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Conserved domains on  [gi|356582438|ref|NP_001239195|]
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islet cell autoantigen 1 isoform 2 [Mus musculus]

Protein Classification

islet cell autoantigen 1 family protein( domain architecture ID 10166608)

islet cell autoantigen 1 family protein, similar to human islet cell autoantigen 1 which functions as an autoantigen in insulin-dependent diabetes mellitus and primary Sjogren's syndrome

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_ICA69 cd07661
The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of ...
52-255 7.56e-135

The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is highly expressed in brain and beta cells. It is involved in membrane trafficking at the Golgi complex in neurosecretory cells. It is coexpressed with Protein Interacting with C Kinase 1 (PICK1), also a the BAR domain containing protein, in many tissues at different developmental stages. In neurons, ICA69 colocalizes with PICK1 in cell bodies and dendrites but is absent in synapses where PICK1 is enriched. ICA69 contains an N-terminal BAR domain and a conserved C-terminal domain of unknown function. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. Autoantibodies against ICA69 have been identified in patients with insulin-dependent diabetes mellitus, rheumatoid arthritis, and primary Sjogren's syndrome. ICA69 has also been shown to be released by pancreatic cancer cells.


:

Pssm-ID: 153345  Cd Length: 204  Bit Score: 386.45  E-value: 7.56e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  52 DADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRN 131
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438 132 PLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDV 211
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 356582438 212 CQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESF 255
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEAF 204
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
260-457 8.47e-77

Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which has been identified as an islet cell autoantigen in type I diabetes mellitus. Its precise function is unknown.


:

Pssm-ID: 461374  Cd Length: 241  Bit Score: 239.68  E-value: 8.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  260 PYEFTTLKSLQDPMKKLVEKEGKKtswRENREAVAPEPRQLISLEDE-------------HKDSSAYKRPIDELLDGKPE 326
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKK---QESEELTENLDSQLISLDDEehagessetavedHNETGFTVGSLEDPQFSGSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  327 EACLGPTAGTPEPESGDKDDLLLLNEIFSTSCLDEGEFSREWAAVFGDDQLKEPAPMGAQGEPDPKPQIGSGFLPSQLLD 406
Cdd:pfam04629  78 NVAKDLLVDSLEGEDFEKDDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLAPSTSSGFLPSQLLD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  407 QNMKDLQASLQ---------------------------------EPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHE 453
Cdd:pfam04629 158 LNLNDLQASFNgwasssvsppsqpqplqhpqspnqnvskpkkkeKAPNSNKDMSAWFNLFADLDPLSNPDAIGKSDDEHE 237

                  ....
gi 356582438  454 LLNA 457
Cdd:pfam04629 238 LLNA 241
 
Name Accession Description Interval E-value
BAR_ICA69 cd07661
The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of ...
52-255 7.56e-135

The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is highly expressed in brain and beta cells. It is involved in membrane trafficking at the Golgi complex in neurosecretory cells. It is coexpressed with Protein Interacting with C Kinase 1 (PICK1), also a the BAR domain containing protein, in many tissues at different developmental stages. In neurons, ICA69 colocalizes with PICK1 in cell bodies and dendrites but is absent in synapses where PICK1 is enriched. ICA69 contains an N-terminal BAR domain and a conserved C-terminal domain of unknown function. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. Autoantibodies against ICA69 have been identified in patients with insulin-dependent diabetes mellitus, rheumatoid arthritis, and primary Sjogren's syndrome. ICA69 has also been shown to be released by pancreatic cancer cells.


Pssm-ID: 153345  Cd Length: 204  Bit Score: 386.45  E-value: 7.56e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  52 DADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRN 131
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438 132 PLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDV 211
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 356582438 212 CQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESF 255
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEAF 204
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
27-248 9.35e-108

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 214974  Cd Length: 217  Bit Score: 318.06  E-value: 9.35e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438    27 QKYWETKQAFIKATGKKEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKT 106
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDEHVVASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438   107 -RAGKMMQATGKALCFSSQQRLalrNPLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRgalLWMKDVSQELDPDLYK 185
Cdd:smart01015  81 lKAFGMMAETQKALCKSGEQLL---APLNPFISDVNTFVNKAIEDTLLTIKRYEDARTEYR---AWMKDVSEELDPEEYK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582438   186 QMEKFRKVQTQVRLAKKNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTM 248
Cdd:smart01015 155 QLEKFRKAQRQVQEAKAKFEKLRNDVCQKVDLLEASRVNVLSHQLLLFQNALAAYWEKTAHAL 217
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
43-248 9.12e-101

