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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR012722",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016887",
"name": "ATP hydrolysis activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0051082",
"name": "unfolded protein binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006457",
"name": "protein folding",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd03342": "TCP1_zeta"
},
"ncbifam": {
"TIGR02347": "T-complex protein 1 subunit zeta"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR002423",
"name": "Chaperonin Cpn60/GroEL/TCP-1 family",
"type": "Family",
"children": [
{
"accession": "IPR001844",
"name": "Chaperonin Cpn60/GroEL",
"type": "Family",
"children": []
},
{
"accession": "IPR017998",
"name": "T-complex protein 1",
"type": "Family",
"children": [
{
"accession": "IPR012714",
"name": "Chaperonin/Thermosome",
"type": "Family",
"children": []
},
{
"accession": "IPR012715",
"name": "T-complex protein 1, alpha subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012716",
"name": "T-complex protein 1, beta subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012717",
"name": "T-complex protein 1, delta subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012718",
"name": "T-complex protein 1, epsilon subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012719",
"name": "T-complex protein 1, gamma subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012720",
"name": "T-complex protein 1, eta subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012721",
"name": "T-complex protein 1, theta subunit",
"type": "Family",
"children": []
},
{
"accession": "IPR012722",
"name": "T-complex protein 1, zeta subunit",
"type": "Family",
"children": []
}
]
},
{
"accession": "IPR028790",
"name": "Molecular chaperone MKKS",
"type": "Family",
"children": []
},
{
"accession": "IPR042984",
"name": "Chaperonin-containing T-complex member BBS12",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "T-complex protein 1, zeta subunit",
"short": "Chap_CCT_zeta"
},
"description": [
{
"text": "<p>Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [[cite:PUB00004127], [cite:PUB00001019]]. Chaperonins are involved in productive folding of proteins [[cite:PUB00080867]]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome [[cite:PUB00080871]]. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [[cite:PUB00004124]], related to the cpn60/groEL chaperonin family (see [interpro:IPR001844]).</p>\r\n\r\n<p>The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place [[cite:PUB00074264]]. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle [[cite:PUB00004129]] with 6 to 8 other different, but homologous, subunits [[cite:PUB00064264]]. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [[cite:PUB00001034], [cite:PUB00005432]]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [[cite:PUB00080868], [cite:PUB00080869], [cite:PUB00080873]]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [[cite:PUB00074265], [cite:PUB00074266]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00080867": {
"PMID": 11340060,
"ISBN": null,
"volume": "30",
"issue": null,
"year": 2001,
"title": "Chaperonin-mediated protein folding.",
"URL": null,
"raw_pages": "245-69",
"medline_journal": "Annu Rev Biophys Biomol Struct",
"ISO_journal": "Annu Rev Biophys Biomol Struct",
"authors": [
"Thirumalai D",
"Lorimer GH."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.biophys.30.1.245"
},
"PUB00080868": {
"PMID": 10753735,
"ISBN": null,
"volume": "10",
"issue": "7",
"year": 2000,
"title": "Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.",
"URL": null,
"raw_pages": "R260-4",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Leroux MR",
"Hartl FU."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-9822(00)00432-2"
},
"PUB00005432": {
"PMID": 7846767,
"ISBN": null,
"volume": "19",
"issue": "12",
"year": 1994,
"title": "Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.",
"URL": null,
"raw_pages": "543-8",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Kim S",
"Willison KR",
"Horwich AL."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(94)90058-2"
},
"PUB00004129": {
"PMID": 1630492,
"ISBN": null,
"volume": "358",
"issue": "6383",
"year": 1992,
"title": "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.",
"URL": null,
"raw_pages": "249-52",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Lewis VA",
"Hynes GM",
"Zheng D",
"Saibil H",
"Willison K."
],
"DOI_URL": "http://dx.doi.org/10.1038/358249a0"
},
"PUB00001019": {
"PMID": 15335898,
"ISBN": null,
"volume": "2",
"issue": "9",
"year": 1992,
"title": "TCP1 - molecular chaperonin of the cytoplasm?",
"URL": null,
"raw_pages": "487-9",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Nelson RJ",
"Craig EA."
