CD59 GLYCOPROTEIN

CD59 (CD59 Molecule (CD59 Blood Group)) is a Protein Coding gene. Diseases associated with CD59 include Hemolytic Anemia, Cd59-Mediated, With Or Without Immune-Mediated Polyneuropathy and Hemolytic Anemia. Among its related pathways are Creation of C4 and C2 activators and Transport to the Golgi and subsequent modification. Gene Ontology (GO) annotations related to this gene include complement binding.

Cd59 Molecule (Cd59 Blood Group)

Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.
The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.

Blood coagulation Source: ProtInc
Cell surface receptor signaling pathway Source: ProtInc
COPII vesicle coating Source: Reactome
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: Reactome
Negative regulation of activation of membrane attack complex Source: GO_Central
Neutrophil degranulation Source: Reactome
Regulation of complement activation Source: MGI
Regulation of complement-dependent cytotoxicity Source: MGI

Secreted; Cell membrane. Soluble form found in a number of tissues.

Hemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59): An autosomal recessive disorder characterized by infantile onset of chronic hemolysis and a relapsing-remitting polyneuropathy, often exacerbated by infection, and manifested as hypotonia, limb muscle weakness, and hyporeflexia.

N- and O-glycosylated. The N-glycosylation mainly consists of a family of biantennary complex-type structures with and without lactosamine extensions and outer arm fucose residues. Also significant amounts of triantennary complexes (22%). Variable sialylation also present in the Asn-43 oligosaccharide. The predominant O-glycans are mono-sialylated forms of the disaccharide, Gal-beta-1,3GalNAc, and their sites of attachment are probably on Thr-76 and Thr-77. The GPI-anchor of soluble urinary CD59 has no inositol-associated phospholipid, but is composed of seven different GPI-anchor variants of one or more monosaccharide units. Major variants contain sialic acid, mannose and glucosamine. Sialic acid linked to an N-acetylhexosamine-galactose arm is present in two variants.
Glycated. Glycation is found in diabetic subjects, but only at minimal levels in nondiabetic subjects. Glycated CD59 lacks MAC-inhibitory function and confers to vascular complications of diabetes.