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Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D (SSC5D) is a member of the scavenger receptor cysteine-rich (SRCR) protein superfamily, characterized by the presence of five SRCR domains in its N-terminal region and a large C-terminal mucin-like domain[1][6]. It is a soluble glycoprotein highly expressed in monocytes, macrophages, and T lymphocytes, with notable enrichment in the placenta[2]. SSC5D functions as a pattern recognition receptor (PRR), directly binding both extracellular matrix proteins and pathogen-associated molecular patterns (PAMPs) found on cell walls of Gram-positive and Gram-negative bacteria[1][3][6][7]. Its SRCR domains enable the discrimination and binding of different bacteria, potentially contributing to innate immune defense by recognizing pathogens[1]. No known drugs target SSC5D, and its role as a direct therapeutic target or biomarker has yet to be established.
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