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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR007330",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF04212": "MIT (microtubule interacting and transport) domain"
},
"smart": {
"SM00745": "Microtubule Interacting and Trafficking molecule domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR007330",
"name": "MIT domain",
"type": "Domain",
"children": [
{
"accession": "IPR045253",
"name": "Vacuolar protein sorting-associated protein 4, MIT domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR045331",
"name": "MITD1, N-terminal domain",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "MIT domain",
"short": "MIT_dom"
},
"description": [
{
"text": "<p>The MIT domain forms an asymmetric three-helix bundle. It is found in vacuolar sorting proteins, spastin (probable ATPase involved in the assembly or function of nuclear protein complexes), and a sorting nexin, which may play a role in intracellular trafficking.</p>\n\n<p>A 'variant' MIT domain has been described at the N-terminal region of a related AAA-ATPase, mammalian katanin p60 represented in [interpro:IPR048611] [[cite:PUB00069769]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00069769": {
"PMID": 20339000,
"ISBN": null,
"volume": "285",
"issue": "22",
"year": 2010,
"title": "A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization.",
"URL": null,
"raw_pages": "16822-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Iwaya N",
"Kuwahara Y",
"Fujiwara Y",
"Goda N",
"Tenno T",
"Akiyama K",
"Mase S",
"Tochio H",
"Ikegami T",
"Shirakawa M",
"Hiroaki H."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M110.108365"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036181",
"name": "MIT domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 323,
"interactions": 0,
"matches": 24140,
"pathways": 26,
"proteins": 21472,
"proteomes": 3395,
"sets": 0,
"structural_models": {
"alphafold": 19041,
"bfvd": 0
},
"structures": 36,
"taxa": 9709
},
"entry_annotations": {
"alignment:seed": 126,
"alignment:full": 13055
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5fvk",
"name": "Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution."
}
}
}