SCGB1C2

Secretoglobin family 1C member 2, a small secreted protein (~10 kDa, 95 AA) that forms homodimers with a four-helix bundle structure creating a hydrophobic pocket for binding small lipophilic ligands. Member of the secretoglobin (uteroglobin) superfamily of secretory proteins involved in immunomodulation, anti-inflammatory responses, and ligand transport. Expression is tissue-enhanced in pancreas, retina (Müller glia and photoreceptors), and testis (spermatocytes/spermatids), suggesting specialized roles in these organs. Like other secretoglobins, SCGB1C2 likely binds and sequesters hydrophobic molecules (steroids, retinoids, lipid mediators) to regulate their local availability and modulate inflammation or signaling. The protein is secreted into extracellular fluids where it functions as a ligand carrier/buffer. Specific binding partners and detailed biochemical function remain to be determined experimentally. IMPORTANT CAVEAT (falcon deep research): SCGB1C2 is a poorly-characterized secretoglobin with essentially no SCGB1C2-specific functional literature. No substrate/ligand specificity, catalytic activity, receptor binding, or pathway placement has been directly reported for SCGB1C2 itself; the lipid-binding and ligand-carrier roles are family-level structural inferences, not direct experimental findings. SCGB1C2 also has extreme sequence similarity to its paralog SCGB1C1 such that all of its tryptic peptides overlap with SCGB1C1 variants, making it a neXtProt "missing protein" that cannot be uniquely validated by standard mass spectrometry and increasing the risk that proteomics or interactome hits are mis-assigned between the two near-identical genes. Functional and localization claims here should be treated as provisional.