Q9Z222; -.
DR PaxDb; Q9Z222; -.
DR PRIDE; Q9Z222; -.
DR ProteomicsDB; 277148; -.
DR Antibodypedia; 1107; 187 antibodies from 27 providers.
DR DNASU; 53625; -.
DR Ensembl; ENSMUST00000055549; ENSMUSP00000053528; ENSMUSG00000051650.
DR Ensembl; ENSMUST00000062844; ENSMUSP00000060247; ENSMUSG00000051650.
DR GeneID; 53625; -.
DR KEGG; mmu:53625; -.
DR UCSC; uc007ieh.2; mouse.
DR CTD; 10678; -.
DR MGI; MGI:1889505; B3gnt2.
DR VEuPathDB; HostDB:ENSMUSG00000051650; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000155345; -.
DR HOGENOM; CLU_036849_5_0_1; -.
DR InParanoid; Q9Z222; -.
DR OMA; DQPDICK; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9Z222; -.
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; 53625; 5 hits in 41 CRISPR screens.
DR ChiTaRS; B3gnt2; mouse.
DR PRO; PR:Q9Z222; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z222; protein.
DR Bgee; ENSMUSG00000051650; Expressed in primary oocyte and 73 other tissues.
DR ExpressionAtlas; Q9Z222; baseline and differential.
DR Genevisible; Q9Z222; 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: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:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..397
FT /note="N-acetyllactosaminide beta-1,3-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000219171"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 283
FT /note="R -> S (in Ref. 2; AAD09763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 45883 MW; D8BBEA1866C1D106 CRC64;
MSVGRRRVKL LGILMMANVF IYLIVEVSKN SSQDKNGKGG VIIPKEKFWK PPSTPRAYWN
REQEKLNRWY NPILNRVANQ TGELATSPNT SHLSYCEPDS TVMTAVTDFN NLPDRFKDFL
LYLRCRNYSL LIDQPKKCAK KPFLLLAIKS LIPHFARRQA IRESWGRETN VGNQTVVRVF
LLGKTPPEDN HPDLSDMLKF ESDKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDAEF
VFKGDDDVFV NTHHILNYLN SLSKSKAKDL FIGDVIHNAG PHRDKKLKYY IPEVFYTGVY
PPYAGGGGFL YSGPLALRLY SATSRVHLYP IDDVYTGMCL QKLGLVPEKH KGFRTFDIEE
KNKKNICSYI DLMLVHSRKP QEMIDIWSQL QSPNLKC
