id: Pfam:PF01062
pfam_id: PF01062
name: Bestrophin, RFP-TM, chloride channel
short_name: Bestrophin
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01062
counters:
  proteins: 8246
  matches: 8846
  proteomes: 1318
  taxa: 4218
  structures: 45
  alphafold_models: 7437
  domain_architectures: 106
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:IPR021134
description: This entry represents animal bestrophin homologues. Bestrophin is a 68-kDa basolateral plasma
  membrane protein expressed in retinal pigment epithelial cells (RPE). It is encoded by the VMD2 gene,
  which is mutated in Best macular dystrophy, a disease characterised by a depressed light peak in the
  electrooculogram [[cite:PUB00011865]]. VMD2 encodes a 585-amino acid protein with an approximate mass
  of 68 kDa which has been designated bestrophin. Bestrophin shares homology with the Caenorhabditis elegans
  RFP gene family, named for the presence of a conserved arginine (R), phenylalanine (F), proline (P),
  amino acid sequence motif. Bestrophin is a plasma membrane protein, localised to the basolateral surface
  of RPE cells consistent with a role for bestrophin in the generation or regulation of the EOG light
  peak. Bestrophin and other RFP family members represent a new class of chloride channels, indicating
  a direct role for bestrophin in generating the light peak [[cite:PUB00011865]]. The VMD2 gene underlying
  Best disease was shown to represent the first human member of the RFP-TM protein family. More than 97%
  of the disease-causing mutations are located in the N-terminal RFP-TM domain implying important functional
  properties [[cite:PUB00011864]]. The bestrophins are four-pass transmembrane chloride-channel proteins
  [[cite:PUB00096747]], and the RFP-TM or bestrophin domain extends from the N-terminus through approximately
  350 amino acids and contains all of the TM domains as well as nearly all reported disease causing mutations
  [[cite:PUB00109156]]. Interestingly, the RFP motif is not conserved evolutionarily back beyond Metazoa,
  neither is it in plant members.