B4GT1_BOVIN
ID B4GT1_BOVIN Reviewed; 402 AA.
AC P08037; Q0VC05; Q8MIG0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Beta-1,4-galactosyltransferase 1 {ECO:0000305};
DE Short=Beta-1,4-GalTase 1;
DE Short=Beta4Gal-T1;
DE Short=b4Gal-T1;
DE EC=2.4.1.- {ECO:0000269|PubMed:9405390};
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.38 {ECO:0000269|PubMed:9405390};
DE AltName: Full=Lactose synthase A protein;
DE EC=2.4.1.22;
DE AltName: Full=N-acetyllactosamine synthase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.90 {ECO:0000269|PubMed:9405390};
DE AltName: Full=Nal synthase;
DE AltName: Full=Neolactotriaosylceramide beta-1,4-galactosyltransferase {ECO:0000303|PubMed:9405390};
DE EC=2.4.1.275 {ECO:0000269|PubMed:9405390};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
DE Contains:
DE RecName: Full=Processed beta-1,4-galactosyltransferase 1;
GN Name=B4GALT1; Synonyms=GALT, GGTB2;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=2502398; DOI=10.1111/j.1432-1033.1989.tb14915.x;
RA D'Agostaro G., Bendiak B., Tropak M.;
RT "Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-
RT galactosyltransferase.";
RL Eur. J. Biochem. 183:211-217(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-402.
RX PubMed=2419911; DOI=10.1073/pnas.83.6.1573;
RA Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R.,
RA Hollis G.F.;
RT "Bovine galactosyltransferase: identification of a clone by direct
RT immunological screening of a cDNA expression library.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-402.
RX PubMed=3014508; DOI=10.1073/pnas.83.13.4720;
RA Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.;
RT "Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-
RT 4)galactosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986).
RN [5]
RP SEQUENCE REVISION TO 164; 256 AND 265.
RA Qasba P.K., Narimatsu H., Masibay A.S.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=2503823; DOI=10.1073/pnas.86.15.5733;
RA Masibay A.S., Qasba P.K.;
RT "Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-165.
RX PubMed=2105947; DOI=10.1016/s0021-9258(19)39770-4;
RA Russo R.N., Shaper N.L., Shaper J.H.;
RT "Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts
RT encode two forms of the protein with different amino-terminal domains. In
RT vitro translation experiments demonstrate that both the short and the long
RT forms of the enzyme are type II membrane-bound glycoproteins.";
RL J. Biol. Chem. 265:3324-3331(1990).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-90.
RX PubMed=2117606; DOI=10.1016/s0021-9258(18)77282-7;
RA Yadav S.P., Brew K.;
RT "Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-
RT galactosyltransferase involved in UDP-galactose binding by differential
RT labeling.";
RL J. Biol. Chem. 265:14163-14169(1990).
RN [9]
RP DISULFIDE BOND.
RX PubMed=1898734; DOI=10.1016/s0021-9258(17)35227-4;
RA Yadav S.P., Brew K.;
RT "Structure and function in galactosyltransferase. Sequence locations of
RT alpha-lactalbumin binding site, thiol groups, and disulfide bond.";
RL J. Biol. Chem. 266:698-703(1991).
RN [10]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9405390; DOI=10.1074/jbc.272.51.31979;
RA Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G.,
RA van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.;
RT "A family of human beta4-galactosyltransferases. Cloning and expression of
RT two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-
RT galactosyltransferases, beta4Gal-T2 and beta4Gal-T3.";
RL J. Biol. Chem. 272:31979-31991(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH SUBSTRATE,
RP AND DISULFIDE BONDS.
RX PubMed=10393171; DOI=10.1093/emboj/18.13.3546;
RA Gastinel L.N., Cambillau C., Bourne Y.;
RT "Crystal structures of the bovine beta4galactosyltransferase catalytic
RT domain and its complex with uridine diphosphogalactose.";
RL EMBO J. 18:3546-3557(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE
RP AND MANGANESE IONS.
RX PubMed=11419947; DOI=10.1006/jmbi.2001.4757;
RA Ramakrishnan B., Qasba P.K.;
RT "Crystal structure of lactose synthase reveals a large conformational
RT change in its catalytic component, the beta1,4-galactosyltransferase-I.";
RL J. Mol. Biol. 310:205-218(2001).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE
RP AND MANGANESE IONS.
RX PubMed=12051854; DOI=10.1016/s0022-2836(02)00020-7;
RA Ramakrishnan B., Balaji P.V., Qasba P.K.;
RT "Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal
RT reveals an oligosaccharide acceptor binding site.";
RL J. Mol. Biol. 318:491-502(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN
RP COMPLEX WITH SUBSTRATE AND MANGANESE IONS, MUTAGENESIS OF TRP-314,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12927542; DOI=10.1016/s0022-2836(03)00790-3;
RA Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.;
RT "The role of tryptophan 314 in the conformational changes of beta1,4-
RT galactosyltransferase-I.";
RL J. Mol. Biol. 331:1065-1076(2003).
