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   27-MAR-2024, entry version 216.
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 = a 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-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC         beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + 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   GlyCosmos; P08037; 2 sites, No reported glycans.
DR   iPTMnet; P08037; -.
DR   PaxDb; 9913-ENSBTAP00000020286; -.
DR   PeptideAtlas; P08037; -.
DR   Ensembl; ENSBTAT00000020286.5; ENSBTAP00000020286.5; ENSBTAG00000015249.5. [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; NAMVGKC; -.
DR   OrthoDB; 306273at2759; -.
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-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
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 cell types or 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: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: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:0005989; P:lactose biosynthetic process; IDA:CAFA.
DR   GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
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:0061755; P:positive regulation of circulating fibrinogen levels; ISS:UniProtKB.
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   CDD; cd00899; b4GalT; 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; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF5; BETA-1,4-GALACTOSYLTRANSFERASE 1; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//