islet cell autoantigen 1 isoform X2 [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
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 ... |
53-256 | 2.88e-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: 389.53 E-value: 2.88e-135
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| ICA69 | pfam04629 | Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ... |
261-512 | 4.41e-70 | |||||
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: 223.89 E-value: 4.41e-70
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| 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 ... |
53-256 | 2.88e-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: 389.53 E-value: 2.88e-135
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| Arfaptin | smart01015 | Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ... |
28-249 | 2.12e-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: 321.53 E-value: 2.12e-108
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| Arfaptin | pfam06456 | Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ... |
44-249 | 1.96e-100 | |||||
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: 300.81 E-value: 1.96e-100
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| ICA69 | pfam04629 | Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ... |
261-512 | 4.41e-70 | |||||
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: 223.89 E-value: 4.41e-70
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| 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 ... |
53-256 | 2.88e-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: 389.53 E-value: 2.88e-135
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| Arfaptin | smart01015 | Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ... |
28-249 | 2.12e-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: 321.53 E-value: 2.12e-108
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| Arfaptin | pfam06456 | Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ... |
44-249 | 1.96e-100 | |||||
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: 300.81 E-value: 1.96e-100
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| ICA69 | pfam04629 | Islet cell autoantigen ICA69, C-terminal domain; This family includes a 69 kD protein which ... |
261-512 | 4.41e-70 | |||||
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: 223.89 E-value: 4.41e-70
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| BAR_Arfaptin_like | cd00011 | The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that ... |
53-254 | 1.47e-62 | |||||
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: 203.23 E-value: 1.47e-62
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| BAR_Arfaptin | cd07660 | The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, ... |
137-240 | 1.47e-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: 43.08 E-value: 1.47e-04
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