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Bin/amphiphysin/Rvs domain
Bin/amphiphysin/Rvs domain
Identifiers
Symbol	BAR-2
Pfam	PF10455
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

BAR domain
BAR domain
	Structure of amphiphysin BAR.
Identifiers
Symbol	BAR
Pfam	PF03114
InterPro	IPR004148
SMART	SM00721
PROSITE	PDOC51021
SCOP2	1uru / SCOPe / SUPFAM
CDD	cd07307
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

BAR domain of APPL family

Identifiers

Symbol

BAR-3

Pfam

PF16746

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

EFC/F-BAR homology domain

Identifiers

Symbol

FCH

Pfam

PF00611

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Vps5 C terminal like (BAR domain)

Identifiers

Symbol

Vps5

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

WASP-binding domain of sorting nexin proteins

Identifiers

Symbol

BAR-3-WASP

Pfam

PF10456

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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]

Human proteins containing this domain

AMPH; ARHGAP17; ARHGAP44; BIN1; BIN2; BIN3; SH3BP1; SH3GL1; SH3GL2; SH3GL3; SH3GLB1; SH3GLB2.^[2]

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.^[3] 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.^[4]