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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR002067",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0055085",
"name": "transmembrane transport",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"prints": {
"PR00784": "MTUNCOUPLING",
"PR00926": "MITOCARRIER"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR002067",
"name": "Mitochondrial carrier protein",
"type": "Family",
"children": [
{
"accession": "IPR002113",
"name": "ADP/ATP carrier protein, eukaryotic type",
"type": "Family",
"children": []
},
{
"accession": "IPR002167",
"name": "Solute carrier family 25 member 16-like",
"type": "Family",
"children": []
},
{
"accession": "IPR045315",
"name": "Mitochondrial carrier protein Mtm1-like",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Mitochondrial carrier protein",
"short": "MCP"
},
"description": [
{
"text": "<p>This family includes mitochondrial carrier proteins that transport a broad variety of substrates and, therefore, they are involved in different metabolic pathways such as the TCA cycle, lipid metabolism, nucleotides metabolism [[cite:PUB00152845], [cite:PUB00152848], [cite:PUB00152846], [cite:PUB00152847]] and energy transfer [[cite:PUB00005351], [cite:PUB00001005], [cite:PUB00005084], [cite:PUB00003301], [cite:PUB00097195]]. Some examples of this group are the uncoupling proteins (UCPs). This family also includes peroxisomal proteins like PMP34 [[cite:PUB00057422]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Mitochondrial brown fat uncoupling protein 1 from chordates (UCP1) is responsible for thermogenic respiration, a specialised capacity of brown adipose tissue to the regulation of energy balance. It regulates the production of reactive oxygen species/ROS by mitochondria [[cite:PUB00101071], [cite:PUB00101070]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>A variety of substrate carrier proteins involved in energy transfer are found in the inner mitochondrial membrane or are integral to the membranes of other eukaryotic organelles such as the peroxisome [[cite:PUB00005351], [cite:PUB00005084], [cite:PUB00003301], [cite:PUB00001675], [cite:PUB00005407]]. Such proteins include:</p>\n\n<ul><li>ADP/ATP carrier protein (ADP/ATP translocase)</li>\n <li>2-oxoglutarate/malate carrier protein</li>\n <li>Phosphate carrier protein</li>\n <li>Tricarboxylate transport protein (or citrate transport protein)</li>\n <li>Graves disease carrier protein</li>\n <li>Yeast mitochondrial proteins MRS3 and MRS4</li>\n <li>Yeast mitochondrial FAD carrier protein</li>\n <li>And many others</li></ul>\n\n<p>These mitochondrial carrier proteins share a tripartite structure, consisting of up to three tandem repeats of a domain approximately 100 residues in length [[cite:PUB00001005]]. Each domain contains two transmembrane (TM) regions, resulting in a total of six TM domains. Sequence analysis has shown that the TM regions and their adjacent hydrophilic loops are more highly conserved than other parts of the protein, with five of the six TM domains followed by the conserved motif (D/E)-Hy(K/R), where Hy denotes a hydrophobic residue [[cite:PUB00001005]]. Structurally, these domains contain six α-helices that form a compact transmembrane unit. This structure exhibits a deep depression on the side facing the space between the inner and outer mitochondrial membranes, resembling a channel-like conformation [[cite:PUB00101069], [cite:PUB00029479]]. It is suggested that substrates bind at the bottom of this cavity, and translocation occurs through a conformational change from a 'pit' to a 'channel' structure.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00152847": {
"PMID": 35288533,
"ISBN": null,
"volume": "13",
"issue": "3",
"year": 2022,
"title": "An integrated bioinformatic investigation of mitochondrial solute carrier family 25 (SLC25) in colon cancer followed by preliminary validation of member 5 (SLC25A5) in tumorigenesis.",
"URL": null,
"raw_pages": "237",
"medline_journal": "Cell Death Dis",
"ISO_journal": "Cell Death Dis",
"authors": [
"Chen YJ",
"Hong WF",
"Liu ML",
"Guo X",
"Yu YY",
"Cui YH",
"Liu TS",
"Liang L."
],
"DOI_URL": "https://doi.org/10.1038/s41419-022-04692-1"
},
"PUB00152845": {
"PMID": 19429682,
"ISBN": null,
"volume": "284",
"issue": "27",
"year": 2009,
"title": "A novel member of solute carrier family 25 (SLC25A42) is a transporter of coenzyme A and adenosine 3',5'-diphosphate in human mitochondria.",
"URL": null,
"raw_pages": "18152-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Fiermonte G",
"Paradies E",
"Todisco S",
"Marobbio CM",
"Palmieri F."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M109.014118"
},
"PUB00101070": {
"PMID": 9139827,
"ISBN": null,
"volume": "387",
"issue": "6628",
"year": 1997,
"title": "Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese.",
"URL": null,
"raw_pages": "90-4",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Enerback S",
"Jacobsson A",
"Simpson EM",
"Guerra C",
"Yamashita H",
"Harper ME",
"Kozak LP."
],
"DOI_URL": null
},
"PUB00152846": {
"PMID": 31356773,
"ISBN": null,
"volume": "1860",
"issue": "9",
"year": 2019,
"title": "The human uncoupling proteins 5 and 6 (UCP5/SLC25A14 and UCP6/SLC25A30) transport sulfur oxyanions, phosphate and dicarboxylates.",
"URL": null,
"raw_pages": "724-733",
"medline_journal": "Biochim Biophys Acta Bioenerg",
"ISO_journal": "Biochim Biophys Acta Bioenerg",
"authors": [
"Gorgoglione R",
"Porcelli V",
"Santoro A",
"Daddabbo L",
"Vozza A",
"Monne M",
"Di Noia MA",
"Palmieri L",
"Fiermonte G",
"Palmieri F."
