MRH domain
IPR044865
Definition
The mannose 6-phosphate (Man-6-P) receptor homology (MRH) domain is present in recycling receptors (mannose 6-phosphate receptors, MRPs), resident endoplasmic reticulum (ER) proteins (glucosidase 2 beta subunit, Endoplasmic reticulum lectin 1 XTP3-B, OS-9), and in Golgi glycosyltransferase (GlcNAc-phosphotransferase gamma-subunit), which are characterised by the presence of one or more MRH domains. Many MRH domains act as lectins and bind specific phosphorylated (MPRs) or non phosphorylated (glycosidase 2 beta subunit, XTP3-B and OS-9) high mannose-type N-glycans. The MPRs are the only proteins known to bind Man-6-P residues via their MRH domains. The MRH domain can function in protein-carbohydrate and protein-protein interactions [[cite:PMID:1470418], [cite:PMID:21723917], [cite:PMID:23609449], [cite:PMID:26062005], [cite:PMID:25692846], [cite:PMID:16168372]]. This domain has a β-barrel structure formed by nine β-strands organised into two orthogonally oriented antiparallel β-sheet [[cite:PMID:23609449], [cite:PMID:26062005]].
8 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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