B4GT3_RAT
ID B4GT3_RAT Reviewed; 395 AA.
AC Q6P768;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
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-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|RGD:1359221};
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=Prostate;
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: 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}.
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DR EMBL; BC061812; AAH61812.1; -; mRNA.
DR RefSeq; NP_001009539.1; NM_001009539.1.
DR RefSeq; XP_006250315.1; XM_006250253.3.
DR RefSeq; XP_006250316.1; XM_006250254.3.
DR AlphaFoldDB; Q6P768; -.
DR SMR; Q6P768; -.
DR STRING; 10116.ENSRNOP00000004735; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q6P768; 4 sites.
DR PhosphoSitePlus; Q6P768; -.
DR PaxDb; Q6P768; -.
DR Ensembl; ENSRNOT00000004735; ENSRNOP00000004735; ENSRNOG00000003551.
DR GeneID; 494342; -.
DR KEGG; rno:494342; -.
DR UCSC; RGD:1359221; rat.
DR CTD; 8703; -.
DR RGD; 1359221; B4galt3.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158549; -.
DR HOGENOM; CLU_044391_1_2_1; -.
DR InParanoid; Q6P768; -.
DR OMA; CDPGGPR; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q6P768; -.
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:Q6P768; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003551; Expressed in spleen and 20 other tissues.
DR Genevisible; Q6P768; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:RGD.
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:RGD.
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 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_0000080540"
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 168
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; 44031 MW; 72BF0E9C7366ED2C CRC64;
MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DPGPTFDYSH PHDVYSNLSH
LPGAPGAAGA PLAQVLPDCP 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 PRAPSGPRYP
PGSSQAFRQE MLQRRPPARP GPLPTANHTA PHGSH
