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{
"metadata": {
"accession": "IPR044865",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"profile": {
"PS51914": "MRH domain profile"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR044865",
"name": "MRH domain",
"type": "Domain",
"children": [
{
"accession": "IPR012913",
"name": "Protein OS9-like domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR036607",
"name": "Glucosidase 2 subunit beta-like",
"type": "Domain",
"children": []
},
{
"accession": "IPR056607",
"name": "Elapor1/2, mannose 6-phosphate receptor homology domain",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "MRH domain",
"short": "MRH_dom"
},
"description": [
{
"text": "<p>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:PUB00097532], [cite:PUB00097533], [cite:PUB00097536], [cite:PUB00097535], [cite:PUB00097534], [cite:PUB00097537]].</p>\n\n<p>This domain has a β-barrel structure formed by nine β-strands organised into two orthogonally oriented antiparallel β-sheet [[cite:PUB00097536], [cite:PUB00097535]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00097532": {
"PMID": 1470418,
"ISBN": null,
"volume": "13",
"issue": "11",
"year": 1992,
"title": "Assessment of myocardial viability with 201Tl SPET and reinjection technique: a quantitative approach.",
"URL": null,
"raw_pages": "783-9",
"medline_journal": "Nucl Med Commun",
"ISO_journal": "Nucl Med Commun",
"authors": [
"Mahmood S",
"Buscombe JR",
"Hall ML",
"Jarritt PH",
"Costa DC",
"Ell PJ."
],
"DOI_URL": null
},
"PUB00097533": {
"PMID": 21723917,
"ISBN": null,
"volume": "1810",
"issue": "9",
"year": 2011,
"title": "Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.",
"URL": null,
"raw_pages": "815-26",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim Biophys Acta",
"authors": [
"Castonguay AC",
"Olson LJ",
"Dahms NM."
],
"DOI_URL": null
},
"PUB00097534": {
"PMID": 25692846,
"ISBN": null,
"volume": "16",
"issue": "1",
"year": 2015,
"title": "Glucosidase II and MRH-domain containing proteins in the secretory pathway.",
"URL": null,
"raw_pages": "31-48",
"medline_journal": "Curr Protein Pept Sci",
"ISO_journal": "Curr Protein Pept Sci",
"authors": [
"D'Alessio C",
"Dahms NM."
],
"DOI_URL": null
},
"PUB00097535": {
"PMID": 26062005,
"ISBN": null,
"volume": "54",
"issue": "26",
"year": 2015,
"title": "Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.",
"URL": null,
"raw_pages": "4097-111",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Olson LJ",
"Orsi R",
"Peterson FC",
"Parodi AJ",
"Kim JJ",
"D'Alessio C",
"Dahms NM."
],
"DOI_URL": null
},
"PUB00097536": {
"PMID": 23609449,
"ISBN": null,
"volume": "288",
"issue": "23",
"year": 2013,
"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.",
"URL": null,
"raw_pages": "16460-16475",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Olson LJ",
"Orsi R",
"Alculumbre SG",
"Peterson FC",
"Stigliano ID",
"Parodi AJ",
"D'Alessio C",
"Dahms NM."
],
"DOI_URL": null
},
"PUB00097537": {
"PMID": 16168372,
"ISBN": null,
"volume": "19",
"issue": "6",
"year": 2005,
"title": "Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.",
"URL": null,
"raw_pages": "765-75",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol Cell",
"authors": [
"Szathmary R",
"Bielmann R",
"Nita-Lazar M",
"Burda P",
"Jakob CA."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR009011",
"name": "Mannose-6-phosphate receptor binding domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 47481,
"pathways": 52,
"proteins": 23582,
"proteomes": 3310,
"sets": 0,
"structural_models": {
"alphafold": 19825,
"bfvd": 0
},
"structures": 66,
"taxa": 9455
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4xqm",
"name": "Crystal structure of the MRH domain of Glucosidase II beta bound to mannose"
}
}
}
