Anti-DPM1 antibody [5C5A7]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

DPM1 also known as dolichyl-phosphate beta-D-mannosyltransferase subunit 1 is an important component of the dolichol-phosphate mannose synthase complex. It has a molecular mass of approximately 29 kDa. DPM1 is localized in the endoplasmic reticulum membrane where it plays a significant role in the synthesis of glycosylphosphatidylinositol (GPI) anchors and protein glycosylation.

Biological function summary

This protein is essential in transferring mannose from GDP-mannose to dolichol phosphate a reaction that synthesizes dolichol-phosphate mannose (DPM). DPM is an important donor substrate in the glycan assembly pathways. DPM1 does not have a transmembrane domain unlike other components of the DPM synthase complex. Association with other complex subunits like DPM2 and DPM3 stabilize its structure and function within the cell ensuring glycosylation processes proceed correctly.

Pathways

Glycosylation is one of the fundamental pathways DPM1 participates in. Its role in glycosylation links it to the protein N-glycosylation pathway and GPI anchor biosynthesis pathway. DPM1 interacts with proteins such as DPM2 in the synthase complex to facilitate the conversion process necessary for glycosylation of proteins and lipids impacting various cellular processes like cell-cell adhesion and protein folding.

Associated diseases and disorders

DPM1 molecule relates to congenital disorders of glycosylation (CDG) particularly CDG-Ie. Mutations in the gene encoding DPM1 can disrupt enzymatic activity leading to issues in glycosylation which manifest in multisystem disorders. The connection of DPM1 to these disorders often involves deficiencies in dolichol-phosphate mannose production. Similarly defects in associated proteins like DPM2 can compound the glycosylation defects exacerbating disease symptoms.