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Conserved domains on  [gi|1624525620|ref|NP_001356843|]
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endophilin-B2 isoform d [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
 21-282 3.65e-150

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


:

Pssm-ID: 153301  Cd Length: 220  Bit Score: 422.51  E-value: 3.65e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  21 QFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAD 100
Cdd:cd07617     1 QFTEEKLGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNAELLGQYMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 101 AASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDackarlkkak 180
Cdd:cd07617    81 AANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERRLLQNRRLDLD---------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 181 aaeakaTCEGdtvpdfqetrprnyilsasasalwndEVDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 260
Cdd:cd07617   151 ------ACKA--------------------------RLKKAEHELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 198

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07617   199 VEAQATYYAQCYRHMLDLQKQL 220
 
Name Accession Description Interval E-value
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
 21-282 3.65e-150

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


Pssm-ID: 153301  Cd Length: 220  Bit Score: 422.51  E-value: 3.65e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  21 QFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAD 100
Cdd:cd07617     1 QFTEEKLGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNAELLGQYMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 101 AASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDackarlkkak 180
Cdd:cd07617    81 AANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERRLLQNRRLDLD---------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 181 aaeakaTCEGdtvpdfqetrprnyilsasasalwndEVDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 260
Cdd:cd07617   151 ------ACKA--------------------------RLKKAEHELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 198

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07617   199 VEAQATYYAQCYRHMLDLQKQL 220
BAR smart00721
BAR domain;
16-284 3.01e-65

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 206.85  E-value: 3.01e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620   16 FTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGella 95
Cdd:smart00721   6 FNRAKQKVGEKVGKAEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEGG---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620   96 qymaDAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASiSFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACkar 175
Cdd:smart00721  82 ----DDGEGLGADSSYGKALDKLGEALKKLLQVEESLSQVKR-TFILPLLNFLLGEFKEIKKARKKLERKLLDYDSA--- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  176 lkkakaaeakatcegdtvpdfqetRPRNYILSASASALWNDEVDKAEQELRVAQTEFDR-QAEVTRLLLEGISSTHVNHL 254
Cdd:smart00721 154 ------------------------RHKLKKAKKSKEKKKDEKLAKAEEELRKAKQEFEEsNAQLVEELPQLVASRVDFFV 209

                          250       260       270
                   ....*....|....*....|....*....|
gi 1624525620  255 RCLHEFVKSQTTYYAQCYRHMLDLQKQLGS 284
Cdd:smart00721 210 NCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 16-284 2.03e-57

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.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 186.77  E-value: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  16 FTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKldrkvpsrvtNGELLA 95
Cdd:pfam03114   5 FNRASQLLGEKVGGAEKTKLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQ----------PEELLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  96 QYMADAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLeGDWKTISKERRLLQNRRLDLDAckar 175
Cdd:pfam03114  75 ESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDA---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 176 lkkakaaeakatcegdtvpdfqeTRPRNYILSASASALWNDEvDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHL- 254
Cdd:pfam03114 150 -----------------------AKTRVKKAKKKKSSKAKDE-SQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVv 205

                         250       260       270
                  ....*....|....*....|....*....|
gi 1624525620 255 RCLHEFVKSQTTYYAQCYRHMLDLQKQLGS 284
Cdd:pfam03114 206 NQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
 
Name Accession Description Interval E-value
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
 21-282 3.65e-150

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


Pssm-ID: 153301  Cd Length: 220  Bit Score: 422.51  E-value: 3.65e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  21 QFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAD 100
Cdd:cd07617     1 QFTEEKLGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNAELLGQYMTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 101 AASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDackarlkkak 180
Cdd:cd07617    81 AANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISKERRLLQNRRLDLD---------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 181 aaeakaTCEGdtvpdfqetrprnyilsasasalwndEVDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 260
Cdd:cd07617   151 ------ACKA--------------------------RLKKAEHELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 198

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07617   199 VEAQATYYAQCYRHMLDLQKQL 220
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
 21-282 4.03e-132

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle.


