{"metadata":{"accession":"PF12063","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR022708","hierarchy":null,"name":{"name":"Atg1-like, MIT domain 1","short":"ATG1-like_MIT1"},"description":[{"text":"<p>Members of this entry are serine/threonine-protein kinases and includes ATG1 from yeasts, Unc-51 from C. elegans and ULK1-2 from humans. ATG1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway [[cite:PUB00101056],[cite:PUB00066530]]. Unc-51 is important for axonal elongation and axonal guidance [[cite:PUB00042769]] and ULK1-2 are involved in autophagy in response to starvation [[cite:PUB00098424]]. They consist of a kinase domain at the N-terminal ([pfam:PF00069]) and two tandem microtubule interacting and transport (MIT) domains (tMIT) at the C-terminal. MIT domains are known to mediate protein-protein interactions. In ATG1, MIT domains mediate the interaction with ATG13 [[cite:PUB00101056]]. In ULK1-2, MIT domains control the regulatory function and localization of the proteins and also mediate interactions with additional autophagy proteins [[cite:PUB00098424]]. This is the C-terminal MIT domain (MIT2).</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00101056":{"PMID":24793651,"ISBN":null,"volume":"21","issue":"6","year":2014,"title":"Structural basis of starvation-induced assembly of the autophagy initiation complex.","URL":null,"raw_pages":"513-21","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat Struct Mol Biol","authors":["Fujioka Y","Suzuki SW","Yamamoto H","Kondo-Kakuta C","Kimura Y","Hirano H","Akada R","Inagaki F","Ohsumi Y","Noda NN."],"DOI_URL":null},"PUB00042769":{"PMID":16887826,"ISBN":null,"volume":"133","issue":"17","year":2006,"title":"The autophagy-related kinase UNC-51 and its binding partner UNC-14 regulate the subcellular localization of the Netrin receptor UNC-5 in Caenorhabditis elegans.","URL":null,"raw_pages":"3441-50","medline_journal":"Development","ISO_journal":"Development","authors":["Ogura K","Goshima Y."],"DOI_URL":"http://dx.doi.org/10.1242/dev.02503"},"PUB00098424":{"PMID":18936157,"ISBN":null,"volume":"29","issue":"1","year":2009,"title":"Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism.","URL":null,"raw_pages":"157-71","medline_journal":"Mol Cell Biol","ISO_journal":"Mol Cell Biol","authors":["Chan EY","Longatti A","McKnight NC","Tooze SA."],"DOI_URL":null},"PUB00066530":{"PMID":17204848,"ISBN":null,"volume":"3","issue":"2","year":2007,"title":"ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes.","URL":null,"raw_pages":"106-16","medline_journal":"Autophagy","ISO_journal":"Autophagy","authors":["Meijer WH","van der Klei IJ","Veenhuis M","Kiel JA."],"DOI_URL":null}},"set_info":{"accession":"CL0745","name":"MIT"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":55,"interactions":0,"matches":4135,"pathways":0,"proteins":4128,"proteomes":2270,"sets":1,"structural_models":{"alphafold":3568},"structures":4,"taxa":5730},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":78,"alignment:full":3291},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}