id: Pfam:PF05093
pfam_id: PF05093
name: Cytokine-induced anti-apoptosis inhibitor 1, Fe-S biogenesis
short_name: CIAPIN1
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05093
counters:
  proteins: 4152
  matches: 4936
  proteomes: 3289
  taxa: 8763
  structures: 0
  alphafold_models: 3590
  domain_architectures: 90
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:IPR046408
description: Anamorsin, subsequently named CIAPIN1 for cytokine-induced anti-apoptosis inhibitor 1, in
  humans is the homologue of yeast Dre2, a conserved soluble eukaryotic Fe-S cluster protein, that functions
  in cytosolic Fe-S protein biogenesis. It is found in both the cytoplasm and in the mitochondrial intermembrane
  space (IMS) [[cite:PUB00055951]]. CIAPIN1 is found to be up-regulated in hepatocellular cancer, is considered
  to be a downstream effector of the receptor tyrosine kinase-Ras signalling pathway, and is essential
  in mouse definitive haematopoiesis [[cite:PUB00055952]]. Dre2 has been found to interact with the yeast
  reductase Tah18, forming a tight cytosolic complex implicated in the response to high levels of oxidative
  stress [[cite:PUB00109169]]. These proteins consist of two domains, the N-terminal well-folded one,
  with a S-adenosylmethionine methyltransferase-like fold and the C-terminal more flexible domain, represented
  in this entry, which contains two highly conserved cysteine rich motifs that bind Fe-S clusters [[cite:PUB00067100],[cite:PUB00056284]].