C-CAP/cofactor C-like domain (IPR017901)

Short name: C-CAP_CF_C-like

Overlapping homologous superfamilies

Domain relationships


The C-CAP/cofactor C-like domain is present in several cytoskeleton-related proteins, which also contain a number of additional domains [PMID: 15311924, PMID: 16472755, PMID: 17645436, PMID: 14536023]:

  • Eukaryotic cyclase-associated protein (CAP or SRV2), a modular actin monomer binding that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localisation and the establishment of cell polarity.
  • Vertebrate retinitis pigmentosa 2 (XRP2). In Homo sapiens (Human), it is the protein responsible for X-linked forms of retinitis pigmentosa, a disease characterised by severe retinal degeneration.
  • Eukaryotic tubulin-specific chaperone cofactor C (TBCC), a GTPase- activating component of the tubulin-folding supercomplex, which directs the assembly of the alpha- and beta-tubulin heterodimer.

The cyclase-associated protein C-CAP/cofactor C-like domain binds G-actin and is responsible for oligomerisation of the entire CAP molecule [PMID: 15311924], whereas the XRP2 C-CAP/cofactor C-like domain is required for binding of ADP ribosylation factor-like protein 3 (Arl3) [PMID: 16472755].

The central core of the C-CAP/cofactor C-like domain is composed of six coils of right-handed parallel beta-helices, termed coils 1-6, which form an elliptical barrel with a tightly packed interior. Each beta-helical coil is composed of three relatively short beta-strands, designated a-c, separated by sharp turns. Flanking the central beta-helical core is an N-terminal beta-strand, beta0, that packs antiparallel to the core, and strand beta7 packs antiparallel to the core near the C-terminal end of the parallel beta-helix [PMID: 15311924, PMID: 16472755].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles