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Vitelline membrane outer layer 1 homolog (VMO1) is a secreted protein originally characterized in the outer layer of avian egg vitelline membranes, where it binds tightly to ovomucin fibrils and contributes to the membrane's structure and antimicrobial function[1][3]. In mammals, such as humans, VMO1 is a 21 kDa secreted protein not linked to cytokine receptor function; it is subject to a rare post-translational modification called *C*-mannosylation, which affects its intracellular stability (destabilizing when mannosylated at a specific tryptophan residue), but does not appear to regulate secretion[3]. In humans, VMO1 has been found to interact with lysozyme C in tear film and may have extracellular structural or protective roles[3]. There are no known drugs, clinical biomarker applications, or notable safety concerns associated with the protein, and it is not classified as a therapeutic target.
Not applicable (no known drugs target VMO1 directly)
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