Pssm-ID: 153278  Cd Length: 229  Bit Score: 376.73  E-value: 4.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  21 QFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAD 100
Cdd:cd07594     1 QFTEEKLGTAEKTEYDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEDFIYEKLDRKKPDRLSNLEQLGQAMIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 101 AASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACkarlkkak 180
Cdd:cd07594    81 AGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISKERKLLENKRLDLDAC-------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 181 aaeakatcegdtvpdfqETRPRNyilsasasALWNDEVDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 260
Cdd:cd07594   153 -----------------KTRVKK--------AKSAEAIEQAEQDLRVAQSEFDRQAEITKLLLEGISSTHANHLRCLRDF 207

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07594   208 VEAQMTYYAQCYQYMDDLQRQL 229
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
 21-282 1.11e-121

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain, which can bind and bend membranes. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain.


Pssm-ID: 153300  Cd Length: 229  Bit Score: 350.53  E-value: 1.11e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  21 QFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAD 100
Cdd:cd07616     1 QFTEEKFGQAEKTELDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRMNNPELLGQYMID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 101 AASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACkarlkkak 180
Cdd:cd07616    81 AGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITKERKLLQNKRLDLDAA-------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 181 aaeakatcegdtvpdfqETRPRNYILSASASAlwndevdkAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEF 260
Cdd:cd07616   153 -----------------KTRLKKAKVAEARAA--------AEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDF 207

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07616   208 VEAQMTYYAQCYQYMLDLQKQL 229
BAR smart00721
BAR domain;
16-284 3.01e-65

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 206.85  E-value: 3.01e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620   16 FTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGella 95
Cdd:smart00721   6 FNRAKQKVGEKVGKAEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEGG---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620   96 qymaDAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASiSFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACkar 175
Cdd:smart00721  82 ----DDGEGLGADSSYGKALDKLGEALKKLLQVEESLSQVKR-TFILPLLNFLLGEFKEIKKARKKLERKLLDYDSA--- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  176 lkkakaaeakatcegdtvpdfqetRPRNYILSASASALWNDEVDKAEQELRVAQTEFDR-QAEVTRLLLEGISSTHVNHL 254
Cdd:smart00721 154 ------------------------RHKLKKAKKSKEKKKDEKLAKAEEELRKAKQEFEEsNAQLVEELPQLVASRVDFFV 209

                          250       260       270
                   ....*....|....*....|....*....|
gi 1624525620  255 RCLHEFVKSQTTYYAQCYRHMLDLQKQLGS 284
Cdd:smart00721 210 NCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 16-284 2.03e-57

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.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 186.77  E-value: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  16 FTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKldrkvpsrvtNGELLA 95
Cdd:pfam03114   5 FNRASQLLGEKVGGAEKTKLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLEQ----------PEELLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  96 QYMADAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLeGDWKTISKERRLLQNRRLDLDAckar 175
Cdd:pfam03114  75 ESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEIQKHRKKLERKRLDYDA---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 176 lkkakaaeakatcegdtvpdfqeTRPRNYILSASASALWNDEvDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHL- 254
Cdd:pfam03114 150 -----------------------AKTRVKKAKKKKSSKAKDE-SQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVv 205

                         250       260       270
                  ....*....|....*....|....*....|
gi 1624525620 255 RCLHEFVKSQTTYYAQCYRHMLDLQKQLGS 284
Cdd:pfam03114 206 NQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
 31-282 3.21e-20

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. The BAR domains of endophilin-A1 and A3 form crescent-shaped dimers that can detect membrane curvature and drive membrane bending.


