B4GT4_RAT
ID B4GT4_RAT Reviewed; 344 AA.
AC Q66HH1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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
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. 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.
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 -!- 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] + H(+) +
CC UDP; 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] + H(+)
CC + UDP; 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 -!- 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 -!- SUBUNIT: Interacts with SLC35A2/UGT1. {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; BC081866; AAH81866.1; -; mRNA.
DR RefSeq; NP_001012018.1; NM_001012018.1.
DR RefSeq; XP_017453489.1; XM_017598000.1.
DR AlphaFoldDB; Q66HH1; -.
DR SMR; Q66HH1; -.
DR STRING; 10116.ENSRNOP00000004289; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q66HH1; 2 sites.
DR PaxDb; Q66HH1; -.
DR Ensembl; ENSRNOT00000004289; ENSRNOP00000004289; ENSRNOG00000003114.
DR GeneID; 303923; -.
DR KEGG; rno:303923; -.
DR UCSC; RGD:1307880; rat.
DR CTD; 8702; -.
DR RGD; 1307880; B4galt4.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158378; -.
DR HOGENOM; CLU_044391_1_0_1; -.
DR InParanoid; Q66HH1; -.
DR OMA; CDNQPKH; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q66HH1; -.
DR TreeFam; TF312834; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q66HH1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000003114; Expressed in duodenum and 18 other tissues.
DR Genevisible; Q66HH1; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001572; P:lactosylceramide biosynthetic process; ISS:UniProtKB.
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; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Beta-1,4-galactosyltransferase 4"
FT /id="PRO_0000080544"
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; 39707 MW; 864967A3E87A3CC5 CRC64;
MGCNPPYLLS YRLRLLLLFT LCLTVLGWAT SNYFVGAIQV IPRAKNFMAT LHKVMYLGNE
ETLGHGAAMK KAELANCPSV SPNLRGQNKL VFKPDLTLEE VQAKNPKVSR GRYRPEECKA
LQRVAVLIPH RNREKHLIYL LEHLHPFLQR QQLDYGIYVI HQTGSKKFNR AKLLNVGYLE
ALKEENWDCF IFHDVDLVPE NDFNLYTCGD QPKHLVVGRN STGYRLRYSK YFGGVTALSR
EQFFKVNGFS NNYWGWGGED DDLRLRVELH KMKISRPKPD VGKYTMIFHT RDKGNEVNGS
RMKLLQQMSR VWKTDGLSSC SYRLLSVEHN PLYANITVDF WTAA
