Search by BoMiProt ID - Bomi46

Primary Information

BoMiProt ID Bomi46
Protein Name Activin receptor type-2B
Organism Bos taurus
Uniprot IDQ95126
Milk FractionExosome
Ref Sequence ID NP_776920.1
Aminoacid Length 512
Molecular Weight 57569
FASTA Sequence Download
Gene Name ACVR2B
Gene ID 282131
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function key regulators of skeletal muscle mass development; ActRIIB binds to a diverse group of TGF- family members, including activin A, BMP-2, BMP-7, GDF-8.  The AcvR2B pathway acts to regulate the muscle stem cell niche providing a more favorable environment for muscle regeneration.
Biochemical Properties single transmembrane domain serine/threonine kinase; primary sequence of ActRIIB extracellular domain is highly conserved; human ActRIIB ECD shares 99% sequence identity with mouse, rat, and bovine ActRIIB; ActRIIB also has a high affinity for myostatin (GDF-8) and the highly related ligand GDF-11; as found in mice The ActRIIB:activin A interface involves hydrophobic, charged and polar residues in both ActRIIB and activin A;
Significance in milk activin receptors were localized mostly in the cytoplasm of the luminal epithelial cells ;during gestation, they were present in both cytoplasm and nucleus of the epithelial cells and in the cytoplasm of the stromal cells
PTMs ActRIIB.Fc protein contains three potential N-glycosylation sites - two in the extracellular domain of ActRIIB and one in the Fc portion of the fusion molecule
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (138-160)
Additional Comments Disruption of ActRIIB expression leads to cardiac and kidney malformation, defects in axial patterning, and disturbance of left-right asymmetry in mice
Bibliography 1. Thompson, T. B., Woodruff, T. K., & Jardetzky, T. S. (2003). Structures of an ActRIIB:activin a complex reveal a novel binding mode for TGF-β ligand:receptor interactions. EMBO Journal, 22(7), 1555–1566.
2. Sako, D., Grinberg, A. V, Liu, J., Davies, M. V, Castonguay, R., Maniatis, S., … Kumar, R. (2010). Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIb. The Journal of Biological Chemistry, 285(27), 21037–21048.
3. Formicola, L., Pannérec, A., Correra, R. M., Gayraud-Morel, B., Ollitrault, D., Besson, V., … Sassoon, D. A. (2018). Inhibition of the Activin Receptor Type-2B Pathway Restores Regenerative Capacity in Satellite Cell-Depleted Skeletal Muscle. Frontiers in Physiology, 9, 515.
4. Ethier, J. F., Lussier, J. G., & Silversides, D. W. (1997). Bovine activin receptor type IIB messenger ribonucleic acid displays alternative splicing involving a sequence homologous to Src-homology 3 domain binding sites. Endocrinology, 138(6), 2425–2434.
5. Bloise, E., Cassali, G. D., Ferreira, M. C., Ciarmela, P., Petraglia, F., & Reis, F. M. (2010). Activin-related proteins in bovine mammary gland: localization and differential expression during gestational development and differentiation. Journal of Dairy Science, 93(10), 4592–4601. 6.Formicola L, Pannérec A, Correra RM, Gayraud-Morel B, Ollitrault D, Besson V, Tajbakhsh S, Lachey J, Seehra JS, Marazzi G, Sassoon DA. Inhibition of the Activin Receptor Type-2B Pathway Restores Regenerative Capacity in Satellite Cell-Depleted Skeletal Muscle. Front Physiol. 2018 May 24;9:515. doi: 10.3389/fphys.2018.00515. PMID: 29881353; PMCID: PMC5978452.