Pssm-ID: 153276  Cd Length: 223  Bit Score: 88.13  E-value: 3.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  31 EKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFL---YEKLDRKVPSRV---TNGeLLAQYMADAASE 104
Cdd:cd07592     1 EGTKLDDEFLEMERKTDATSKLVEDLIPKTKEYLQPNPAARAKLAMqntYSKIRGQAKSTKypqPEG-LLGEVMLKYGRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 105 LGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDackarlkkakaaea 184
Cdd:cd07592    80 LGEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEINHHRKKLEGRRLDYD-------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 185 katCE---GDTVPDfqetrprnyilsasasalwnDEVDKAEQELrvaqTEFDRQAEVTRL-LLEGisstHVNHLRCLHEF 260
Cdd:cd07592   146 ---YKkrkQGKGPD--------------------EELKQAEEKF----EESKELAENSMFnLLEN----DVEQVSQLSAL 194

                         250       260
                  ....*....|....*....|..
gi 1624525620 261 VKSQTTYYAQCYRHMLDLQKQL 282
Cdd:cd07592   195 VEAQLDYHRQSAEILEELQSKL 216
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 31-236 3.49e-15

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 73.89  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  31 EKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDR-----KVPSRVTNGELLAQYMADAASEL 105
Cdd:cd07613     1 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKirgqeKGPGYPQAEALLAEAMLKFGREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 106 GPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLKKAKAAEAK 185
Cdd:cd07613    81 GDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1624525620 186 ATCEgdtvpDFQETRPrnyILSASASALWNDEVDKAEQ--ELRVAQTEFDRQA 236
Cdd:cd07613   161 QALE-----KFDESKE---IAESSMFNLLEMDIEQVSQlsALVQAQLEYHKQA 205
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
 31-282 4.57e-13

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain.


Pssm-ID: 153298  Cd Length: 223  Bit Score: 67.82  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  31 EKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDR-----KVPSRVTNGELLAQYMADAASEL 105
Cdd:cd07614     1 EGTKLDDDFKEMEKKVDLTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKirgqvKNPGYPQSEGLLGETMIRYGKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 106 GPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLkkakaaeak 185
Cdd:cd07614    81 GDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKRQ--------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 186 atcegDTVPDfqetrprnyilsasasalwndevdkaeQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEFVKSQT 265
Cdd:cd07614   152 -----GKIPD---------------------------EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQL 199

                         250
                  ....*....|....*..
gi 1624525620 266 TYYAQCYRHMLDLQKQL 282
Cdd:cd07614   200 DYHRQAVQILDELAEKL 216
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 25-171 9.75e-13

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.


Pssm-ID: 153279 [Multi-domain]  Cd Length: 244  Bit Score: 67.36  E-value: 9.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  25 EKFGQAEKTE-LDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARveeflYEKLDRKVPSRVtngelLAQYMADAAS 103
Cdd:cd07595     2 QTVGRAEKTEvLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGED-----KDKRLKKLPEYG-----LAQSMLESSK 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525620 104 ELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDA 171
Cdd:cd07595    72 ELPDDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQKKRLSKLVLDMDS 139
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 45-281 1.37e-12

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.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 65.93  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  45 RADSTKNWTEKILRQTEVLLQpnpsarveeflyekldrKVPSRVTNGELLAQYMADAASELGP--TTPYGKTLIKVAEAE 122
Cdd:cd07307     1 KLDELEKLLKKLIKDTKKLLD-----------------SLKELPAAAEKLSEALQELGKELPDlsNTDLGEALEKFGKIQ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 123 KQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACkarlkkakaaeakatcegdtvpdfqetrpR 202
Cdd:cd07307    64 KELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAA-----------------------------R 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 203 NYILSASASALWNDEVDKAEQELRVAQTEFDrqaEVTRLLLEGISSTHVNHLR----CLHEFVKSQTTYYAQCYRHMLDL 278
Cdd:cd07307   115 EKLKKLRKKKKDSSKLAEAEEELQEAKEKYE---ELREELIEDLNKLEEKRKElflsLLLSFIEAQSEFFKEVLKILEQL 191


                  ...
gi 1624525620 279 QKQ 281
Cdd:cd07307   192 LPY 194
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
 31-170 6.28e-11

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins localized at synapses that interacts with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate.


