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Conserved domains on  [gi|568599857|ref|NP_001275551|]
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islet cell autoantigen 1-like protein isoform 1 [Homo sapiens]

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 ...
46-248 8.45e-115

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: 336.37  E-value: 8.45e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  46 DAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQAGKMMDATGKALCSSAKQRLALCT 125
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857 126 PLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSKASFDKLKMDV 205
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568599857 206 CQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMMSQIHEA 248
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEA 203
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
254-482 4.63e-99

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: 297.46  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  254 PYDFVALKQLQDTPSKISEDNKDEQIGGFLTEQLN-KLVLSDEE--ASFESEQANKDHNEKHSQMREFGAPQFSNSENVA 330
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKKQESEELTENLDsQLISLDDEehAGESSETAVEDHNETGFTVGSLEDPQFSGSENVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  331 KDLPVDSLEGEDFEK-EFSFLNNLLSSGSSSTSEFTQECQTAFGSPSASLTSQEPSMGSEPLA--HSSRFLPSQLFDLGF 407
Cdd:pfam04629  81 KDLLVDSLEGEDFEKdDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLApsTSSGFLPSQLLDLNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  408 HVAGA-FNNWVSQEES----ELCLSHTDNQPVPSQSPKKLTRSPNnGNQDMSAWFNLFADLDPLSNPDAIGHSDD--ELL 480
Cdd:pfam04629 161 NDLQAsFNGWASSSVSppsqPQPLQHPQSPNQNVSKPKKKEKAPN-SNKDMSAWFNLFADLDPLSNPDAIGKSDDehELL 239

                  ..
gi 568599857  481 NA 482
Cdd:pfam04629 240 NA 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 ...
46-248 8.45e-115

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: 336.37  E-value: 8.45e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  46 DAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQAGKMMDATGKALCSSAKQRLALCT 125
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857 126 PLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSKASFDKLKMDV 205
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568599857 206 CQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMMSQIHEA 248
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEA 203
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
21-242 6.41e-102

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: 303.81  E-value: 6.41e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857    21 KKYWKTKQVFIKATGKKEDEHLVASDAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDAT 100
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDEHVVASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857   101 -QAGKMMDATGKALCSSAKQRLAlctPLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRgalLWMKDVSQELDPDTLK 179
Cdd:smart01015  81 lKAFGMMAETQKALCKSGEQLLA---PLNPFISDVNTFVNKAIEDTLLTIKRYEDARTEYR---AWMKDVSEELDPEEYK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568599857   180 QMEKFRKVQMQVRNSKASFDKLKMDVCQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMM 242
Cdd:smart01015 155 QLEKFRKAQRQVQEAKAKFEKLRNDVCQKVDLLEASRVNVLSHQLLLFQNALAAYWEKTAHAL 217
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
254-482 4.63e-99

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: 297.46  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  254 PYDFVALKQLQDTPSKISEDNKDEQIGGFLTEQLN-KLVLSDEE--ASFESEQANKDHNEKHSQMREFGAPQFSNSENVA 330
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKKQESEELTENLDsQLISLDDEehAGESSETAVEDHNETGFTVGSLEDPQFSGSENVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  331 KDLPVDSLEGEDFEK-EFSFLNNLLSSGSSSTSEFTQECQTAFGSPSASLTSQEPSMGSEPLA--HSSRFLPSQLFDLGF 407
Cdd:pfam04629  81 KDLLVDSLEGEDFEKdDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLApsTSSGFLPSQLLDLNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  408 HVAGA-FNNWVSQEES----ELCLSHTDNQPVPSQSPKKLTRSPNnGNQDMSAWFNLFADLDPLSNPDAIGHSDD--ELL 480
Cdd:pfam04629 161 NDLQAsFNGWASSSVSppsqPQPLQHPQSPNQNVSKPKKKEKAPN-SNKDMSAWFNLFADLDPLSNPDAIGKSDDehELL 239

                  ..
gi 568599857  481 NA 482
Cdd:pfam04629 240 NA 241
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
37-242 1.31e-93

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: 282.32  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857   37 KEDEHLVASDAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQA-GKMMDATGKALCS 115
Cdd:pfam06456   1 KEDSHAITSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKHEKQQAaGEAFTAFGETHRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  116 SAKQRLALCTPLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSK 195
Cdd:pfam06456  81 LAKQGLALLVPLNRFISSVNTFVNKAIPDTLLTIKRYEDARTEYRAYLLWMKEASDELDPDVAKQMPKFRVAQGNYQEAK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568599857  196 ASFDKLKMDVCQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMM 242
Cdd:pfam06456 161 AKFDKLRTDVLQKMDLLEANRINVLSHQLTLYQNTLAAYYSKNAKAL 207
 
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 ...
46-248 8.45e-115

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: 336.37  E-value: 8.45e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  46 DAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQAGKMMDATGKALCSSAKQRLALCT 125
Cdd:cd07661    1 DAELDAKLELFRSVQDTCLELLKIIDNYQERLCILSQEENVLGKFLKEQGKIDKTTAGKMMAATGKALSFSSQQRLALRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857 126 PLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSKASFDKLKMDV 205
Cdd:cd07661   81 PLLRLYQEVETFRERAIADTLQTIQRMEKCRTEYRAALLWMKSVSQELDPDTYKQLEKFRKAQAQVRSAKERFDKLKMDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568599857 206 CQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMMSQIHEA 248
Cdd:cd07661  161 CQKVDLLGASRCNLLSHALVTYQNTLLQFWEKTSRTMATIHEA 203
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
21-242 6.41e-102

