B4GT3_BOVIN
ID B4GT3_BOVIN Reviewed; 396 AA.
AC Q5EA87; Q08DJ2; Q0V8R0; Q5E9K4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; BT020682; AAX08699.1; -; mRNA.
DR EMBL; BT020868; AAX08885.1; -; mRNA.
DR EMBL; BT020916; AAX08933.1; -; mRNA.
DR EMBL; BT026158; ABG66997.1; -; mRNA.
DR EMBL; BC123718; AAI23719.1; -; mRNA.
DR RefSeq; NP_001015609.1; NM_001015609.1.
DR RefSeq; XP_005203558.1; XM_005203501.3.
DR RefSeq; XP_005203559.1; XM_005203502.3.
DR RefSeq; XP_010801059.1; XM_010802757.2.
DR AlphaFoldDB; Q5EA87; -.
DR SMR; Q5EA87; -.
DR STRING; 9913.ENSBTAP00000049355; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR PaxDb; Q5EA87; -.
DR PRIDE; Q5EA87; -.
DR GeneID; 515771; -.
DR KEGG; bta:515771; -.
DR CTD; 8703; -.
DR eggNOG; KOG3916; Eukaryota.
DR HOGENOM; CLU_044391_1_2_1; -.
DR InParanoid; Q5EA87; -.
DR OrthoDB; 1201618at2759; -.
DR TreeFam; TF312834; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
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; IBA:GO_Central.
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..396
FT /note="Beta-1,4-galactosyltransferase 3"
FT /id="PRO_0000080535"
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..396
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 341..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..137
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 199..200
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 263..266
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 294..296
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 306
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 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..122
FT /evidence="ECO:0000250"
FT DISULFID 193..212
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="K -> E (in Ref. 1; AAX08699 and 2; AAI23719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 44371 MW; 8C2611ED7C26250D CRC64;
MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR EQEPAFDYSH PHDVYSNLSH
MPGAPVAPGG LPAPQGLPYC PKRSPLLVGP ISVSFSPVPS LAEIVERNPR VEPGGRYRPA
RCEPRSRTAI IVPHRAREHH LRLLLYHLHP FLQRQQLAYG IYVIHQAGNG TFNRAKLLNV
GVREALRDEE WDCLFLHDVD LLPENDHNLY VCDPRGPRHV AVAMNKFGYS LPYPQYFGGV
SALTPDQYLK MNGFPNEYWG WGGEDDDIAT RVRLAGMKIS RPPTSVGHYK MVKHRGDKGN
EENPHRFDLL VRTQNSWTQD GMNSLTYQLL SRELGPLYTN ITADIGTDPR GPRTSSGPHY
PPGSSQAFRQ EMLQRRPPAR PGPLPTANHT APHGSH
