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Cofilin-2
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere. Belongs to the actin-binding proteins ADF family. Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: Cytoskeletal; Motility/polarity/chemotaxis; Nuclear receptor co-regulator |
| Chromosomal Location of human Ortholog: 14q13.1 |
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Cellular Component:
actin cytoskeleton; cytoplasm; I band; nuclear matrix; Z disc
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Molecular Function:
actin filament binding; protein binding
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Biological Process:
actin filament depolymerization; actin filament fragmentation; actin filament severing; muscle cell cellular homeostasis; positive regulation of actin filament depolymerization; sarcomere organization; skeletal muscle tissue development
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Disease: Nemaline Myopathy 7
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Reference #:
Q9Y281
(UniProtKB)
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Alt. Names/Synonyms: CFL2; COF2; cofilin 2; cofilin 2 (muscle); Cofilin, muscle isoform; Cofilin-2; NEM7; nemaline myopathy type 7
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Gene Symbols: CFL2
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Molecular weight:
18,737 Da
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Basal Isoelectric point:
7.66
Predict pI for various phosphorylation states
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CST Pathways:
Actin Dynamics
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Microtubule Dynamics
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TGF-ß Signaling
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