The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. 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 568927288  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATR 232
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927288 233 TSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 290
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. 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 568927288  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATR 232
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927288 233 TSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 290
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

MAEBL; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288  150 QDYRQAEMLMNMAKVErlEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHAETELQRA--- 226
Cdd:PTZ00121 1650 EELKKAEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeee 1727

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568927288  227 -TIDATRTSRHLEE--------TIDNFEKQKIKDIK 253
Cdd:PTZ00121 1728 nKIKAEEAKKEAEEdkkkaeeaKKDEEEKKKIAHLK 1763

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. 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 568927288  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATR 232
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927288 233 TSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 290
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

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 568927288  74 NLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNeinlyastetPNLKQGLKDFADEFAKLQDYR 153
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN----------TDLGEALEKFGKIQKELEEFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 154 QAEmlmnmakVERLEAKVVEPLKAYgtivkmKRDDLKATLTARNREAKQLSQLERTRQRNPSDR----------HAETEL 223
Cdd:cd07307   71 DQL-------EQKLENKVIEPLKEY------LKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRkkkkdssklaEAEEEL 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568927288 224 QRATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQN 280
Cdd:cd07307  138 QEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. 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 568927288  72 RRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVneinlyastetpnLKQGLKDFADEFAKLQD 151
Cdd:cd07664   28 QQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTA-------------LSRALSQLAEVEEKIDQ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 152 YRQAEMLMNMAKVERLEAKVVEPLKAYGTIVK------MKRDDLKATLTaRNREAKQLSQL----ERTRQRNPSDRHAET 221
Cdd:cd07664   95 LHQDQAFADFYLFSELLGDYIRLIAAVKGVFDqrmkcwQKWQDAQVTLQ-KKREAEAKLQYankpDKLQQAKDEIKEWEA 173

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568927288 222 ELQRATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFI 260
Cdd:cd07664  174 KVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYL 212

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 135 LKQGLKDFADEfaKLQDYRQAEMLMNMAKVE------------RLEAKVVEPLKAYgtivkmKRDDLKATLTARNREAKQ 202
Cdd:cd07595   62 LAQSMLESSKE--LPDDSLLGKVLKLCGEAQntlarelvdhemNVEEDVLSPLQNI------LEVEIPNIQKQKKRLSKL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927288 203 LSQLERTRQRNpsdrHAETELQRATIDATRtSRHLEETIDN----FEKQKIK-------------DIKNILSEFITIEML 265
Cdd:cd07595  134 VLDMDSARSRY----NAAHKSSGGQGAAAK-VDALKDEYEEaelkLEQCRDAlatdmyeflakeaEIASYLIDLIEAQRE 208

                        170
                 ....*....|....*..
gi 568927288 266 FHGKALEVFTAAYQNIQ 282
Cdd:cd07595  209 YHRTALSVLEAVLPELQ 225