Chain C, Gelsolin
gelsolin/scinderin family protein; villin/gelsolin family protein( domain architecture ID 10181872)
gelsolin/scinderin family protein similar to portion of Homo sapiens gelsolin, a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping), and to portion of Homo sapiens scinderin, a Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane; villin/gelsolin family protein similar to portion of Homo sapiens gelsolin, a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping), and to portion of Homo sapiens villin, an epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments
List of domain hits
Name | Accession | Description | Interval | E-value | |||
gelsolin_S4_like | cd11293 | Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ... |
1-101 | 5.39e-57 | |||
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. : Pssm-ID: 200449 Cd Length: 101 Bit Score: 180.16 E-value: 5.39e-57
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gelsolin_S6_like | cd11291 | Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ... |
228-326 | 1.39e-55 | |||
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. : Pssm-ID: 200447 [Multi-domain] Cd Length: 99 Bit Score: 176.33 E-value: 1.39e-55
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gelsolin_S5_like | cd11288 | Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ... |
123-211 | 4.94e-44 | |||
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. : Pssm-ID: 200444 Cd Length: 92 Bit Score: 146.61 E-value: 4.94e-44
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Name | Accession | Description | Interval | E-value | |||
gelsolin_S4_like | cd11293 | Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ... |
1-101 | 5.39e-57 | |||
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200449 Cd Length: 101 Bit Score: 180.16 E-value: 5.39e-57
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gelsolin_S6_like | cd11291 | Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ... |
228-326 | 1.39e-55 | |||
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200447 [Multi-domain] Cd Length: 99 Bit Score: 176.33 E-value: 1.39e-55
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gelsolin_S5_like | cd11288 | Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ... |
123-211 | 4.94e-44 | |||
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200444 Cd Length: 92 Bit Score: 146.61 E-value: 4.94e-44
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
234-325 | 5.24e-27 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 101.99 E-value: 5.24e-27
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
10-104 | 2.00e-26 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 100.44 E-value: 2.00e-26
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
128-210 | 4.52e-21 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 86.19 E-value: 4.52e-21
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Gelsolin | pfam00626 | Gelsolin repeat; |
241-319 | 2.50e-18 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 78.12 E-value: 2.50e-18
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Gelsolin | pfam00626 | Gelsolin repeat; |
16-98 | 4.19e-17 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 75.04 E-value: 4.19e-17
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Gelsolin | pfam00626 | Gelsolin repeat; |
136-204 | 1.55e-09 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 53.85 E-value: 1.55e-09
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Name | Accession | Description | Interval | E-value | |||
gelsolin_S4_like | cd11293 | Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ... |
1-101 | 5.39e-57 | |||
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200449 Cd Length: 101 Bit Score: 180.16 E-value: 5.39e-57
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gelsolin_S6_like | cd11291 | Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ... |
228-326 | 1.39e-55 | |||
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200447 [Multi-domain] Cd Length: 99 Bit Score: 176.33 E-value: 1.39e-55
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gelsolin_S5_like | cd11288 | Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ... |
123-211 | 4.94e-44 | |||
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200444 Cd Length: 92 Bit Score: 146.61 E-value: 4.94e-44
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gelsolin_S1_like | cd11290 | Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ... |
4-112 | 6.26e-34 | |||
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200446 Cd Length: 113 Bit Score: 120.79 E-value: 6.26e-34
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
234-325 | 5.24e-27 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 101.99 E-value: 5.24e-27
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
10-104 | 2.00e-26 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 100.44 E-value: 2.00e-26
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GEL | smart00262 | Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ... |
128-210 | 4.52e-21 | |||
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains. Pssm-ID: 214590 [Multi-domain] Cd Length: 90 Bit Score: 86.19 E-value: 4.52e-21
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gelsolin_S3_like | cd11292 | Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ... |
229-322 | 5.15e-20 | |||
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200448 Cd Length: 98 Bit Score: 83.45 E-value: 5.15e-20
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gelsolin_like | cd11280 | Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
8-101 | 6.88e-20 | |||
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200436 Cd Length: 88 Bit Score: 82.80 E-value: 6.88e-20
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gelsolin_like | cd11280 | Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
228-322 | 8.05e-19 | |||
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200436 Cd Length: 88 Bit Score: 80.10 E-value: 8.05e-19
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Gelsolin | pfam00626 | Gelsolin repeat; |
241-319 | 2.50e-18 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 78.12 E-value: 2.50e-18
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gelsolin_like | cd11280 | Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ... |
124-207 | 2.67e-18 | |||
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200436 Cd Length: 88 Bit Score: 78.56 E-value: 2.67e-18
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Gelsolin | pfam00626 | Gelsolin repeat; |
16-98 | 4.19e-17 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 75.04 E-value: 4.19e-17
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gelsolin_S2_like | cd11289 | Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ... |
125-208 | 2.88e-10 | |||
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200445 Cd Length: 92 Bit Score: 56.48 E-value: 2.88e-10
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Gelsolin | pfam00626 | Gelsolin repeat; |
136-204 | 1.55e-09 | |||
Gelsolin repeat; Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 53.85 E-value: 1.55e-09
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ADF_gelsolin | cd00013 | Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ... |
124-198 | 3.59e-05 | |||
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Pssm-ID: 200435 Cd Length: 97 Bit Score: 42.07 E-value: 3.59e-05
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gelsolin_S2_like | cd11289 | Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ... |
228-325 | 6.50e-05 | |||
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200445 Cd Length: 92 Bit Score: 41.07 E-value: 6.50e-05
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gelsolin_S3_like | cd11292 | Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ... |
125-200 | 5.48e-04 | |||
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins. Pssm-ID: 200448 Cd Length: 98 Bit Score: 38.77 E-value: 5.48e-04
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Blast search parameters | ||||
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