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{
"metadata": {
"accession": "IPR000096",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0005576",
"name": "extracellular region",
"category": {
"code": "C",
"name": "cellular_component"
}
}
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"PS00992": "Serum amyloid A proteins signature"
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"pirsf": {
"PIRSF002472": "Amyloid protein, SAA type"
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"SM00197": "Serum amyloid A proteins"
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"PF00277": "Serum amyloid A protein"
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"PR00306": "SERUMAMYLOID"
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"accession": "IPR000096",
"name": "Serum amyloid A protein",
"type": "Family",
"children": []
},
"name": {
"name": "Serum amyloid A protein",
"short": "Serum_amyloid_A"
},
"description": [
{
"text": "<p>The serum amyloid A (SAA) proteins comprise a family of vertebrate amphipathic α-helical apolipoproteins that associate predominantly with high density lipoproteins (HDL) [[cite:PUB00000177], [cite:PUB00001955]]. They play a role in the mobilisation of cholesterol for tissue repair and regeneration [[cite:PUB00095064]]. The synthesis of these proteins is greatly increased (as much as a 1000 fold) in inflammation, being a major acute phase reactant together with C-reactive protein. They act as cytokine-like proteins that are involved in cell-cell communication and in inflammatory, immunologic, neoplastic and protective pathways [[cite:PUB00095063]]. Prolonged elevation of plasma SAA levels, as in chronic inflammation, results in a pathological condition, called amyloidosis, which affects the liver, kidney and spleen and which is characterised by the highly insoluble accumulation of SAA in these tissues. During chronic inflammation, SAA association with HDL can change its protein and lipid composition which abrogates the HDL anti-atherogenic properties, contributing to a pro-atherogenic state [[cite:PUB00095064], [cite:PUB00095063]].</p>",
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"PUB00000177": {
"PMID": 7504491,
"ISBN": null,
"volume": "102",
"issue": "2",
"year": 1993,
"title": "Serum amyloid A (SAA): an acute phase protein and apolipoprotein.",
"URL": null,
"raw_pages": "131-46",
"medline_journal": "Atherosclerosis",
"ISO_journal": "Atherosclerosis",
"authors": [
"Malle E",
"Steinmetz A",
"Raynes JG."
],
"DOI_URL": "http://dx.doi.org/10.1016/0021-9150(93)90155-N"
},
"PUB00001955": {
"PMID": 8188253,
"ISBN": null,
"volume": "19",
"issue": "2",
"year": 1994,
"title": "Evolution of the serum amyloid A (SAA) protein superfamily.",
"URL": null,
"raw_pages": "228-35",
"medline_journal": "Genomics",
"ISO_journal": "Genomics",
"authors": [
"Uhlar CM",
"Burgess CJ",
"Sharp PM",
"Whitehead AS."
],
"DOI_URL": "http://dx.doi.org/10.1006/geno.1994.1052"
},
"PUB00095063": {
"PMID": 30165816,
"ISBN": null,
"volume": "24",
"issue": "1",
"year": 2018,
"title": "Serum amyloid A - a review.",
"URL": null,
"raw_pages": "46",
"medline_journal": "Mol Med",
"ISO_journal": "Mol. Med.",
"authors": [
"Sack GH Jr."
],
"DOI_URL": null
},
"PUB00095064": {
"PMID": 30852808,
"ISBN": null,
"volume": "188",
"issue": "4",
"year": 2019,
"title": "Serum amyloid A levels are associated with polymorphic variants in the serum amyloid A 1 and 2 genes.",
"URL": null,
"raw_pages": "1175-1183",
"medline_journal": "Ir J Med Sci",
"ISO_journal": "Ir J Med Sci",
"authors": [
"Griffiths K",
"Maxwell AP",
"McCarter RV",
"Nicol P",
"Hogg RE",
"Harbinson M",
"McKay GJ."
],
"DOI_URL": null
}
},
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"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00762",
"url": "http://prosite.expasy.org/PDOC00762"
}
]
}
},
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"representative_structure": {
"accession": "6pxz",
"name": "Crystal Structure of mouse Serum Amyloid A3 (SAA3) in the trimeric form"
}
}
}
