ID   B4GT4_CRIGR             Reviewed;         344 AA.
AC   Q80WN7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 107.
DE   RecName: Full=Beta-1,4-galactosyltransferase 4;
DE            Short=Beta-1,4-GalTase 4;
DE            Short=Beta4Gal-T4;
DE            Short=b4Gal-T4;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:O60513};
DE   AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE   AltName: Full=Lactotriaosylceramide beta-1,4-galactosyltransferase;
DE            EC=2.4.1.275 {ECO:0000250|UniProtKB:O60513};
DE   AltName: Full=N-acetyllactosamine synthase;
DE            EC=2.4.1.90 {ECO:0000250|UniProtKB:O60513};
DE   AltName: Full=Nal synthase;
DE   AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4;
DE   AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4;
GN   Name=B4GALT4;
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).
CC   -!- FUNCTION: Galactose (Gal) transferase involved in the synthesis of
CC       terminal N-acetyllactosamine (LacNac) unit present on glycan chains of
CC       glycoproteins and glycosphingolipids. Catalyzes the transfer of Gal
CC       residue via a beta1->4 linkage from UDP-Gal to the non-reducing
CC       terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the
CC       linearly growing chain of both N- and O-linked keratan sulfate
CC       proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase
CC       and CHST6 and CHST1 sulfotransferases to construct and elongate mono-
CC       and disulfated disaccharide units [->3Galbeta1->4(6-
CC       sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-
CC       sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Transfers Gal
CC       residue via a beta1->4 linkage to terminal 6-O-sulfoGlcNAc within the
CC       LacNac unit of core 2 O-glycans forming 6-sulfo-sialyl-Lewis X (sLex).
CC       May contribute to the generation of sLex epitope on mucin-type
CC       glycoproteins that serve as ligands for SELL/L-selectin, a major
CC       regulator of leukocyte migration. In the biosynthesis pathway of
CC       neolacto-series glycosphingolipids, transfers Gal residue via a
CC       beta1->4 linkage to terminal GlcNAc of a lactotriaosylceramide (Lc3Cer)
CC       acceptor to form a neolactotetraosylceramide. Efficiently
CC       galactosylates both non-sulfated and 6-O-sulfated terminal GlcNAc
CC       moities on G0 complex-type N-glycans. {ECO:0000250|UniProtKB:O60513}.
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:O60513};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
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:O60513};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC         glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-
CC         [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC         [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC         (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + UDP +
CC         H(+); Xref=Rhea:RHEA:67948, Rhea:RHEA-COMP:17367, Rhea:RHEA-
CC         COMP:17398, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:176494, ChEBI:CHEBI:176635;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67949;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC         glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC         [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC         [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC         (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + UDP +
CC         H(+); Xref=Rhea:RHEA:67872, Rhea:RHEA-COMP:17370, Rhea:RHEA-
CC         COMP:17397, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:176493, ChEBI:CHEBI:176634;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67873;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(4)-{6-O-sulfo-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-
CC         [beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC         GlcNAc-(1->4)-beta-D-GlcNAc}-L--asparaginyl-[protein] + 2 UDP-alpha-
CC         D-galactose = an N(4)-{beta-D-Gal-(1->4)-6-O-sulfo-beta-D-GlcNAc-
CC         (1->2)-alpha-D-Man-(1->3)-[beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC         GlcNAc}-L-asparaginyl-[protein] + 2 UDP + 2 H(+);
CC         Xref=Rhea:RHEA:84279, Rhea:RHEA-COMP:20335, Rhea:RHEA-COMP:20336,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:233660, ChEBI:CHEBI:233661;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84280;
CC         Evidence={ECO:0000250|UniProtKB:O60513};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:O60513}.
CC   -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:O60513}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:O60513}; Single-pass type II membrane protein
CC       {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:O60513}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR   EMBL; AY117538; AAM77197.1; -; mRNA.
DR   RefSeq; NP_001233624.1; NM_001246695.1.
DR   RefSeq; XP_007647946.1; XM_007649756.4.
DR   RefSeq; XP_007647947.1; XM_007649757.4.
DR   RefSeq; XP_016834525.1; XM_016979036.3.
DR   AlphaFoldDB; Q80WN7; -.
DR   SMR; Q80WN7; -.
DR   GlyCosmos; Q80WN7; 2 sites, No reported glycans.
DR   GlyGen; Q80WN7; 2 sites.
DR   Ensembl; ENSCGRT00000023727; ENSCGRP00000023406; ENSCGRG00000016951.
DR   Ensembl; ENSCGRT00001023241; ENSCGRP00001018997; ENSCGRG00001018573.
DR   GeneID; 100689435; -.
DR   KEGG; cge:100689435; -.
DR   CTD; 8702; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   OMA; TSNYFVD; -.
DR   OrthoDB; 10016069at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP001108280; Chromosome 4.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
DR   GO; GO:0035250; F:UDP-galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0018146; P:keratan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0001572; P:lactosylceramide biosynthetic 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:SF9; BETA-1,4-GALACTOSYLTRANSFERASE 4; 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   Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..344
FT                   /note="Beta-1,4-galactosyltransferase 4"
FT                   /id="PRO_0000080541"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..344
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         129..133
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..170
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..196
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         258..261
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   BINDING         289..291
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  39893 MW;  23AA84AB3187E53E CRC64;
     MGCNPPYLLP YRLRLLLFFT LCLTVVGWVT SNYFVDPIQV IPKAKVFMAS FYKVIPLGKE
     ETLVHDATME KVELGNCPSV SPNLRGQSKL IFEPDLTLEE VQAKNPKVSG GRYHPEECKA
     VQRVAVLIPH RNREKHLTYL LEHLHPFLQR QQLDYGIYII HQTGSKKFNR AKLLNVGYLE
     ALKEQNWDCF IFHDVDLVPE NDFNLYTCGD QPKHLVVGRN STGYRLRYSK YFGGVTALSR
     EQFFKVNGFS NNYWGWGGED DDLRLRVELH KMKISRPNPD VGKYTMIFHT RDKGNEVNVD
     RMKLLHQMSR VWKTDGLSSC SYRLLSVEHN PLYTNITVDF WTGV
//