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PROSITE documentation PDOC51914 [for PROSITE entry PS51914]

MRH domain profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

MRH, PS51914; MRH domain profile  (MATRIX)


References

1AuthorsMunro S.
TitleThe MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins.
SourceCurr. Biol. 11:R499-R501(2001).
PubMed ID11470418
DOI10.1016/s0960-9822(01)00302-5

2AuthorsCastonguay A.C. Olson L.J. Dahms N.M.
TitleMannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.
SourceBiochim. Biophys. Acta. 1810:815-826(2011).
PubMed ID21723917
DOI10.1016/j.bbagen.2011.06.016

3AuthorsOlson L.J. Orsi R. Alculumbre S.G. Peterson F.C. Stigliano I.D. Parodi A.J. D'Alessio C. Dahms N.M.
TitleStructure 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.
SourceJ. Biol. Chem. 288:16460-16475(2013).
PubMed ID23609449
DOI10.1074/jbc.M113.450239

4AuthorsOlson L.J. Orsi R. Peterson F.C. Parodi A.J. Kim J.J. D'Alessio C. Dahms N.M.
TitleCrystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.
SourceBiochemistry 54:4097-4111(2015).
PubMed ID26062005
DOI10.1021/acs.biochem.5b00256

5AuthorsD'Alessio C. Dahms N.M.
TitleGlucosidase II and MRH-domain containing proteins in the secretory pathway.
SourceCurr. Protein. Pept. Sci. 16:31-48(2015).
PubMed ID25692846
DOI10.2174/1389203716666150213160438

6AuthorsSzathmary R. Bielmann R. Nita-Lazar M. Burda P. Jakob C.A.
TitleYos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.
SourceMol. Cell. 19:765-775(2005).
PubMed ID16168372
DOI10.1016/j.molcel.2005.08.015



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