UniProtKB - P80225 (B4GT1_RAT)
Protein
Beta-1,4-galactosyltransferase 1
Gene
B4galt1
Organism
Rattus norvegicus (Rat)
Status
Functioni
This protein is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.By similarity
Catalytic activityi
- EC:2.4.1.22By similarityThis reaction proceeds in the forwardBy similarity direction.
- an N-acetyl-β-D-glucosaminyl derivative + UDP-α-D-galactose = a β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl derivative + H+ + UDPBy similarityEC:2.4.1.38By similarityThis reaction proceeds in the forwardBy similarity direction.
- N-acetyl-D-glucosamine + UDP-α-D-galactose = β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine + H+ + UDPBy similarityEC:2.4.1.90By similarityThis reaction proceeds in the forwardBy similarity direction.
- a β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1)-Cer(d18:1(4E)) + UDP-α-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H+ + UDPBy similarityEC:2.4.1.275By similarityThis reaction proceeds in the forwardBy similarity direction.
- β-D-glucosylceramide + UDP-α-D-galactose = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide + H+ + UDPBy similarityThis reaction proceeds in the forwardBy similarity direction.
- a neolactoside IV3-β-GlcNAc-nLc4Cer + UDP-α-D-galactose = β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide + H+ + UDPBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Mn2+By similarity
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
GO - Molecular functioni
- beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: RGD
- cytoskeletal protein binding Source: RGD
- galactosyltransferase activity Source: RGD
- lactose synthase activity Source: RGD
- laminin binding involved in cell-matrix adhesion Source: RGD
- manganese ion binding Source: RGD
- N-acetyllactosamine synthase activity Source: RGD
- UDP-galactosyltransferase activity Source: RGD
GO - Biological processi
- acute inflammatory response Source: RGD
- angiogenesis involved in wound healing Source: RGD
- binding of sperm to zona pellucida Source: RGD
- branching morphogenesis of an epithelial tube Source: RGD
- cell adhesion Source: RGD
- cell-matrix adhesion Source: RGD
- development of secondary sexual characteristics Source: RGD
- epithelial cell development Source: RGD
- extracellular matrix organization Source: RGD
- galactose metabolic process Source: RGD
- glycoprotein biosynthetic process Source: RGD
- lactose biosynthetic process Source: RGD
- leukocyte migration Source: RGD
- mammary gland development Source: RGD
- negative regulation of cell population proliferation Source: RGD
- oligosaccharide biosynthetic process Source: RGD
- penetration of zona pellucida Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of apoptotic process involved in mammary gland involution Source: RGD
- positive regulation of epithelial cell proliferation involved in wound healing Source: RGD
- protein glycosylation Source: RGD
- protein N-linked glycosylation Source: RGD
- regulation of acrosome reaction Source: RGD
- regulation of cell population proliferation Source: RGD
- regulation of cellular component movement Source: RGD
- response to wounding Source: RGD
- wound healing Source: RGD
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 2.4.1.133, 5301 2.4.1.38, 5301 |
SABIO-RKi | P80225 |
UniPathwayi | UPA00378 |
Names & Taxonomyi
Protein namesi | Recommended name: Beta-1,4-galactosyltransferase 1Curated (EC:2.4.1.-)Short name: Beta-1,4-GalTase 1 Short name: Beta4Gal-T1 Short name: b4Gal-T1 Alternative name(s): Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38) Lactose synthase A protein (EC:2.4.1.22) N-acetyllactosamine synthase (EC:2.4.1.90) Nal synthase Neolactotriaosylceramide beta-1,4-galactosyltransferase (EC:2.4.1.275By similarity) UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1 UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1 |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 620900, B4galt1 |
Subcellular locationi
Golgi apparatus
- Golgi stack membrane By similarity; Single-pass type II membrane protein
Extracellular region or secreted
- Secreted By similarity
Plasma membrane
- Cell membrane By similarity; Single-pass type II membrane protein By similarity
Other locations
- filopodium By similarity
Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: RGD
- Golgi cisterna membrane Source: UniProtKB-SubCell
- Golgi trans cisterna Source: RGD
Plasma Membrane
- basolateral plasma membrane Source: RGD
- brush border membrane Source: RGD
- external side of plasma membrane Source: RGD
- plasma membrane Source: RGD
Other locations
- cell surface Source: RGD
- desmosome Source: RGD
- filopodium Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, Cell projection, Golgi apparatus, Membrane, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080531 | 1 – ›32 | Beta-1,4-galactosyltransferase 1Add BLAST | ›32 |
Post-translational modificationi
The soluble form derives from the membrane form by proteolytic processing.
Interactioni
GO - Molecular functioni
- cytoskeletal protein binding Source: RGD
- laminin binding involved in cell-matrix adhesion Source: RGD
(1+)i Sequence
Sequence statusi: Fragments.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketG3V722 | G3V722_RAT | Beta-1,4-galactosyltransferase 1 | B4galt1 B4galt1_mapped, rCG_54921 | 399 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-adjacent residuesi | 15 – 16 | Curated | 2 | |
Non-terminal residuei | 32 | 1 |
Sequence databases
PIRi | S36825 |
Genome annotation databases
UCSCi | RGD:620900, rat |
Cross-referencesi
Sequence databases
PIRi | S36825 |
3D structure databases
ModBasei | Search... |
Genome annotation databases
UCSCi | RGD:620900, rat |
Organism-specific databases
RGDi | 620900, B4galt1 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 2.4.1.133, 5301 2.4.1.38, 5301 |
SABIO-RKi | P80225 |
Family and domain databases
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | B4GT1_RAT | |
Accessioni | P80225Primary (citable) accession number: P80225 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | April 7, 2021 | |
This is version 89 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families