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 399453  Cd Length: 207  Bit Score: 299.66  E-value: 9.12e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438   43 KEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRA-GKMMQATGKALCF 121
Cdd:pfam06456   1 KEDSHAITSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKHEKQQAaGEAFTAFGETHRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  122 SSQQRLALRNPLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAK 201
Cdd:pfam06456  81 LAKQGLALLVPLNRFISSVNTFVNKAIPDTLLTIKRYEDARTEYRAYLLWMKEASDELDPDVAKQMPKFRVAQGNYQEAK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 356582438  202 KNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTM 248
Cdd:pfam06456 161 AKFDKLRTDVLQKMDLLEANRINVLSHQLTLYQNTLAAYYSKNAKAL 207
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
260-457 8.47e-77

Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which has been identified as an islet cell autoantigen in type I diabetes mellitus. Its precise function is unknown.


Pssm-ID: 461374  Cd Length: 241  Bit Score: 239.68  E-value: 8.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  260 PYEFTTLKSLQDPMKKLVEKEGKKtswRENREAVAPEPRQLISLEDE-------------HKDSSAYKRPIDELLDGKPE 326
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKK---QESEELTENLDSQLISLDDEehagessetavedHNETGFTVGSLEDPQFSGSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  327 EACLGPTAGTPEPESGDKDDLLLLNEIFSTSCLDEGEFSREWAAVFGDDQLKEPAPMGAQGEPDPKPQIGSGFLPSQLLD 406
Cdd:pfam04629  78 NVAKDLLVDSLEGEDFEKDDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLAPSTSSGFLPSQLLD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  407 QNMKDLQASLQ---------------------------------EPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHE 453
Cdd:pfam04629 158 LNLNDLQASFNgwasssvsppsqpqplqhpqspnqnvskpkkkeKAPNSNKDMSAWFNLFADLDPLSNPDAIGKSDDEHE 237

                  ....
gi 356582438  454 LLNA 457
Cdd:pfam04629 238 LLNA 241
 
Name Accession Description Interval E-value
BAR_ICA69 cd07661
The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of ...
52-255 7.56e-135

The Bin/Amphiphysin/Rvs (BAR) domain of Islet Cell Autoantigen 69-kDa; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is highly expressed in brain and beta cells. It is involved in membrane trafficking at the Golgi complex in neurosecretory cells. It is coexpressed with Protein Interacting with C Kinase 1 (PICK1), also a the BAR domain containing protein, in many tissues at different developmental stages. In neurons, ICA69 colocalizes with PICK1 in cell bodies and dendrites but is absent in synapses where PICK1 is enriched. ICA69 contains an N-terminal BAR domain and a conserved C-terminal domain of unknown function. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. Autoantibodies against ICA69 have been identified in patients with insulin-dependent diabetes mellitus, rheumatoid arthritis, and primary Sjogren's syndrome. ICA69 has also been shown to be released by pancreatic cancer cells.


Pssm-ID: 153345  Cd Length: 204  Bit Score: 386.45  E-value: 7.56e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  52 DADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRN 131
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438 132 PLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDV 211
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 356582438 212 CQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESF 255
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEAF 204
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
27-248 9.35e-108

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 214974  Cd Length: 217  Bit Score: 318.06  E-value: 9.35e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438    27 QKYWETKQAFIKATGKKEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKT 106
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDEHVVASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438   107 -RAGKMMQATGKALCFSSQQRLalrNPLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRgalLWMKDVSQELDPDLYK 185
Cdd:smart01015  81 lKAFGMMAETQKALCKSGEQLL---APLNPFISDVNTFVNKAIEDTLLTIKRYEDARTEYR---AWMKDVSEELDPEEYK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582438   186 QMEKFRKVQTQVRLAKKNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTM 248
Cdd:smart01015 155 QLEKFRKAQRQVQEAKAKFEKLRNDVCQKVDLLEASRVNVLSHQLLLFQNALAAYWEKTAHAL 217
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
43-248 9.12e-101

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 399453  Cd Length: 207  Bit Score: 299.66  E-value: 9.12e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438   43 KEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRA-GKMMQATGKALCF 121
Cdd:pfam06456   1 KEDSHAITSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKHEKQQAaGEAFTAFGETHRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  122 SSQQRLALRNPLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAK 201
Cdd:pfam06456  81 LAKQGLALLVPLNRFISSVNTFVNKAIPDTLLTIKRYEDARTEYRAYLLWMKEASDELDPDVAKQMPKFRVAQGNYQEAK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 356582438  202 KNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTM 248
Cdd:pfam06456 161 AKFDKLRTDVLQKMDLLEANRINVLSHQLTLYQNTLAAYYSKNAKAL 207
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
260-457 8.47e-77

Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which has been identified as an islet cell autoantigen in type I diabetes mellitus. Its precise function is unknown.


