ID   B4GT3_MOUSE             Reviewed;         395 AA.
AC   Q91YY2; Q9QY13;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   29-SEP-2021, entry version 149.
DE   RecName: Full=Beta-1,4-galactosyltransferase 3 {ECO:0000305};
DE            Short=Beta-1,4-GalTase 3;
DE            Short=Beta4Gal-T3;
DE            Short=b4Gal-T3;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:O60512};
DE   AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE   AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
DE            EC=2.4.1.38 {ECO:0000250|UniProtKB:O60512};
DE   AltName: Full=N-acetyllactosamine synthase;
DE            EC=2.4.1.90 {ECO:0000250|UniProtKB:O60512};
DE   AltName: Full=Nal synthase;
DE   AltName: Full=Neolactotriaosylceramide beta-1,4-galactosyltransferase;
DE            EC=2.4.1.275;
DE   AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3;
DE   AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3;
GN   Name=B4galt3 {ECO:0000312|MGI:MGI:1928767};
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].
RX   PubMed=9597550; DOI=10.1093/glycob/8.5.517;
RA   Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
RT   "The expanding beta 4-galactosyltransferase gene family: messages from the
RT   databanks.";
RL   Glycobiology 8:517-526(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-339.
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).
CC   -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC       oligosaccharides in many glycoproteins as well as the carbohydrate
CC       moieties of glycolipids. {ECO:0000250|UniProtKB:O60512}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC         galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC         derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:133507; EC=2.4.1.38;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC         galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC         Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC         EC=2.4.1.90; Evidence={ECO:0000250|UniProtKB:O60512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC         Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside
CC         nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-
CC         galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP;
CC         Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC         galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC         (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC         beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) +
CC         UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC         Evidence={ECO:0000250|UniProtKB:O60512};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:O60512}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC       Note=Trans cisternae of Golgi stack. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b4GalT3;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_462";
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DR   EMBL; AF142671; AAF22221.1; -; mRNA.
DR   EMBL; BC013619; AAH13619.1; -; mRNA.
DR   CCDS; CCDS15486.1; -.
DR   RefSeq; NP_065604.2; NM_020579.2.
DR   SMR; Q91YY2; -.
DR   MINT; Q91YY2; -.
DR   STRING; 10090.ENSMUSP00000106945; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyConnect; 2150; 2 N-Linked glycans (1 site).
DR   GlyGen; Q91YY2; 4 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q91YY2; -.
DR   PhosphoSitePlus; Q91YY2; -.
DR   MaxQB; Q91YY2; -.
DR   PaxDb; Q91YY2; -.
DR   PRIDE; Q91YY2; -.
DR   ProteomicsDB; 273461; -.
DR   Antibodypedia; 2534; 219 antibodies.
DR   DNASU; 57370; -.
DR   Ensembl; ENSMUST00000064272; ENSMUSP00000066353; ENSMUSG00000052423.
DR   Ensembl; ENSMUST00000111313; ENSMUSP00000106945; ENSMUSG00000052423.
DR   GeneID; 57370; -.
DR   KEGG; mmu:57370; -.
DR   UCSC; uc007dnp.2; mouse.
DR   CTD; 8703; -.
DR   MGI; MGI:1928767; B4galt3.
DR   VEuPathDB; HostDB:ENSMUSG00000052423; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   GeneTree; ENSGT00940000158549; -.
DR   HOGENOM; CLU_044391_1_2_1; -.
DR   InParanoid; Q91YY2; -.
DR   OMA; TANHTAH; -.
DR   OrthoDB; 1201618at2759; -.
DR   PhylomeDB; Q91YY2; -.
DR   TreeFam; TF312834; -.
DR   Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 57370; 4 hits in 64 CRISPR screens.
DR   ChiTaRS; B4galt3; mouse.
DR   PRO; PR:Q91YY2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q91YY2; protein.
DR   Bgee; ENSMUSG00000052423; Expressed in granulocyte and 310 other tissues.
DR   Genevisible; Q91YY2; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008378; F:galactosyltransferase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003945; F:N-acetyllactosamine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006682; P:galactosylceramide biosynthetic process; ISO:MGI.
DR   GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; PTHR19300; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Lipid metabolism; Manganese; Membrane; Metal-binding; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Beta-1,4-galactosyltransferase 3"
FT                   /id="PRO_0000080538"
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..395
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          132..136
FT                   /note="UDP-alpha-D-galactose binding"
FT                   /evidence="ECO:0000250"
FT   REGION          171..173
FT                   /note="UDP-alpha-D-galactose binding"
FT                   /evidence="ECO:0000250"
FT   REGION          198..199
FT                   /note="UDP-alpha-D-galactose binding"
FT                   /evidence="ECO:0000250"
FT   REGION          262..265
FT                   /note="N-acetyl-D-glucosamine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          293..295
FT                   /note="UDP-alpha-D-galactose binding"
FT                   /evidence="ECO:0000250"
FT   REGION          340..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           199
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           293
FT                   /note="Manganese; via tele nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /note="UDP-alpha-D-galactose"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /note="UDP-alpha-D-galactose"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..211
FT                   /evidence="ECO:0000250"
FT   CONFLICT        353
FT                   /note="S -> A (in Ref. 1; AAF22221)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  44084 MW;  16401B033EEB4B21 CRC64;
     MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DPGPTFDYSH PHDVYSNLSH
     LPAAPGAAGA PPAQALPYCP ERSPFLVGPV SVSFSPVPSL AEIVERNPRV ESGGRYRPAG
     CEPRSRTAII VPHRAREHHL RLLLYHLHPF LQRQQLAYGI YVIHQAGNGT FNRAKLLNVG
     VREALRDEEW DCLFLHDVDL LPENDHNLYV CDPRGPRHVA VAMNKFGYSL PYPQYFGGVS
     ALTPDQYLKM NGFPNEYWGW GGEDDDIATR VRLAGMKISR PPTSVGHYKM VKHRGDKGNE
     ENPHRFDLLV RTQNSWTQDG MNSLTYRLLA RELGPLYTNI TADIGTDPRG PRSPSGPRYP
     PGSSQAFRQE MLQRRPPARP GPLPTANHTA PRGSH
//