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Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008]
Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes (). Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions.
ANK3: In skeletal muscle, required for costamere localization of DMD and betaDAG1. Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Genetic variations in ANK3 are associated with autism spectrum disorders susceptibility. 3 isoforms of the human protein are produced by alternative splicing.
Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis
Cellular Component: axon; basal plasma membrane; basolateral plasma membrane; cell surface; cytoplasm; dendrite; lateral plasma membrane; membrane; neuromuscular junction; neuron projection; paranode region of axon; plasma membrane; postsynaptic membrane; sarcolemma; sarcoplasmic reticulum; synapse; T-tubule; tight junction; Z disc
Molecular Function: cadherin binding; cytoskeletal adaptor activity; cytoskeletal protein binding; protein binding; protein binding, bridging; spectrin binding; structural constituent of cytoskeleton
Biological Process: axon guidance; axonogenesis; cytokinesis after mitosis; establishment of protein localization; generation of action potential; Golgi to plasma membrane protein transport; plasma membrane organization and biogenesis; positive regulation of action potential; positive regulation of homotypic cell-cell adhesion; positive regulation of membrane potential; regulation of potassium ion transport; synapse organization and biogenesis
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