id: Pfam:PF07092
pfam_id: PF07092
name: TM106 protein C-terminal domain
short_name: TMEM106
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF07092
counters:
  proteins: 2857
  matches: 2902
  proteomes: 908
  taxa: 2827
  structures: 28
  alphafold_models: 2587
  domain_architectures: 28
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:IPR048509
description: This family includes Transmembrane protein 106A/B/C, type II transmembrane proteins which
  have homology to the late embryogenesis abundant-2 (LEA-2) domain [[cite:PUB00100166]]. TMEM106A has
  been identified as a key factor to regulate macrophage activation and a tumour suppressor in gastric,
  renal cancer and non small-cell lung carcinoma (NSCLC) [[cite:PUB00100168],[cite:PUB00100167]]. TMEM106B
  localises to late endosomes and lysosomes, and it is involved in dendrite morphogenesis and maintenance
  by regulating lysosomal trafficking via its interaction with MAP6 [[cite:PUB00070924]]. Its overexpression
  is associated with familial frontotemporal lobar degeneration [[cite:PUB00100169]]. It has also been
  identified as a protein required for productive SARS-CoV-2 [[cite:PUB00100166]]. Structural analysis
  of LEA-2 domains revealed that they have a long, conserved lipid-binding groove, implying that TMEM106B
  and its homologues Vac7 and Tag1 from yeast, may all be lipid transfer proteins in the lumen of late
  endocytic organelles [[cite:PUB00100166]].