id: Pfam:PF12063
pfam_id: PF12063
name: Atg1-like, MIT domain 1
short_name: ATG1-like_MIT1
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12063
counters:
  proteins: 4128
  matches: 4135
  proteomes: 2270
  taxa: 5730
  structures: 4
  alphafold_models: 3568
  domain_architectures: 55
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR022708
description: 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).