MRC2
Domain
C-type lectin domains 3 to 8 are not required for calcium-dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner.
Fibronectin type-II domain mediates collagen-binding.
Ricin B-type lectin domain contacts with the second C-type lectin domain.
Function
May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).
Post-translational modifications
N-glycosylated.
Tissue Specificity
Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney.
Cellular localization
- Membrane
- Single-pass type I membrane protein
Alternative names
CD280, CLEC13E, ENDO180, KIAA0709, UPARAP, MRC2, C-type mannose receptor 2, C-type lectin domain family 13 member E, Endocytic receptor 180, Macrophage mannose receptor 2, Urokinase-type plasminogen activator receptor-associated protein, UPAR-associated protein, Urokinase receptor-associated protein