Asn175

Asn175 is a residue designation used in protein sequence and structure annotation to refer to the asparagine located at position 175 in a given polypeptide chain. The number is specific to a particular protein sequence and can shift in alternative isoforms or after sequence insertions or deletions. Consequently, Asn175 carries the properties of the asparagine side chain within that context.

Asparagine side chains participate in hydrogen bonding and polar interactions, contributing to local structure and, in secreted or membrane proteins, potential sites for N-linked glycosylation. N-linked glycosylation attaches a preassembled oligosaccharide to the amide nitrogen of asparagine in the consensus sequence N-X-S/T, where X is any residue except proline. If Asn175 lies within such a motif and is solvent-exposed, it may be glycosylated in the endoplasmic reticulum and Golgi apparatus, influencing folding, stability, trafficking, and interactions. However, glycosylation is determined by the motif, accessibility, and cellular context; not all Asn175 residues are glycosylated.

Mutations at Asn175 can have functional consequences that are protein-dependent. Substituting the residue with one that cannot be glycosylated (for example, Asp or Gln) may disrupt glycosylation patterns or alter hydrogen-bond networks, potentially affecting folding or activity. Experimental studies often use site-directed mutagenesis at such positions to probe structural roles or regulatory mechanisms.

In structural data, Asn175 is referenced by residue numbering in the respective protein's chain, and its environment (secondary structure, proximity to active sites or interfaces) determines its role. It may be part of a loop, an interface, or a catalytic or binding region in specific proteins.