DDOST Antibody – Mouse Monoclonal

This gene encodes a component of the oligosaccharyltransferase complex which catalyzes the transfer of high-mannose oligosaccharides to asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum. The protein complex co-purifies with ribosomes. The product of this gene is also implicated in the processing of advanced glycation endproducts (AGEs), which form from non-enzymatic reactions between sugars and proteins or lipids and are associated with aging and hyperglycemia. [provided by RefSeq, Jul 2008]

DDOST: Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Defects in DDOST are the cause of congenital disorder of glycosylation type 1R (CDG1R). 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. Belongs to the DDOST 48 kDa subunit family.

Protein type: Membrane protein, integral; EC 2.4.99.18; Endoplasmic reticulum; Glycan Metabolism - N-glycan biosynthesis; Transferase

Chromosomal Location of Human Ortholog: 1p36.1

Cellular Component: endoplasmic reticulum membrane; protein complex; membrane; intracellular membrane-bound organelle; endoplasmic reticulum; oligosaccharyl transferase complex; integral to membrane

Molecular Function: protein binding; dolichyl-diphosphooligosaccharide-protein glycotransferase activity; oligosaccharyl transferase activity

Biological Process: SRP-dependent cotranslational protein targeting to membrane; cellular protein metabolic process; translation; T cell activation; response to cytokine stimulus; protein amino acid N-linked glycosylation; innate immune response; protein amino acid glycosylation; protein amino acid N-linked glycosylation via asparagine; gene expression; post-translational protein modification

Disease: Congenital Disorder Of Glycosylation, Type Ir