Otogelin-like/Mucin, TIL domain
IPR058753
Definition
This entry describes a trypsin inhibitor-like (TIL) cysteine rich domain found in Otogelin, Otogelin-like proteins and some Mucin proteins from eukaryotes. The TIL domain is characterised by the presence of five disulphide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues PMID:11353828. Otogelin is a structurally complex glycoprotein with specialised roles in the inner ear membranes. While it shares some structural similarities with mucins, including von Willebrand factor-like domains and cysteine-rich regions, it differs in its glycosylation patterns and functions. Otogelin undergoes primarily N-glycosylation and plays a critical role in the organisation of the extracellular matrix within the inner ear [[cite:PMID:9405633], [cite:PMID:31776257], [cite:PMID:17911254]]. Otogelin proteins are specific to the acellular membranes of the inner ear. Otogelin and Otogelin-like proteins are potentially involved in the anchoring of otoconial membranes and cupulae to the underlying neuroepithelia in the vestibule. They may also play a role in the organisation and stabilisation of the fibrillar network that composes the tectorial membrane in the cochlea. Additionally, these proteins might be involved in mechanotransduction processes, which are crucial for the conversion of mechanical stimuli in neural signals in the auditory system [[cite:PMID:9405633], [cite:PMID:31776257]]. Mucins like MUC5B and MUC19 are heavily O-glycosylated, gel-forming proteins that provide lubrication and protective barriers on mucosal epithelial surfaces [[cite:PMID:40004452], [cite:PMID:17950376]].
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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