],
"DOI_URL": "http://dx.doi.org/10.1016/0960-9822(92)90673-X"
},
"PUB00064264": {
"PMID": 7601114,
"ISBN": null,
"volume": "230",
"issue": "1",
"year": 1995,
"title": "The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.",
"URL": null,
"raw_pages": "3-16",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Kubota H",
"Hynes G",
"Willison K."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1995.tb20527.x"
},
"PUB00080869": {
"PMID": 10550210,
"ISBN": null,
"volume": "293",
"issue": "2",
"year": 1999,
"title": "Group II chaperonins: new TRiC(k)s and turns of a protein folding machine.",
"URL": null,
"raw_pages": "295-312",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Gutsche I",
"Essen LO",
"Baumeister W."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1999.3008"
},
"PUB00080873": {
"PMID": 12354605,
"ISBN": null,
"volume": "529",
"issue": "1",
"year": 2002,
"title": "Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.",
"URL": null,
"raw_pages": "11-6",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Valpuesta JM",
"Martin-Benito J",
"Gomez-Puertas P",
"Carrascosa JL",
"Willison KR."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(02)03180-0"
},
"PUB00074264": {
"PMID": 20194787,
"ISBN": null,
"volume": "107",
"issue": "11",
"year": 2010,
"title": "4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.",
"URL": null,
"raw_pages": "4967-72",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Cong Y",
"Baker ML",
"Jakana J",
"Woolford D",
"Miller EJ",
"Reissmann S",
"Kumar RN",
"Redding-Johanson AM",
"Batth TS",
"Mukhopadhyay A",
"Ludtke SJ",
"Frydman J",
"Chiu W."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.0913774107"
},
"PUB00074265": {
"PMID": 18595008,
"ISBN": null,
"volume": "14",
"issue": "1",
"year": 2009,
"title": "Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.",
"URL": null,
"raw_pages": "23-31",
"medline_journal": "Cell Stress Chaperones",
"ISO_journal": "Cell Stress Chaperones",
"authors": [
"Brackley KI",
"Grantham J."
],
"DOI_URL": "http://dx.doi.org/10.1007/s12192-008-0057-x"
},
"PUB00074266": {
"PMID": 15027029,
"ISBN": null,
"volume": "17",
"issue": "2",
"year": 2004,
"title": "The substrate recognition mechanisms in chaperonins.",
"URL": null,
"raw_pages": "85-94",
"medline_journal": "J Mol Recognit",
"ISO_journal": "J. Mol. Recognit.",
"authors": [
"Gomez-Puertas P",
"Martin-Benito J",
"Carrascosa JL",
"Willison KR",
"Valpuesta JM."
],
"DOI_URL": "http://dx.doi.org/10.1002/jmr.654"
},
"PUB00080871": {
"PMID": 11580264,
"ISBN": null,
"volume": "135",
"issue": "2",
"year": 2001,
"title": "Review: nucleotide binding to the thermoplasma thermosome: implications for the functional cycle of group II chaperonins.",
"URL": null,
"raw_pages": "147-56",
"medline_journal": "J Struct Biol",
"ISO_journal": "J. Struct. Biol.",
"authors": [
"Steinbacher S",
"Ditzel L."
],
"DOI_URL": "http://dx.doi.org/10.1006/jsbi.2001.4382"
},
"PUB00004127": {
"PMID": 1352857,
"ISBN": null,
"volume": "358",
"issue": "6383",
"year": 1992,
"title": "Protein folding. Cytosolic chaperonin confirmed.",
"URL": null,
"raw_pages": "191",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Ellis J."
],
"DOI_URL": "http://dx.doi.org/10.1038/358191a0"
},
"PUB00004124": {
"PMID": 1352040,
"ISBN": null,
"volume": "357",
"issue": "6380",
"year": 1992,
"title": "What is a chaperonin?",
"URL": null,
"raw_pages": "650",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Hemmingsen SM."
],
"DOI_URL": "http://dx.doi.org/10.1038/357650b0"
},
"PUB00001034": {
"PMID": 7953530,
"ISBN": null,
"volume": "4",
"issue": "2",
"year": 1994,
"title": "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.",
"URL": null,
"raw_pages": "89-99",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Kubota H",
"Hynes G",
"Carne A",
"Ashworth A",
"Willison K."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-9822(94)00024-2"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR027413",
"name": "GroEL-like equatorial domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR027410",
"name": "TCP-1-like chaperonin intermediate domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 5108,
"pathways": 34,
"proteins": 5108,
"proteomes": 3165,
"sets": 0,
"structural_models": {
"alphafold": 4566,
"bfvd": 0
},
"structures": 73,
"taxa": 9031
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.6.1.-",
"url": "https://enzyme.expasy.org/EC/3.6.1.-"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