],
"DOI_URL": "https://doi.org/10.1016/j.bbabio.2019.07.010"
},
"PUB00152848": {
"PMID": 35727412,
"ISBN": null,
"volume": "79",
"issue": "7",
"year": 2022,
"title": "Mitochondrial FAD shortage in SLC25A32 deficiency affects folate-mediated one-carbon metabolism.",
"URL": null,
"raw_pages": "375",
"medline_journal": "Cell Mol Life Sci",
"ISO_journal": "Cell Mol Life Sci",
"authors": [
"Peng MZ",
"Shao YX",
"Li XZ",
"Zhang KD",
"Cai YN",
"Lin YT",
"Jiang MY",
"Liu ZC",
"Su XY",
"Zhang W",
"Jiang XL",
"Liu L."
],
"DOI_URL": "https://doi.org/10.1007/s00018-022-04404-0"
},
"PUB00101071": {
"PMID": 20416274,
"ISBN": null,
"volume": "1797",
"issue": "8",
"year": 2010,
"title": "The role of UCP 1 in production of reactive oxygen species by mitochondria isolated from brown adipose tissue.",
"URL": null,
"raw_pages": "1470-6",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim Biophys Acta",
"authors": [
"Dlaskova A",
"Clarke KJ",
"Porter RK."
],
"DOI_URL": null
},
"PUB00005351": {
"PMID": 2158156,
"ISBN": null,
"volume": "15",
"issue": "3",
"year": 1990,
"title": "Mechanism and evolution of the uncoupling protein of brown adipose tissue.",
"URL": null,
"raw_pages": "108-12",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Klingenberg M."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(90)90194-G"
},
"PUB00001005": {
"PMID": 8325039,
"ISBN": null,
"volume": "28",
"issue": "3",
"year": 1993,
"title": "The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.",
"URL": null,
"raw_pages": "209-33",
"medline_journal": "Crit Rev Biochem Mol Biol",
"ISO_journal": "Crit. Rev. Biochem. Mol. Biol.",
"authors": [
"Kuan J",
"Saier MH Jr."
],
"DOI_URL": "http://intl.crbmb.com/cgi/content/abstract/28/3/209"
},
"PUB00005084": {
"PMID": 8140286,
"ISBN": null,
"volume": "144",
"issue": "8",
"year": 1993,
"title": "Expansion of the mitochondrial carrier family.",
"URL": null,
"raw_pages": "671-2",
"medline_journal": "Res Microbiol",
"ISO_journal": "Res. Microbiol.",
"authors": [
"Kuan J",
"Saier MH Jr."
],
"DOI_URL": "http://dx.doi.org/10.1016/0923-2508(93)90073-B"
},
"PUB00003301": {
"PMID": 8487299,
"ISBN": null,
"volume": "230",
"issue": "4",
"year": 1993,
"title": "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.",
"URL": null,
"raw_pages": "1159-70",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Nelson DR",
"Lawson JE",
"Klingenberg M",
"Douglas MG."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1993.1233"
},
"PUB00057422": {
"PMID": 11121399,
"ISBN": null,
"volume": "276",
"issue": "12",
"year": 2001,
"title": "Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments. study using human membrane protein PMP34.",
"URL": null,
"raw_pages": "9375-82",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Honsho M",
"Fujiki Y."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M003304200"
},
"PUB00097195": {
"PMID": 30611538,
"ISBN": null,
"volume": "176",
"issue": "3",
"year": 2019,
"title": "The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.",
"URL": null,
"raw_pages": "435-447.e15",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Ruprecht JJ",
"King MS",
"Zogg T",
"Aleksandrova AA",
"Pardon E",
"Crichton PG",
"Steyaert J",
"Kunji ERS."
],
"DOI_URL": null
},
"PUB00001675": {
"PMID": 8206158,
"ISBN": null,
"volume": "346",
"issue": "1",
"year": 1994,
"title": "Mitochondrial carrier proteins.",
"URL": null,
"raw_pages": "48-54",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Palmieri F."
],
"DOI_URL": "http://dx.doi.org/10.1016/0014-5793(94)00329-7"
},
"PUB00005407": {
"PMID": 8291088,
"ISBN": null,
"volume": "18",
"issue": "11",
"year": 1993,
"title": "PMP47, a peroxisomal homologue of mitochondrial solute carrier proteins.",
"URL": null,
"raw_pages": "427-8",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Jank B",
"Habermann B",
"Schweyen RJ",
"Link TA."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(93)90141-9"
},
"PUB00029479": {
"PMID": 14603310,
"ISBN": null,
"volume": "426",
"issue": "6962",
"year": 2003,
"title": "Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside.",
"URL": null,
"raw_pages": "39-44",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Pebay-Peyroula E",
"Dahout-Gonzalez C",
"Kahn R",
"Trezeguet V",
"Lauquin GJ",
"Brandolin G."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature02056"
},
"PUB00101069": {
"PMID": 21785437,
"ISBN": null,
"volume": "476",
"issue": "7358",
"year": 2011,
"title": "Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching.",
"URL": null,
"raw_pages": "109-13",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Berardi MJ",
"Shih WM",
"Harrison SC",
"Chou JJ."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR023395",
"name": "Mitochondrial carrier protein domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 513032,
"pathways": 109,
"proteins": 108052,
"proteomes": 3380,
"sets": 0,
"structural_models": {
"alphafold": 97321,
"bfvd": 2
},
"structures": 13,
"taxa": 12670
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
