PROSITE documentation PDOC51914 [for PROSITE entry PS51914]MRH domain profile
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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Munro S. |
| 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). | |
| PubMed ID | 11470418 | |
| DOI | 10.1016/s0960-9822(01)00302-5 |
| 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). | |
| PubMed ID | 21723917 | |
| DOI | 10.1016/j.bbagen.2011.06.016 |
| 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). | |
| PubMed ID | 23609449 | |
| DOI | 10.1074/jbc.M113.450239 |
| 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. | |
| Source | Biochemistry 54:4097-4111(2015). | |
| PubMed ID | 26062005 | |
| DOI | 10.1021/acs.biochem.5b00256 |
| 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). | |
| PubMed ID | 25692846 | |
| DOI | 10.2174/1389203716666150213160438 |
| 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). | |
| PubMed ID | 16168372 | |
| DOI | 10.1016/j.molcel.2005.08.015 |
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