module: dmel_prefoldin
title: Prefoldin complex in Drosophila melanogaster
label: Prefoldin
module_type: PROTEIN_COMPLEX
description: >-
  Prefoldin is a heterohexameric co-chaperone shaped like a jellyfish, with
  six coiled-coil tentacles that bind nascent or unfolded polypeptides,
  notably actin and tubulin, and pass them to the CCT chaperonin. It is built
  from two alpha-class subunits (Pfdn3, encoded by mgr, and Pfdn5) and four
  beta-class subunits (Pfdn1, Pfdn2, Pfdn4 and Pfdn6). In Drosophila, mgr is
  needed for normal tubulin levels and spindle formation.
summary: >-
  Heterohexameric co-chaperone of two alpha and four beta subunits that
  delivers unfolded actin and tubulin to CCT.
concepts:
  - {id: GO:0016272, label: prefoldin complex}
complex: false
parts:
  - id: alpha_subunits
    label: Alpha-class prefoldin subunits
    role: alpha subunits
    genes: [mgr, Pfdn5]
  - id: beta_subunits
    label: Beta-class prefoldin subunits
    role: beta subunits
    genes: [Pfdn1, Pfdn2, Pfdn4, Pfdn6]
notes: >-
  The alpha/beta class split follows the conserved prefoldin architecture.
  The former GO term for unfolded protein binding is obsolete; the
  ATP-independent protein folding chaperone term (GO:0044183), which Pfdn1
  carries in GOA by IBA, is recorded on a complex-level annoton with all six
  subunits as active units, matching the placement in
  modules/cct_chaperonin_folding.yaml.
complex_term: {id: GO:0016272, label: prefoldin complex}
complex_function:
  function: {id: GO:0044183, label: protein folding chaperone}
  role_description: >-
    Captures non-native actin and tubulin chains without ATP and transfers
    them to the CCT chaperonin.