Recombinant Rat Asialoglycoprotein receptor 1 (Asgr1), partial (Active)

Function

Transmembrane protein predominantly expressed on hepatocytes that plays a key role in endocytosis of plasma glycoproteins that lack terminal sialic acid residues. Specifically recognizes terminal galactose and N-acetylgalactosamine residues, facilitating the clearance of desialylated glycoproteins from circulation. Plays thereby a role in a variety of physiological processes, such as removal of desialylated platelets, elimination of activated lymphocytes and maintenance of serum glycoprotein homeostasis. Plays a role in the removal of desialylated platelets by activating a feedback loop regulating thrombopoietin (TPO) expression via the JAK2-STAT3 signaling pathway. Contributes also to recognition and elimination of activated lymphocytes by hepatocytes that can act as cytotoxic effectors (By similarity). May also play a physiological role in the regulatory network of lipid homeostasis (By similarity). Upon ligand binding, the receptor-ligand complex is internalized and trafficked to a sorting organelle, where dissociation occurs. The receptor is then recycled back to the cell surface (By similarity)

Subcellular Location

Membrane (Single-pass type II membrane protein)

Tissue Specificity

Expressed exclusively in hepatic parenchymal cells

Subunit

Interacts with LASS2

• Holland E.C. et al. Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence. — Proc. Natl. Acad. Sci. U.S.A. (1984)
• Leung J.O. et al. Characterization of the gene encoding the major rat liver asialoglycoprotein receptor. — J. Biol. Chem. (1985)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Watts C. et al. Isolation and expression of cDNA clones for a rat liver asialoglycoprotein receptor. — Biosci. Rep. (1986)
• Zeng F.Y. et al. Fatty acylation of the rat and human asialoglycoprotein receptors. A conserved cytoplasmic cysteine residue is acylated in all receptor subunits. — J. Biol. Chem. (1996)