Pssm-ID: 153299  Cd Length: 223  Bit Score: 61.57  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  31 EKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGE-----LLAQYMADAASEL 105
Cdd:cd07615     1 EGTKLDDDFQEMERKIDVTNKVVAELLSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYpqtegLLGDCMLRYGREL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624525620 106 GPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLD 170
Cdd:cd07615    81 GEESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEIGHHLKKLEGRRLDFD 145
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
 77-271 1.99e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins; 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 subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153277  Cd Length: 215  Bit Score: 51.20  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  77 YEKLDRKVP-----SRVTNGELLAQYMADAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEgD 151
Cdd:cd07593    34 VEYLSKKKPllddkDKCLPVEALGLVMINHGEEFPQDSEYGSCLSKLGRAHCKIGTLQEEFADRLSDTFLANIERSLA-E 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 152 WKTISKERRLLQNRRLDLDackarlkkakaaeakatcegdtvpdfqetrprnyilsASASALWNDEVDK--AEQELRVAQ 229
Cdd:cd07593   113 MKEYHSARKKLESRRLAYD-------------------------------------AALTKSQKAKKEDsrLEEELRRAK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1624525620 230 TEFDRQAEVTRLLLEGISSTHVNHLRCLHEFVKSQTTYYAQC 271
Cdd:cd07593   156 AKYEESSEDVEARMVAIKESEADQYRDLTDLLDAELDYHQQS 197
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
 110-282 5.76e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; 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. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 40.80  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 110 PYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKArlkkakaaeakatce 189
Cdd:cd07600   104 PLSKALGKYSDAEEKIAEARLEQDQLIQKEFNAKLRETLNTSFQKAHKARKKVEDKRLQLDTARA--------------- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620 190 gdtvpDFQETRPRNYILSAsasalwNDEVDKAEQELrVAQTEfdrqAEVTrLLLEGISSThvNHLRCLHEFVKSQTTYYA 269
Cdd:cd07600   169 -----ELKSAEPAEKQEAA------RVEVETAEDEF-VSATE----EAVE-LMKEVLDNP--EPLQLLKELVKAQLAYHK 229

                         170
                  ....*....|...
gi 1624525620 270 QCYRHMLDLQKQL 282
Cdd:cd07600   230 TAAELLEELLSVL 242
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 99-170 9.94e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 40.04  E-value: 9.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624525620  99 ADAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQN----RRLDLD 170
Cdd:cd07605    54 GELASQSRGSQELGEALKQIVDTHKSIEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKeykqKREDLD 129
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 28-172 1.05e-03

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It 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. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 40.40  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  28 GQAEKTELDAhfENLLA---RADSTKNWTEKILRQTEVLLQPNPSARVEeflyeKLDRKVPSRVtngelLAQYMADAASE 104
Cdd:cd07618     5 GRAEKTEVLS--EDLLQierRLDTVRSVSHNVHKRLIACFQGQVGTDAE-----KRHKKLPLTA-----LAQNMQEGSAQ 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525620 105 LGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDAC 172
Cdd:cd07618    73 LGEESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQRKQLAKLVLDWDSA 140
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 28-170 2.34e-03

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153303  Cd Length: 248  Bit Score: 39.26  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525620  28 GQAEKTELDAhfENLL---ARADSTKNWTEKILRQTEVLLQPNPSARVEeflyeKLDRKVPSRVtngelLAQYMADAASE 104
Cdd:cd07619     5 GRAEKTEVLS--EDLLqveKRLELVKQVSHSTHKKLTACLQGQQGVDAD-----KRSKKLPLTT-----LAQCMVEGAAV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624525620 105 LGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLD 170
Cdd:cd07619    73 LGDDSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKLVLDMD 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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