Summary: Bin/amphiphysin/Rvs domain for vesicular trafficking
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BAR domain Edit Wikipedia article
Structure of amphiphysin BAR.
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: 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.
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.
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. Examples of the F-BAR domain family are CIP4/FBP17/Toca-1 and Syndapins (also called PACSINs). 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.
Human proteins containing this domain
- 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.
- 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 . PMID 21878992.
- 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 . PMID 21926968.
- Leventis PA, Chow BM, Stewart BA, Iyengar B, Campos AR, Boulianne GL (November 2001). "Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis". Traffic. 2 (11): 839–50. doi:10.1034/j.1600-0854.2001.21113.x. PMID 11733051.
- Zhang B, Zelhof AC (July 2002). "Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp". Traffic. 3 (7): 452–60. doi:10.1034/j.1600-0854.2002.30702.x. PMID 12047553.Review.
- Zelhof AC, Bao H, Hardy RW, Razzaq A, Zhang B, Doe CQ (December 2001). "Drosophila Amphiphysin is implicated in protein localization and membrane morphogenesis but not in synaptic vesicle endocytosis". Development. 128 (24): 5005–15. PMID 11748137.
- Mathew D, Popescu A, Budnik V (November 2003). "Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling". J. Neurosci. 23 (33): 10710–6. PMID 14627656.
- 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.
- Weissenhorn W (August 2005). "Crystal structure of the endophilin-A1 BAR domain". J. Mol. Biol. 351 (3): 653–61. doi:10.1016/j.jmb.2005.06.013. PMID 16023669.
- Gallop JL, Jao CC, Kent HM, et al. (June 2006). "Mechanism of endophilin N-BAR domain-mediated membrane curvature". EMBO J. 25 (12): 2898–910. doi:10.1038/sj.emboj.7601174. PMC . PMID 16763559.
- Masuda M, Takeda S, Sone M, et al. (June 2006). "Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms". EMBO J. 25 (12): 2889–97. doi:10.1038/sj.emboj.7601176. PMC . PMID 16763557.
- Frost A, Perera R, Roux A, et al. (March 2008). "Structural basis of membrane invagination by F-BAR domains". Cell. 132 (5): 807–17. doi:10.1016/j.cell.2007.12.041. PMC . PMID 18329367.
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.
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
|SCOOP:||Arfaptin BAR BAR_3 IMD|
|Similarity to PfamA using HHSearch:||BAR|
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.
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.
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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 . The Sec34 family is involved in tethering vesicles to the Golgi .
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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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_12557 (release 22.0)|
|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 build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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