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: 303.81  E-value: 6.41e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857    21 KKYWKTKQVFIKATGKKEDEHLVASDAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDAT 100
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDEHVVASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857   101 -QAGKMMDATGKALCSSAKQRLAlctPLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRgalLWMKDVSQELDPDTLK 179
Cdd:smart01015  81 lKAFGMMAETQKALCKSGEQLLA---PLNPFISDVNTFVNKAIEDTLLTIKRYEDARTEYR---AWMKDVSEELDPEEYK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568599857   180 QMEKFRKVQMQVRNSKASFDKLKMDVCQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMM 242
Cdd:smart01015 155 QLEKFRKAQRQVQEAKAKFEKLRNDVCQKVDLLEASRVNVLSHQLLLFQNALAAYWEKTAHAL 217
ICA69 pfam04629
Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ...
254-482 4.63e-99

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: 297.46  E-value: 4.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  254 PYDFVALKQLQDTPSKISEDNKDEQIGGFLTEQLN-KLVLSDEE--ASFESEQANKDHNEKHSQMREFGAPQFSNSENVA 330
Cdd:pfam04629   1 PYEFTTLKDLQDPVEKLTEKGKKKQESEELTENLDsQLISLDDEehAGESSETAVEDHNETGFTVGSLEDPQFSGSENVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  331 KDLPVDSLEGEDFEK-EFSFLNNLLSSGSSSTSEFTQECQTAFGSPSASLTSQEPSMGSEPLA--HSSRFLPSQLFDLGF 407
Cdd:pfam04629  81 KDLLVDSLEGEDFEKdDMALLNELLSPGSLSEGEFSQEWQAVFGSFTLSLSAQTPSAGEEPLApsTSSGFLPSQLLDLNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  408 HVAGA-FNNWVSQEES----ELCLSHTDNQPVPSQSPKKLTRSPNnGNQDMSAWFNLFADLDPLSNPDAIGHSDD--ELL 480
Cdd:pfam04629 161 NDLQAsFNGWASSSVSppsqPQPLQHPQSPNQNVSKPKKKEKAPN-SNKDMSAWFNLFADLDPLSNPDAIGKSDDehELL 239

                  ..
gi 568599857  481 NA 482
Cdd:pfam04629 240 NA 241
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
37-242 1.31e-93

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: 282.32  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857   37 KEDEHLVASDAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQA-GKMMDATGKALCS 115
Cdd:pfam06456   1 KEDSHAITSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKHEKQQAaGEAFTAFGETHRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  116 SAKQRLALCTPLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSK 195
Cdd:pfam06456  81 LAKQGLALLVPLNRFISSVNTFVNKAIPDTLLTIKRYEDARTEYRAYLLWMKEASDELDPDVAKQMPKFRVAQGNYQEAK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568599857  196 ASFDKLKMDVCQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMM 242
Cdd:pfam06456 161 AKFDKLRTDVLQKMDLLEANRINVLSHQLTLYQNTLAAYYSKNAKAL 207
BAR_Arfaptin_like cd00011
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that ...
46-248 8.41e-73

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: 228.65  E-value: 8.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  46 DAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELGLFLKFQAERDATQAGKMMDATGKALCSSAKQRLALCT 125
Cdd:cd00011    1 DLELELQLELLRETKRKYESVLQLGRALTAHLYSLSQTQHALGDAFADLSQKDPELAGEEFGYNAEAQKLLCKNGETLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857 126 PLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGALLWMKDVSQELDPDTLKQMEKFRKVQMQVRNSKASFDKLKMDV 205
Cdd:cd00011   81 AVNFFVSSINTLVTKAIEDTLLTVKQYEAARLEYDAYRLDLKELSLEPRDDTAGTRGRLRSAQATFQEHRDKFEKLRGDV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568599857 206 CQKVDLLGASRCNMLSHSLTTYQRTLLGFWKKTARMMSQIHEA 248
Cdd:cd00011  161 AIKLKFLEENKIKVMHKQLLLFHNTVSAYFAGNQKVLEQTLQQ 203
BAR_Arfaptin cd07660
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, ...
46-224 1.54e-06

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: 48.86  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857  46 DAELDAKLEVFHSVQETCTELLKIIEKYQLRLNVISEEENELG-LFLKFQAERDATQAGKMMDA-TGKALCSSAKQRLAl 123
Cdd:cd07660    1 DLELEAQIEVLRDTQRKYESVLRLARALASQFYQMLQTQKALGdAFADLSQKSPELQEEFTYNAeTQKLLCKNGETLLG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568599857 124 ctPLSRLKQEVATFSQRAVSDTLMTINRMEQARTEYRGallWMKDVSQ-ELDPDTLKQMEKFRKVQMQVRNSKASFDKLK 202
Cdd:cd07660   80 --ALNFFVSSLNTLVNKTMEDTLMTVKQYESARIEYDA---YRNDLEAlNLGPRDAATSARLEEAQRRFQAHKDKYEKLR 154
                        170       180
                 ....*....|....*....|..
gi 568599857 203 MDVCQKVDLLGASRCNMLSHSL 224
Cdd:cd07660  155 NDVSVKLKFLEENKVKVMHKQL 176
 
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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