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{
"metadata": {
"accession": "cd14807",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "cdd",
"member_databases": null,
"integrated": "IPR038001",
"hierarchy": null,
"name": {
"name": "Domain 2 of receptor-associated protein (RAP)",
"short": "RAP_D2"
},
"description": [
{
"text": "<p>This subfamily is the N-terminal domain (D2) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease. [[cite:PUB00013423], [cite:PUB00131576], [cite:PUB00088026], [cite:PUB00048583], [cite:PUB00013422], [cite:PUB00012366], [cite:PUB00131330], [cite:PUB00131331], [cite:PUB00131332]]</p>",
"llm": false,
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}
],
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"literature": {
"PUB00131331": {
"PMID": 9792434,
"ISBN": null,
"volume": "379",
"issue": "8-9",
"year": 1998,
"title": "Receptor-associated protein (RAP): a specialized chaperone for endocytic receptors.",
"URL": null,
"raw_pages": "1025-31",
"medline_journal": "Biol Chem",
"ISO_journal": "Biol Chem",
"authors": [
"Willnow TE."
],
"DOI_URL": null
},
"PUB00012366": {
"PMID": 9207124,
"ISBN": null,
"volume": "94",
"issue": "14",
"year": 1997,
"title": "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.",
"URL": null,
"raw_pages": "7521-5",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Nielsen PR",
"Ellgaard L",
"Etzerodt M",
"Thogersen HC",
"Poulsen FM."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.94.14.7521"
},
"PUB00013422": {
"PMID": 9119022,
"ISBN": null,
"volume": "244",
"issue": "2",
"year": 1997,
"title": "Dissection of the domain architecture of the alpha2macroglobulin-receptor-associated protein.",
"URL": null,
"raw_pages": "544-51",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Ellgaard L",
"Holtet TL",
"Nielsen PR",
"Etzerodt M",
"Gliemann J",
"Thogersen HC."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1997.00544.x"
},
"PUB00131332": {
"PMID": 16916634,
"ISBN": null,
"volume": "23",
"issue": "4",
"year": 2006,
"title": "The switch on the RAPper's necklace...",
"URL": null,
"raw_pages": "451-5",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol Cell",
"authors": [
"Herz J."
],
"DOI_URL": null
},
"PUB00131576": {
"PMID": 9873007,
"ISBN": null,
"volume": "274",
"issue": "2",
"year": 1999,
"title": "Domain organization of the 39-kDa receptor-associated protein.",
"URL": null,
"raw_pages": "717-27",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Medved LV",
"Migliorini M",
"Mikhailenko I",
"Barrientos LG",
"Llinas M",
"Strickland DK."
],
"DOI_URL": null
},
"PUB00131330": {
"PMID": 9714598,
"ISBN": null,
"volume": "8",
"issue": "7",
"year": 1998,
"title": "RAP, a novel type of ER chaperone.",
"URL": null,
"raw_pages": "272-6",
"medline_journal": "Trends Cell Biol",
"ISO_journal": "Trends Cell Biol",
"authors": [
"Bu G",
"Schwartz AL."
],
"DOI_URL": null
},
"PUB00013423": {
"PMID": 7691821,
"ISBN": null,
"volume": "268",
"issue": "29",
"year": 1993,
"title": "Identification of domains on the 39-kDa protein that inhibit the binding of ligands to the low density lipoprotein receptor-related protein.",
"URL": null,
"raw_pages": "22046-54",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Warshawsky I",
"Bu G",
"Schwartz AL."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/268/29/22046"
},
"PUB00048583": {
"PMID": 17656581,
"ISBN": null,
"volume": "16",
"issue": "8",
"year": 2007,
"title": "The structure of receptor-associated protein (RAP).",
"URL": null,
"raw_pages": "1628-40",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Lee D",
"Walsh JD",
"Migliorini M",
"Yu P",
"Cai T",
"Schwieters CD",
"Krueger S",
"Strickland DK",
"Wang YX."
],
"DOI_URL": "http://dx.doi.org/10.1110/ps.072865407"
},
"PUB00088026": {
"PMID": 19397492,
"ISBN": null,
"volume": "421",
"issue": "2",
"year": 2009,
"title": "Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP.",
"URL": null,
"raw_pages": "273-82",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Jensen JK",
"Dolmer K",
"Schar C",
"Gettins PG."
],
"DOI_URL": "https://doi.org/10.1042/BJ20090175"
}
},
"set_info": {
"accession": "cl05743",
"name": "RAP"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
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"matches": 977,
"pathways": 0,
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"sets": 1,
"structural_models": {
"alphafold": 926,
"bfvd": 0
},
"structures": 6,
"taxa": 2107
},
"entry_annotations": {},
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"is_llm": false,
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}
}
