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{
"metadata": {
"accession": "PF21002",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR048511",
"hierarchy": null,
"name": {
"name": "Transmembrane protein 106 N-terminal region",
"short": "TMEM106_N"
},
"description": [
{
"text": "<p>This family includes Transmembrane protein 106A/B/C, type II transmembrane proteins which have homology to the late embryogenesis abundant-2 (LEA-2) domain [[cite:PUB00100166]]. TMEM106A has been identified as a key factor to regulate macrophage activation and a tumour suppressor in gastric, renal cancer and non small-cell lung carcinoma (NSCLC) [[cite:PUB00100168],[cite:PUB00100167]]. TMEM106B localises to late endosomes and lysosomes, and it is involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6 [[cite:PUB00070924]]. Its overexpression is associated with familial frontotemporal lobar degeneration [[cite:PUB00100169]]. It has also been identified as a protein required for productive SARS-CoV-2 [[cite:PUB00100166]]. Structural analysis of LEA-2 domains revealed that they have a long, conserved lipid-binding groove, implying that TMEM106B and its homologues Vac7 and Tag1 from yeast, may all be lipid transfer proteins in the lumen of late endocytic organelles [[cite:PUB00100166]].</p>",
"llm": false,
"checked": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00100167": {
"PMID": 29131025,
"ISBN": null,
"volume": "42",
"issue": "5",
"year": 2017,
"title": "TMEM106a is a Novel Tumor Suppressor in Human Renal Cancer.",
"URL": null,
"raw_pages": "853-864",
"medline_journal": "Kidney Blood Press Res",
"ISO_journal": "Kidney Blood Press Res",
"authors": [
"Wu C",
"Xu J",
"Wang H",
"Zhang J",
"Zhong J",
"Zou X",
"Chen Y",
"Yang G",
"Zhong Y",
"Lai D",
"Li X",
"Tang A."
],
"DOI_URL": null
},
"PUB00100166": {
"PMID": 34347309,
"ISBN": null,
"volume": "90",
"issue": "1",
"year": 2022,
"title": "TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.",
"URL": null,
"raw_pages": "164-175",
"medline_journal": "Proteins",
"ISO_journal": "Proteins",
"authors": [
"Levine TP."
],
"DOI_URL": null
},
"PUB00070924": {
"PMID": 24357581,
"ISBN": null,
"volume": "33",
"issue": "5",
"year": 2014,
"title": "The FTLD risk factor TMEM106B and MAP6 control dendritic trafficking of lysosomes.",
"URL": null,
"raw_pages": "450-67",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Schwenk BM",
"Lang CM",
"Hogl S",
"Tahirovic S",
"Orozco D",
"Rentzsch K",
"Lichtenthaler SF",
"Hoogenraad CC",
"Capell A",
"Haass C",
"Edbauer D."
],
"DOI_URL": "http://dx.doi.org/10.1002/embj.201385857"
},
"PUB00100168": {
"PMID": 30456879,
"ISBN": null,
"volume": null,
"issue": null,
"year": 2018,
"title": "TMEM106A inhibits cell proliferation, migration, and induces apoptosis of lung cancer cells.",
"URL": null,
"raw_pages": null,
"medline_journal": "J Cell Biochem",
"ISO_journal": "J Cell Biochem",
"authors": [
"Liu J",
"Zhu H."
],
"DOI_URL": null
},
"PUB00100169": {
"PMID": 23136129,
"ISBN": null,
"volume": "22",
"issue": "4",
"year": 2013,
"title": "The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function.",
"URL": null,
"raw_pages": "685-95",
"medline_journal": "Hum Mol Genet",
"ISO_journal": "Hum Mol Genet",
"authors": [
"Brady OA",
"Zheng Y",
"Murphy K",
"Huang M",
"Hu F."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 33,
"interactions": 0,
"matches": 3111,
"pathways": 0,
"proteins": 3105,
"proteomes": 905,
"sets": 0,
"structural_models": {
"alphafold": 2906,
"bfvd": 0
},
"structures": 16,
"taxa": 2884
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 12,
"alignment:full": 2380
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
