Description
The egg peptide speract receptor is a transmembrane glycoprotein of about
500 amino acids PUBMED:2538832. 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 extracellular
domain contains 4 repeats of a well-conserved region, which spans 115
amino acids and contains 6 conserved cysteines. A similar domain is also
found towards the C-terminus of macrophage scavenger receptor type I PUBMED:1978939, a membrane glycoprotein implicated in the pathologic deposition of
cholesterol 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) PUBMED:2251254. Immunohistochemical studies have indicated the presence of scavenger
receptors in the macrophages of lipid-rich atherosclerotic lesions, suggesting the involvement of these receptors in atherogenesis PUBMED:2251254.
The macrophage scavenger receptor is trimeric and has unusual ligand-binding
properties PUBMED:2300204. 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 PUBMED:2300204.
Description text from InterPro entry IPR003543
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