LCN8

Members of the lipocalin family, such as LCN8, have a common structure consisting of an 8-stranded antiparallel beta-barrel that forms a cup-shaped ligand-binding pocket or calyx. Lipocalins generally bind small hydrophobic ligands and transport them to specific cells (Suzuki et al., 2004 [PubMed 15363845]).[supplied by OMIM, Aug 2009]

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in human LCN8 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

Biological processes and signaling networks where the LCN8 gene in human plays a role, providing insight into its function and relevance in health or disease.

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.

Describes the biological processes, cellular components, and molecular functions associated with the human LCN8 gene, providing context for its role in the cell.