CC -!- FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form
CC catalyzes the production of lactose in the lactating mammary gland and
CC could also be responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. {ECO:0000269|PubMed:12927542}.
CC -!- FUNCTION: [Processed beta-1,4-galactosyltransferase 1]: The cell
CC surface form functions as a recognition molecule during a variety of
CC cell to cell and cell to matrix interactions, as those occurring during
CC development and egg fertilization, by binding to specific
CC oligosaccharide ligands on opposing cells or in the extracellular
CC matrix. The secreted form is responsible for the synthesis of complex-
CC type to N-linked oligosaccharides in many glycoproteins as well as the
CC carbohydrate moieties of glycolipids (PubMed:9405390).
CC {ECO:0000269|PubMed:9405390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC Evidence={ECO:0000269|PubMed:12927542, ECO:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC Evidence={ECO:0000269|PubMed:9405390, ECO:0000305|PubMed:12927542};
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:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000269|PubMed:9405390};
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:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000269|PubMed:9405390};
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:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000269|PubMed:9405390};
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:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000269|PubMed:9405390};
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:0000269|PubMed:9405390};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000269|PubMed:9405390};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P15291};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.034 mM for UDP-galactose {ECO:0000269|PubMed:9405390};
CC KM=0.53 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390};
CC KM=9.6 mM for D-GlcNAc {ECO:0000269|PubMed:9405390};
CC Vmax=73 pmol/min/mg enzyme towards UDP-galactose
CC {ECO:0000269|PubMed:9405390};
CC Vmax=44.1 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC Vmax=56.8 pmol/min/mg enzyme towards D-GlcNAc
CC {ECO:0000269|PubMed:9405390};
CC Vmax=297 nmol/h/mg enzyme towards lactotriaosylceramide (d18:1(4E))
CC {ECO:0000269|PubMed:9405390};
CC Vmax=333 nmol/h/mg enzyme towards lactopentaosylceramide (d18:1(4E))
CC {ECO:0000269|PubMed:9405390};
CC Vmax=40.3 nmol/h/mg enzyme towards GlcCer
CC {ECO:0000269|PubMed:9405390};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9405390}.
CC -!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form
CC lactose synthase (PubMed:10393171, PubMed:11419947, PubMed:12051854,
CC PubMed:12927542). Interacts (via N-terminal cytoplasmic domain) with
CC UBE2Q1 (via N-terminus); the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:10393171,
CC ECO:0000269|PubMed:11419947, ECO:0000269|PubMed:12051854,
CC ECO:0000269|PubMed:12927542}.
CC -!- INTERACTION:
CC P08037; P29752: Lalba; Xeno; NbExp=10; IntAct=EBI-1031436, EBI-1031454;
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack
CC membrane {ECO:0000250|UniProtKB:P15535}; Single-pass type II membrane
CC protein. Cell membrane; Single-pass type II membrane protein. Cell
CC surface. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}.
CC Note=Found in trans cisternae of Golgi. B4GALT1 cell surface expression
CC is regulated by UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535}.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Golgi apparatus, Golgi stack
CC membrane; Single-pass type II membrane protein. Note=Found in trans
CC cisternae of Golgi.
CC -!- SUBCELLULAR LOCATION: [Processed beta-1,4-galactosyltransferase 1]:
CC Secreted {ECO:0000305|PubMed:9405390}. Note=Soluble form found in body
CC fluids. {ECO:0000269|PubMed:9405390}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long; Synonyms=Cell surface;
CC IsoId=P08037-1; Sequence=Displayed;
CC Name=Short; Synonyms=Golgi complex;
CC IsoId=P08037-2; Sequence=VSP_018801;
CC -!- TISSUE SPECIFICITY: Detected in milk (at protein level).
CC {ECO:0000269|PubMed:9405390}.
CC -!- PTM: The soluble form derives from the membrane forms by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR EMBL; X14558; CAA32695.1; -; mRNA.
DR EMBL; BC120415; AAI20416.1; -; mRNA.
DR EMBL; M13214; AAA30534.1; -; mRNA.
DR EMBL; AF515786; AAM54035.2; -; mRNA.
DR EMBL; M25398; AAA30533.1; -; Genomic_DNA.
DR EMBL; J05217; AAA30559.1; -; mRNA.
DR PIR; I45897; I45897.
DR PIR; S05018; S05018.
DR RefSeq; NP_803478.1; NM_177512.2.
DR PDB; 1FGX; X-ray; 2.40 A; A/B=115-402.
DR PDB; 1FR8; X-ray; 2.40 A; A/B=115-402.
DR PDB; 1NF5; X-ray; 2.00 A; B/D=130-402.
DR PDB; 1NHE; X-ray; 2.50 A; B/D=130-402.
DR PDB; 1NKH; X-ray; 2.00 A; B/D=130-402.
DR PDB; 1NMM; X-ray; 2.00 A; B/D=130-402.
DR PDB; 1NQI; X-ray; 2.00 A; B/D=130-402.
DR PDB; 1NWG; X-ray; 2.32 A; B/D=130-402.
