| Description | ACVR2 is a member of the transforming growth factor beta (TGF-b) receptor family. It is a 70-75kDA protein consisting of 513 amino acids. It is a transmembrane receptor for activin, with a cysteine-rich extracellular ligand-binding domain, a single pass transmembrane domain, and an intracellular domain with constitutive serine/threonine kinase activity. Upon binding activin, ACVR2 associates with and phosphorylates ACVR1. ACVR1, in turn, phosphorylates Smad2 and/or Smad3. Phosphorylated Smad2 and Smad3 associate with Smad4, translocate to the nucleus, and regulate gene expression. There may be other non-Smad pathways in activin signal transduction. These include the RhoA-ROCK-MEKK1-JNK and MEKK1-p38 pathways. In addition to activin, other ligands such as myostatin, nodal, and bone morphogenetic protein 7 (BMP-7) may also bind to ACVR2 and affect signal transduction. |
| Expression | Abundant expression in multiple tissues, including skeletal muscle, stomach, heart, endometrium, testes, prostate, ovary, and neural tissues. The cell surface level of ACVR2 and ACVR2B is regulated by proteins called ARIPs (activin receptor-interacting proteins). |
| Localisation | Cell surface, spanning cytoplasmic membrane. |
| Function | Activin signaling via its receptors has roles in cell proliferation, differentiation, apoptosis, metabolism, immune response, wound repair, and endocrine function. |
| Characterization of type II activin receptors. Binding, processing, and phosphorylation. |
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