GALK2 acts as a galactokinase when galactose is present at high concentrations. GALK2 may be involved in a salvage pathway for the reutilization of free GalNAc derived from the degradation of complex carbohydrates. GALK2 has been reported to participate in pathways , such as Amino sugar and nucleotide sugar metabolism, Galactose metabolism and Metabolic pathways.
Galactose Mutarotase (GALM) is a cytoplasmic enzyme that belongs to the Aldose Epimerase family. GALM is a Mutarotase that converts α-Aldose to the β-Anomer. GALM is active on D-Glucose, L-Arabinose, D-Xylose, D-Galactose, Maltose and Lactose. GALM may be required for normal Galactose metabolism by maintaining the equilibrium of α- and β- anomers of Galactose.
GALNT2, also known as GalNAc-T2, is a member of the GalNAc-transferases family. Members of this family transfer an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. GALNT2 may play a role in lipid metabolism. It catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b.
Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults.
N-acetylgalactosaminyltransferase 7(GALNT7) is expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.It belongs to the glycosyltransferase 2 family and galNAc-T subfamily. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation.
Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1, also known as Polypeptide GalNAc transferase-like protein 1, Protein-UDP acetylgalactosaminyltransferase-like protein 1, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1, GalNAC-T-like protein 1, pp-GaNTase-like protein 1 and GALNTL1, belongs to the glycosyltransferase 2 family. GALNTL1 plays an important role in the protein modification and protein glycosylation process. GALNTL1 uses the manganese and calcium ion as a cofactor, may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, transfers the N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD180, also known as RP105, is a B-cell surface molecule belonging to the family of pathogen receptors, Toll-like receptors (TLR). CD180 has an extracellular leucine-rich repeats and a short cytoplasmic tail. CD180 / RP105 interact with an extracellular molecule named MD1 and then together form the cell surface receptor complex RP105 / MD1 which induces B-cell activation in humans and mice, leading to proliferation and up-regulation of a costimulatory molecule, B7.2 / CD86. CD180 / RP105 also has a role in LPS response because B cells lacking RP105 show hyporesponsiveness to LPS.
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