Pssm-ID: 461374  Cd Length: 241  Bit Score: 239.68  E-value: 8.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  260 PYEFTTLKSLQDPMKKLVEKEGKKtswRENREAVAPEPRQLISLEDE-------------HKDSSAYKRPIDELLDGKPE 326
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKK---QESEELTENLDSQLISLDDEehagessetavedHNETGFTVGSLEDPQFSGSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  327 EACLGPTAGTPEPESGDKDDLLLLNEIFSTSCLDEGEFSREWAAVFGDDQLKEPAPMGAQGEPDPKPQIGSGFLPSQLLD 406
Cdd:pfam04629  78 NVAKDLLVDSLEGEDFEKDDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLAPSTSSGFLPSQLLD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  407 QNMKDLQASLQ---------------------------------EPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHE 453
Cdd:pfam04629 158 LNLNDLQASFNgwasssvsppsqpqplqhpqspnqnvskpkkkeKAPNSNKDMSAWFNLFADLDPLSNPDAIGKSDDEHE 237

                  ....
gi 356582438  454 LLNA 457
Cdd:pfam04629 238 LLNA 241
BAR_Arfaptin_like cd00011
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that ...
52-253 9.43e-63

The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that binds and bends membranes; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization, lipid binding and curvature sensing module present in Arfaptins, PICK1, ICA69, and similar proteins. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also binds to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Protein Interacting with C Kinase 1 (PICK1) plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is involved in membrane trafficking at the Golgi complex in neurosecretory cells. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153270  Cd Length: 203  Bit Score: 202.08  E-value: 9.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  52 DADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRN 131
Cdd:cd00011    1 DLELELQLELLRETKRKYESVLQLGRALTAHLYSLSQTQHALGDAFADLSQKDPELAGEEFGYNAEAQKLLCKNGETLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438 132 PLCRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDV 211
Cdd:cd00011   81 AVNFFVSSINTLVTKAIEDTLLTVKQYEAARLEYDAYRLDLKELSLEPRDDTAGTRGRLRSAQATFQEHRDKFEKLRGDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 356582438 212 CQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHE 253
Cdd:cd00011  161 AIKLKFLEENKIKVMHKQLLLFHNTVSAYFAGNQKVLEQTLQ 202
BAR_Arfaptin cd07660
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, ...
52-239 1.48e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also bind to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Mammals contain at least two isoforms of Arfaptin. Arfaptin 1 has been shown to inhibit the activation of Arf-dependent phospholipase D (PLD) and the secretion of matrix metalloproteinase-9 (MMP-9), an enzyme implicated in cancer invasiveness and metastasis. Arfaptin 2 regulates the aggregation of the protein huntingtin, which is implicated in Huntington disease. Arfaptins are single-domain proteins with a BAR-like structure. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153344  Cd Length: 201  Bit Score: 42.70  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438  52 DADLDAKLELFHSIQR---TCLDLSK--AIVLYQkricfLSQEENELGKF-----LRSQGFQDKTRagkMMQATGKALCF 121
Cdd:cd07660    1 DLELEAQIEVLRDTQRkyeSVLRLARalASQFYQ-----MLQTQKALGDAfadlsQKSPELQEEFT---YNAETQKLLCK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582438 122 SSQQRLALRNplcRFHQEVETFRHRAISDTWLTVNRMEQYRTEYRGallWMKDVSQ-ELDPDLYKQMEKFRKVQTQVRLA 200
Cdd:cd07660   73 NGETLLGALN---FFVSSLNTLVNKTMEDTLMTVKQYESARIEYDA---YRNDLEAlNLGPRDAATSARLEEAQRRFQAH 146
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 356582438 201 KKNFDKLKMDVCQKVDLLGASRCNLLSHmlatyQTTLLH 239
Cdd:cd07660  147 KDKYEKLRNDVSVKLKFLEENKVKVMHK-----QLLLFH 180
 
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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