The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380263   1 MAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLI 80
Cdd:cd07590   112 AAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALI 191

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720380263  81 RAQVIYYSEMHKIFGDLTQQLDQPGHSDEQRERE 114
Cdd:cd07590   192 KSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380263   1 MAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLI 80
Cdd:cd07590   112 AAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALI 191

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720380263  81 RAQVIYYSEMHKIFGDLTQQLDQPGHSDEQRERE 114
Cdd:cd07590   192 KSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380263  38 QAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQVIYYSEMHKIFGDLTQQLDQ 103
Cdd:pfam03114 170 QAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380263   1 MAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLI 80
Cdd:cd07590   112 AAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALI 191

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720380263  81 RAQVIYYSEMHKIFGDLTQQLDQPGHSDEQRERE 114
Cdd:cd07590   192 KSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380263   2 AVKRREQALQDYGRLQAKVEKYEEKEKTGPvlAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIR 81
Cdd:cd07591   114 AIKKRNHKLLDYDAARAKVRKLIDKPSEDP--TKLPRAEKELDEAKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVK 191

                          90       100
                  ....*....|....*....|..
gi 1720380263  82 AQVIYYSEMHKIFGDLTQQLDQ 103
Cdd:cd07591   192 IQLRFFTEGYERLAQVQRYLDA 213

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380263   2 AVKRREQALQDYGRLQAKVEKYEEKEKTgpvLAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIR 81
Cdd:cd07307    99 RRKKLDKARLDYDAAREKLKKLRKKKKD---SSKLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIE 175

                          90
                  ....*....|....*....
gi 1720380263  82 AQVIYYSEMHKIFGDLTQQ 100
Cdd:cd07307   176 AQSEFFKEVLKILEQLLPY 194

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720380263  34 AKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQVIYYSEMHKIFGDL 97
Cdd:cd07612   139 AKIAKAEEEFNRAQVVFEDINRELREELPILYDSRIGCYVTVFQNISNLRDTFYKEMSKLNHDL 202