ID   B4GT3_CRIGR             Reviewed;         395 AA.
AC   Q80WN8; G3HU17;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Beta-1,4-galactosyltransferase 3;
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;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=14567696; DOI=10.1021/bi0353068;
RA   Lee J., Park S.-H., Sundaram S., Raju T.S., Shaper N.L., Stanley P.;
RT   "A mutation causing a reduced level of expression of six beta4-
RT   galactosyltransferase genes is the basis of the Lec19 CHO glycosylation
RT   mutant.";
RL   Biochemistry 42:12349-12357(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23929341; DOI=10.1038/nbt.2645;
RA   Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA   Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA   Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA   Helk B., Mott J.E., Puhler A., Borth N.;
RT   "Chinese hamster genome sequenced from sorted chromosomes.";
RL   Nat. Biotechnol. 31:694-695(2013).
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 + UDP + H(+); 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 + UDP + H(+);
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)) + UDP + H(+); 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=a beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-
CC         galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + UDP + H(+);
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 = a neolactoside nLc6Cer + UDP + H(+);
CC         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}.
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DR   EMBL; AY117537; AAM77196.1; -; mRNA.
DR   EMBL; JH000722; EGW08561.1; -; Genomic_DNA.
DR   EMBL; KE676296; ERE74030.1; -; Genomic_DNA.
DR   RefSeq; NP_001233706.1; NM_001246777.2.
DR   RefSeq; XP_007645568.1; XM_007647378.4.
DR   RefSeq; XP_007645569.1; XM_007647379.4.
DR   RefSeq; XP_007645570.1; XM_007647380.4.
DR   RefSeq; XP_007645571.1; XM_007647381.3.
DR   RefSeq; XP_007645572.1; XM_007647382.4.
DR   AlphaFoldDB; Q80WN8; -.
DR   SMR; Q80WN8; -.
DR   GlyCosmos; Q80WN8; 3 sites, No reported glycans.
DR   GlyGen; Q80WN8; 3 sites.
DR   PaxDb; 10029-G3HU17; -.
DR   Ensembl; ENSCGRT00000002360; ENSCGRP00000002306; ENSCGRG00000001697.
DR   Ensembl; ENSCGRT00001031762; ENSCGRP00001027515; ENSCGRG00001024503.
DR   Ensembl; ENSCGRT00015028454; ENSCGRP00015023207; ENSCGRG00015017584.
DR   GeneID; 100689346; -.
DR   KEGG; cge:100689346; -.
DR   CTD; 8703; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   GeneTree; ENSGT00940000158549; -.
DR   InParanoid; G3HU17; -.
DR   OMA; CDPGGPR; -.
DR   OrthoDB; 10016069at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP001108280; Chromosome 5.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006682; P:galactosylceramide biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0006678; P:glucosylceramide metabolic process; IEA:Ensembl.
DR   CDD; cd00899; b4GalT; 1.
DR   FunFam; 3.90.550.10:FF:000028; beta-1,4-galactosyltransferase 1; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF33; BETA-1,4-GALACTOSYLTRANSFERASE 3; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   2: Evidence at transcript 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_0000080536"
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          341..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132..136
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..173
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         262..265
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   BINDING         293..295
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   395 AA;  44060 MW;  7FB9760DC6329680 CRC64;
     MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DQGPTFDYSH PRDVYSNLSH
     LPGAPVAAGA SPAEALPFCP ERSPFLVGPV SVSFSPVPSL AEIVERNPRV EPGGRYRPAG
     CEARSRTAII VPHRAREHHL RLLLYHLHPF LQRQQLAYGI YVIHQAGNGM FNRAKLLNVG
     VREALRDEEW DCLFLHDVDL LPENDHNLYV CDPRGPRHVA VAMNKFGYSL PYPQYFGGVS
     ALTPDQYLKM NGFPNEYWGW GGEDDDIATR VRLAGMKISR PPTSVGHYKM VKHRGDKGNE
     ENPHRFDLLV RTQNSWTQDG MNSLTYQLLA KELGPLYTNI TADIGTDPRG PRAPSGPRYP
     PGSSQAFRQE MLQRRPPARP GPLPTANHTA PHGSH
//