DR PDB; 1O0R; X-ray; 2.30 A; A/B=130-402.
DR PDB; 1O23; X-ray; 2.32 A; B/D=130-402.
DR PDB; 1OQM; X-ray; 2.10 A; B/D=130-402.
DR PDB; 1PZT; X-ray; 1.92 A; A=130-402.
DR PDB; 1PZY; X-ray; 2.30 A; B/D=130-402.
DR PDB; 1TVY; X-ray; 2.30 A; A/B=130-402.
DR PDB; 1TW1; X-ray; 2.30 A; A/B=130-402.
DR PDB; 1TW5; X-ray; 2.30 A; A/B=130-402.
DR PDB; 1YRO; X-ray; 1.90 A; B/D=130-402.
DR PDB; 2FYC; X-ray; 2.00 A; B/D=130-402.
DR PDB; 2FYD; X-ray; 2.00 A; B/D=130-400.
DR PDB; 4KRV; X-ray; 2.40 A; A/B=130-402.
DR PDBsum; 1FGX; -.
DR PDBsum; 1FR8; -.
DR PDBsum; 1NF5; -.
DR PDBsum; 1NHE; -.
DR PDBsum; 1NKH; -.
DR PDBsum; 1NMM; -.
DR PDBsum; 1NQI; -.
DR PDBsum; 1NWG; -.
DR PDBsum; 1O0R; -.
DR PDBsum; 1O23; -.
DR PDBsum; 1OQM; -.
DR PDBsum; 1PZT; -.
DR PDBsum; 1PZY; -.
DR PDBsum; 1TVY; -.
DR PDBsum; 1TW1; -.
DR PDBsum; 1TW5; -.
DR PDBsum; 1YRO; -.
DR PDBsum; 2FYC; -.
DR PDBsum; 2FYD; -.
DR PDBsum; 4KRV; -.
DR AlphaFoldDB; P08037; -.
DR SMR; P08037; -.
DR IntAct; P08037; 1.
DR STRING; 9913.ENSBTAP00000020286; -.
DR BindingDB; P08037; -.
DR ChEMBL; CHEMBL3214; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR MoonProt; P08037; -.
DR iPTMnet; P08037; -.
DR PaxDb; P08037; -.
DR PeptideAtlas; P08037; -.
DR PRIDE; P08037; -.
DR Ensembl; ENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-1]
DR GeneID; 281781; -.
DR KEGG; bta:281781; -.
DR CTD; 2683; -.
DR VEuPathDB; HostDB:ENSBTAG00000015249; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000155244; -.
DR HOGENOM; CLU_044391_0_1_1; -.
DR InParanoid; P08037; -.
DR OMA; KDCISSH; -.
DR OrthoDB; 1201618at2759; -.
DR TreeFam; TF312834; -.
DR BRENDA; 2.4.1.133; 908.
DR BRENDA; 2.4.1.38; 908.
DR BRENDA; 2.4.1.90; 908.
DR Reactome; R-BTA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-BTA-5653890; Lactose synthesis.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-975577; N-Glycan antennae elongation.
DR SABIO-RK; P08037; -.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; P08037; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000015249; Expressed in parenchyma of mammary gland and 104 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0030057; C:desmosome; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004461; F:lactose synthase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl.
DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0006012; P:galactose metabolic process; IEA:Ensembl.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; IDA:CAFA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR GO; GO:0042125; P:protein galactosylation; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:CAFA.
DR GO; GO:0060046; P:regulation of acrosome reaction; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lipid metabolism; Manganese;
KW Membrane; Metal-binding; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="Beta-1,4-galactosyltransferase 1"
FT /id="PRO_0000012276"
FT CHAIN ?..402
FT /note="Processed beta-1,4-galactosyltransferase 1"
FT /id="PRO_0000296228"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..402
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 77..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..191
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 226..228
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 253..254
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 314
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 316..319
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT BINDING 347..349
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 359
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2117606"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..176
FT DISULFID 247..266
FT VAR_SEQ 1..13
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018801"
FT MUTAGEN 314
FT /note="W->A: Reduces galactosyltransferase activity,
FT lactose synthase activity and substrate binding by 99%."
FT /evidence="ECO:0000269|PubMed:12927542"
FT CONFLICT 65..66
FT /note="HG -> QA (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> I (in Ref. 1; CAA32695)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="P -> L (in Ref. 1; CAA32695)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..206
FT /note="IL -> MV (in Ref. 1; CAA32695)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="F -> L (in Ref. 3; AAA30534)"
FT /evidence="ECO:0000305"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1TVY"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:1FR8"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1NF5"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:1YRO"
SQ SEQUENCE 402 AA; 44843 MW; FABF94E74E0C6F81 CRC64;
MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL PQLVGVHPPL
QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS NLDAYSHPGP GPGPGSNLTS
APVPSTTTRS LTACPEESPL LVGPMLIEFN IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH
KVAIIIPFRN RQEHLKYWLY YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL
KDYDYNCFVF SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ
FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD KKNEPNPQRF
DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT PS
