UniProt functional annotation for P15291



	UniProt functional annotation for P15291

UniProt code: P15291.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed:16157350}.

Function: [Processed beta-1,4-galactosyltransferase 1]: The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. {ECO:0000269|PubMed:16157350}.

Catalytic activity: Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000269|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; Evidence={ECO:0000269|PubMed:16157350};

Catalytic activity: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D- galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507; EC=2.4.1.38; Evidence={ECO:0000269|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933; Evidence={ECO:0000269|PubMed:16157350};

Catalytic activity: Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D- galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP; Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227; EC=2.4.1.90; Evidence={ECO:0000269|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; Evidence={ECO:0000269|PubMed:16157350};

Catalytic activity: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)- Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275; Evidence={ECO:0000250|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500; Evidence={ECO:0000250|UniProtKB:P08037};

Catalytic activity: Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D- galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP; Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264; Evidence={ECO:0000250|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553; Evidence={ECO:0000250|UniProtKB:P08037};

Catalytic activity: Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D- galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl- (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)- beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378; Evidence={ECO:0000250|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549; Evidence={ECO:0000250|UniProtKB:P08037};

Cofactor: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107};

Pathway: Protein modification; protein glycosylation. {ECO:0000269|PubMed:16157350}.

Subunit: Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase. Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107, ECO:0000269|PubMed:7744867}.

Subcellular location: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903, ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:1714903}.

Subcellular location: [Isoform Short]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:1714903}.

Subcellular location: [Processed beta-1,4-galactosyltransferase 1]: Secreted {ECO:0000303|PubMed:2120039}. Note=Soluble form found in body fluids. {ECO:0000303|PubMed:2120039}.

Tissue specificity: Ubiquitously expressed, but at very low levels in fetal and adult brain.

Ptm: The soluble form derives from the membrane forms by proteolytic processing.

Disease: Congenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:11901181}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		[Beta-1,4-galactosyltransferase 1]: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269\|PubMed:16157350}.



Function:		[Processed beta-1,4-galactosyltransferase 1]: The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. {ECO:0000269\|PubMed:16157350}.


Catalytic activity:		Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000269\|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; Evidence={ECO:0000269\|PubMed:16157350};
Catalytic activity:		Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D- galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507; EC=2.4.1.38; Evidence={ECO:0000269\|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933; Evidence={ECO:0000269\|PubMed:16157350};
Catalytic activity:		Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D- galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP; Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227; EC=2.4.1.90; Evidence={ECO:0000269\|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; Evidence={ECO:0000269\|PubMed:16157350};
Catalytic activity:		Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)- Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275; Evidence={ECO:0000250\|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500; Evidence={ECO:0000250\|UniProtKB:P08037};
Catalytic activity:		Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D- galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP; Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264; Evidence={ECO:0000250\|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553; Evidence={ECO:0000250\|UniProtKB:P08037};
Catalytic activity:		Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D- galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl- (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)- beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378; Evidence={ECO:0000250\|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549; Evidence={ECO:0000250\|UniProtKB:P08037};
Cofactor:		Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269\|PubMed:16157350, ECO:0000269\|PubMed:16497331, ECO:0000269\|PubMed:19106107};
Pathway:		Protein modification; protein glycosylation. {ECO:0000269\|PubMed:16157350}.
Subunit:		Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase. Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity). {ECO:0000250\|UniProtKB:P15535, ECO:0000269\|PubMed:16157350, ECO:0000269\|PubMed:16497331, ECO:0000269\|PubMed:19106107, ECO:0000269\|PubMed:7744867}.
Subcellular location:		[Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269\|PubMed:1714903, ECO:0000269\|PubMed:20378551}; Single-pass type II membrane protein. Cell membrane {ECO:0000269\|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269\|PubMed:1714903}. Cell projection, filopodium {ECO:0000250\|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). {ECO:0000250\|UniProtKB:P15535, ECO:0000269\|PubMed:1714903}.
Subcellular location:		[Isoform Short]: Golgi apparatus, Golgi stack membrane {ECO:0000269\|PubMed:1714903}; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi. {ECO:0000269\|PubMed:1714903}.
Subcellular location:		[Processed beta-1,4-galactosyltransferase 1]: Secreted {ECO:0000303\|PubMed:2120039}. Note=Soluble form found in body fluids. {ECO:0000303\|PubMed:2120039}.
Tissue specificity:		Ubiquitously expressed, but at very low levels in fetal and adult brain.
Ptm:		The soluble form derives from the membrane forms by proteolytic processing.
Disease:		Congenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269\|PubMed:11901181}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the glycosyltransferase 7 family. {ECO:0000305}.