Uteroglobin (UG (also SCGB1A1))

Uteroglobin is a small, evolutionarily conserved, steroid-inducible, secreted protein and the founding member of the secretoglobin family, encoded in humans by the SCGB1A1 gene. It forms a homodimer of 70 amino acid subunits linked by disulfide bridges and is primarily expressed in lung club cells and other mucosal epithelia. Its physiological roles include immunomodulation, inhibition of phospholipase A2, binding of various hydrophobic ligands (e.g., progesterone, phospholipids), and anti-inflammatory, antiallergic, and antitumorigenic properties. Uteroglobin acts as a natural homeostatic protein protecting against oxidative damage, inflammation, autoimmunity, and potentially tumorigenesis. Although its detailed molecular mechanisms are not fully elucidated, its multifunctional biological effects and disease associations have rendered it a candidate therapeutic target and biomarker in respiratory medicine, immunology, and nephrology

Other names

Secretoglobin family 1A member 1SCGB1A1BlastokininClub-cell secretory protein (CCSP)Clara-cell 16 kD protein (CC16; CC10)Polychlorinated biphenyl-binding protein (PCB-BP)Uteroglobin-like antigen (UGL)Human protein 1Urine protein 1 (UP-1)Human club cell phospholipid-binding protein (hCCPBP)

Not a typical pharmacological target with a small-molecule agonist or antagonist, but potential mechanisms include immunomodulation, anti-inflammatory action, and inhibition of enzymatic (phospholipase) activity. Its ability to sequester hydrophobic ligands is also a key mechanism