|PROSITE documentation PDOC51914|
The mannose 6-phosphate (Man-6-P) receptor homology (MRH) domain-containing family of proteins, which include recycling receptors (mannose 6-phosphate receptors, MRPs), resident endoplasmic reticulum (ER) proteins (glucosidase II β-subunit, XTP3-B, OS-9), and a Golgi glycosyltransferase (GlcNAc-phosphotransferase γ-subunit), are characterized by the presence of one or more MRH domains. Many MRH domains act as lectins and bind specific phosphorylated (MPRs) or non phosphorylated (glycosidase II β-subunit (GIIβ, 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 [1,2,3,4,5,6,7].
The overall fold of the MRH domain comprises a flattened β-barrel structure consisting of nine β-strands organized into two orthogonally oriented anti-parallel β-sheets, β1-β4 and β5-β9, with β9 interjecting between β7 and β8 (see <PDB:1SZ0>). MRH domains display a similar size and conservation of residues, including cysteines involved in disulfide bonding. The GIIβ MRH domain contains only two disulfide bonds in contrast to the three (OS-9, CD-MPR, CI-MPR domain 5) or four (CI-MPR domains 3 and 9) [3,4].
The profile we developed covers the entire MRH domain.Last update:
February 2020 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins.|
|Source||Curr. Biol. 11:R499-R501(2001).|
|2||Authors||Castonguay A.C. Olson L.J. Dahms N.M.|
|Title||Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.|
|Source||Biochim. Biophys. Acta. 1810:815-826(2011).|
|3||Authors||Olson L.J. Orsi R. Alculumbre S.G. Peterson F.C. Stigliano I.D. Parodi A.J. D'Alessio C. Dahms N.M.|
|Title||Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.|
|Source||J. Biol. Chem. 288:16460-16475(2013).|
|4||Authors||Olson L.J. Orsi R. Peterson F.C. Parodi A.J. Kim J.J. D'Alessio C. Dahms N.M.|
|Title||Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.|
|5||Authors||D'Alessio C. Dahms N.M.|
|Title||Glucosidase II and MRH-domain containing proteins in the secretory pathway.|
|Source||Curr. Protein. Pept. Sci. 16:31-48(2015).|
|6||Authors||Szathmary R. Bielmann R. Nita-Lazar M. Burda P. Jakob C.A.|
|Title||Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.|
|Source||Mol. Cell. 19:765-775(2005).|