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74  structures 1187  species 0  interactions 12916  sequences 201  architectures

Family: FCH (PF00611)

Summary: Fes/CIP4, and EFC/F-BAR homology domain

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Fes/CIP4, and EFC/F-BAR homology domain Provide feedback

Alignment extended from [1]. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins [2]. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerises into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localise to actin-rich structures [3].

Literature references

  1. Aspenstrom P , Curr Biol 1997;7:479-487.: A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. PUBMED:9210375 EPMC:9210375

  2. Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B;, EMBO J. 2009;28:3103-3116.: Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. PUBMED:19713939 EPMC:19713939

  3. Itoh T, De Camilli P;, Biochim Biophys Acta. 2006;1761:897-912.: BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. PUBMED:16938488 EPMC:16938488

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001060

FCH domain is a short conserved region of around 60 amino acids first described as a region of homology between FER and CIP4 proteins [ PUBMED:9210375 ]. In the CIP4 protein the FCH domain binds to microtubules [ PUBMED:10713100 ]. The FCH domain is always found N-terminally and is followed by a coiled-coil region. The FCH and coiled-coil domains are structurally similar to Bin/amphiphysin/RVS (BAR) domains [ PUBMED:18525024 ]. They are alpha-helical membrane-binding modules that function in endocytosis, regulation of the actin cytoskeleton and signalling [ PUBMED:18525024 ].

Proteins containing an FCH domain can be divided in 3 classes [ PUBMED:11994747 ]:

  1. A subfamily of protein kinases usually associated with an SH2 domain:
    • Fps/fes (Fujimani poultry sarcoma/feline sarcoma) proto-oncogenes. They are non-receptor protein-tyrosine kinases preferentially expressed in myeloid lineage. The viral oncogene has an unregulated kinase activity which abrogates the need for cytokines and influences differentiation of haematopoietic progenitor cells.
    • Fes related protein (fer). It is an ubiquitously expressed homologue of Fes.
  2. Adaptor proteins usually associated with a C-terminal SH3 domain:
    • Schizosaccharomyces pombe CDC15 protein. It mediates cytoskeletal rearrangements required for cytokinesis. It is essential for viability.
    • CD2 cytoplasmic domain binding protein.
    • Mammalian Cdc42-interacting protein 4 (CIP4). It may act as a link between Cdc42 signaling and regulation of the actin cytoskeleton.
    • Mammalian PACSIN proteins. A family of cytoplasmic phosphoproteins playing a role in vesicle formation and transport.
  3. A subfamily of Rho-GAP proteins:
    • Mammalian RhoGAP4 proteins. They may down-regulate Rho-like GTPases in hematopoietic cells.
    • Yeast hypothetical protein YBR260C.
    • Caenorhabditis elegans hypothetical protein ZK669.1.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Golgi-transport (CL0145), which has the following description:

This clan contains families that are involved in intracellular transport and signalling. Arfaptins are proteins which interact with small GTPases involved in vesicular budding at the Golgi complex. They form an elongated dimer of three helix coiled coils and are structurally very similar to the BAR domain [1][2]. The Sec34 family is involved in tethering vesicles to the Golgi [3].

The clan contains the following 9 members:

Arfaptin BAR BAR_2 BAR_3 BAR_3_WASP_bdg FAM92 FCH IMD Vps5


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: SMART
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Ponting CP , Schultz J, Bork P
Number in seed: 528
Number in full: 12916
Average length of the domain: 79.10 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 11.06 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.8 27.8
Trusted cut-off 27.8 27.8
Noise cut-off 27.7 27.7
Model length: 78
Family (HMM) version: 25
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FCH domain has been found. There are 74 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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