id: Pfam:PF10186
pfam_id: PF10186
name: Vacuolar sorting 38 and autophagy-related subunit 14
short_name: ATG14
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF10186
counters:
  proteins: 5914
  matches: 6025
  proteomes: 2963
  taxa: 7961
  structures: 15
  alphafold_models: 5015
  domain_architectures: 82
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:IPR018791
description: 'The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of
  40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective
  not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase,
  to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated
  with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form
  a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic
  process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required
  for the function of Apg6/Vps30p through the autophagic pathway [[cite:PUB00009843]]. There are 17 auto-phagosomal
  component proteins which are categorized into six functional units, one of which is the AS-PI3K complex
  (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation,
  and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P)
  at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled
  by Atg14 [[cite:PUB00055554]]. Autophagy mediates the cellular response to nutrient deprivation, protein
  aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple
  human diseases including cancer. This effect seems to be mediated through direct interaction of the
  human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [[cite:PUB00054155]].'