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0  structures 375  species 0  interactions 460  sequences 9  architectures

Family: BAR_2 (PF10455)

Summary: Bin/amphiphysin/Rvs domain for vesicular trafficking

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BAR domain Edit Wikipedia article

BAR domain
PDB 1uru EBI.jpg
Structure of amphiphysin BAR.[1]
Symbol BAR
Pfam PF03114
InterPro IPR004148
SCOP 1uru
CDD cd07307

In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs.

BAR domains occur in combinations with other domains

Many BAR family proteins contain alternative lipid specificity domains that help target these protein to particular membrane compartments. Some also have SH3 domains that bind to dynamin and thus proteins like amphiphysin and endophilin are implicated in the orchestration of vesicle scission.

N-BAR domain

Some BAR domain containing proteins have an N-terminal amphipathic helix preceding the BAR domain. This helix inserts (like in the epsin ENTH domain) into the membrane and induces curvature, which is stabilised by the BAR dimer. Amphiphysin, endophilin, BRAP1/bin2 and nadrin are examples of such proteins containing an N-BAR. The Drosophila amphiphysin N-BAR (DA-N-BAR) is an example of a protein with a preference for negatively charged surfaces.[1]

F-BAR (EFC) domain

F-BAR domains (for FCH-BAR, or EFC for Extended FCH Homology) are BAR domains that are extensions of the already established FCH domain. They are frequently found at the amino terminus of proteins. They can bind lipid membranes and can tubulate lipids in vitro and in vivo, but their exact physiological role still is under investigation.[2] Examples of the F-BAR domain family are CIP4/FBP17/Toca-1, Syndapins (also called PACSINs) and muniscins. Gene knock-out of syndapin I in mice revealed that this brain-enriched isoform of the syndapin family is crucial for proper size control of synaptic vesicles and thereby indeed helps to define membrane curvature a physiological process. Work of the lab of Britta Qualmann also demonstrated that syndapin I is crucial for proper targeting of the large GTPase dynamin to membranes.[3]

Sorting nexins

The sorting nexin family of proteins includes several members that possess a BAR domain, including the well characterized SNX1 and SNX9.

Human proteins containing this domain


See also

External links


  1. ^ a b Peter BJ, Kent HM, Mills IG, et al. (January 2004). "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science. 303 (5657): 495–9. doi:10.1126/science.1092586. PMID 14645856. 
  2. ^ Qualmann B, Koch D, Kessels MM (August 2011). "Let's go bananas: revisiting the endocytic BAR code". EMBO J. 30 (17): 3501–15. doi:10.1038/emboj.2011.266. PMC 3181480Freely accessible. PMID 21878992. 
  3. ^ Koch D, Spiwoks-Becker I, Sabanov V, Sinning A, Dugladze T, Stellmacher A, Ahuja R, Grimm J, Schüler S, Müller A, Angenstein F, Ahmed T, Diesler A, Moser M, Tom Dieck S, Spessert R, Boeckers TM, Fässler R, Hübner CA, Balschun D, Gloveli T, Kessels MM, Qualmann B (December 2011). "Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I". EMBO J. 30 (24): 4955–69. doi:10.1038/emboj.2011.339. PMC 3243622Freely accessible. PMID 21926968. 

Further reading

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Bin/amphiphysin/Rvs domain for vesicular trafficking Provide feedback

This Pfam entry includes proteins that are not matched by PF03114.

Literature references

  1. Querin L, Sanvito R, Magni F, Busti S, Van Dorsselaer A, Alberghina L, Vanoni M; , J Biol Chem. 2007; [Epub ahead of print]: Proteomic analysis of a nutritional Shift-up in S. cerevisiae identifies Gvp36 as a BAR-containing protein involved in vesicular traffic and nutritional adaptation. PUBMED:18156177 EPMC:18156177

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018859

Endocytosis and intracellular transport involve several mechanistic steps:

  • (1) for the internalisation of cargo molecules, the membrane needs to bend to form a vesicular structure, which requires membrane curvature and a rearrangement of the cytoskeleton;
  • (2) following its formation, the vesicle has to be pinched off the membrane;
  • (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.
Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis, involved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain, known as the BAR (Bin-Amphiphysin-Rvs)-domain, which is required for their in vivo function and their ability to tubulate membranes [PUBMED:14993925].

The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise, heterodimerise or, in a few cases, interact with small GTPases.

This entry identifies several fungal BAR domain-containing proteins, such as Gvp36, that are not detected by INTERPRO [PUBMED:18156177].

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


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Curation View help on the curation process

Seed source: Pfam-B_12557 (release 22.0)
Previous IDs: none
Type: Family
Author: Mistry J, Wood V
Number in seed: 10
Number in full: 460
Average length of the domain: 268.90 aa
Average identity of full alignment: 44 %
Average coverage of the sequence by the domain: 81.75 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.4 25.4
Trusted cut-off 25.4 25.4
Noise cut-off 25.3 25.3
Model length: 289
Family (HMM) version: 8
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Archea Archea Eukaryota Eukaryota
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Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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