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 https://www.uniprot.org/uniprot/Q95126.fasta
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,
Phosphorylation
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. https://doi.org/10.1093/emboj/cdg156.
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. https://doi.org/10.1074/jbc.M110.114959.
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. https://doi.org/10.3389/fphys.2018.00515.
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. https://doi.org/10.1210/endo.138.6.5173.
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. https://doi.org/10.3168/jds.jds.2009-2981. 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.