3 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0005044 | IPR003543 |
| GO:0006898 | IPR003543 |
| GO:0016020 | IPR003543 |
| Type: | Domain | Name: | Macrophage scavenger receptor |
| Description: | The egg peptide speract receptor is a transmembrane glycoprotein of about 500 amino acids []. Topologically, it comprises a large extracellular domain of about 450 residues, followed by a transmembrane domain and a short cytoplasmic region of about 12 amino acids. The extracellulardomain contains 4 repeats of a well-conserved region, which spans 115 amino acids and contains 6 conserved cysteines. A similar domain is alsofound towards the C terminus of macrophage scavenger receptor type I [], a membrane glycoprotein implicated in the pathologic deposition ofcholesterol in arterial walls during artherogenesis, and in the CD5 glycoprotein, which acts as a receptor in regulating T-cell proliferation.The type I and type II human scavenger receptors are similar to their bovine, rabbit and murine counterparts. They consist of 6 domains:cytoplasmic (I); membrane-spanning (II); spacer (III); alpha-helical coiled- coil (IV); collagen-like (V); and a type-specific C-terminal (VI) []. Immunohistochemical studies have indicated the presence of scavengerreceptors in the macrophages of lipid-rich atherosclerotic lesions, suggesting the involvement of these receptors in atherogenesis []. The macrophage scavenger receptor is trimeric and has unusual ligand-binding properties []. The trimeric structure of the bovine type I scavenger receptor contains 3 extracellular C-terminal cysteine-rich domains connected to the transmembrane domain by a long fibrous stalk. The stalk structure,which consists of an alpha-helical coiled coil and a collagen-like triple helix, has not previously been observed in an integral membrane protein []. | Short Name: | Macro_scav_rcpt |
| GO Term | Gene Name |
|---|---|
| GO:0005044 | IPR003543 |
| GO:0006898 | IPR003543 |
| GO:0016020 | IPR003543 |
