id: Pfam:PF12053
pfam_id: PF12053
name: N-terminal of Par3 and HAL proteins
short_name: Par3_HAL_N_term
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12053
counters:
  proteins: 5578
  matches: 5617
  proteomes: 1060
  taxa: 3712
  structures: 3
  alphafold_models: 2696
  domain_architectures: 54
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:IPR021922
description: This domain is about 150 amino acids in length found associated with [pfam:PF00595] in eukaryotes.
  It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity
  establishment and maintenance such as Par3 (partitioning defective) [swissprot:Q8TEW0] and involved
  in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine
  ammonia lyase (HAL) [swissprot:P42357]. This N-terminal domain is found to mediate oligomerization critical
  for the membrane localization of Par-3. It is also found to possess a self-association capacity via
  a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles
  into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament
  but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due
  to the absence of equivalent charged residues that are essential for the longitudinal packing of the
  Par-3 N-terminal domain filament [[cite:PUB00085056]].