B4GT4_CRIGR
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 03-AUG-2022, entry version 94.
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 biosynthesis of
CC glycoproteins, proteoglycans, and glycosyphingolipids. Catalyzes the
CC transfer of Gal residue via a beta1->4 linkage from UDP-Gal to the non-
CC reducing terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in
CC the 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
CC mono- and disulfated disaccharide units [->3Galbeta1->4(6-
CC sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-
CC sulfoGlcNAcbeta)1->] within keratan sulfate polymer.
CC {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 + 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: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)) + 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:O60513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
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 -!- 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; AY117538; AAM77197.1; -; mRNA.
DR RefSeq; NP_001233624.1; NM_001246695.1.
DR RefSeq; XP_007647946.1; XM_007649756.2.
DR RefSeq; XP_007647947.1; XM_007649757.2.
DR RefSeq; XP_007647948.1; XM_007649758.2.
DR RefSeq; XP_016834525.1; XM_016979036.1.
DR AlphaFoldDB; Q80WN7; -.
DR SMR; Q80WN7; -.
DR STRING; 10029.XP_007647949.1; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR Ensembl; ENSCGRT00001023241; ENSCGRP00001018997; ENSCGRG00001018573.
DR GeneID; 100689435; -.
DR KEGG; cge:100689435; -.
DR CTD; 8702; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158378; -.
DR OMA; CDNQPKH; -.
DR OrthoDB; 1201618at2759; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0035250; F:UDP-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001572; P:lactosylceramide biosynthetic process; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Manganese; Membrane; Metal-binding; Signal-anchor;
KW 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
