Search by BoMiProt ID - Bomi227


Primary Information

BoMiProt ID Bomi227
Protein Name Actin-related protein 2
Organism Bos taurus
Uniprot IdA7MB62
Milk FractionExosome
Ref Sequence Id NP_001095683.1
Amino Acid Lenth 394
Molecular Weight 44761
Fasta Sequence https://www.uniprot.org/uniprot/A7MB62.fasta
Gene Name ACTR2
Gene Id 538486
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function stimulates formation of actin filaments at the leading edge of motile cells; hydrolyses ATP required for nucleation of filaments; concentrated at the leading edge of motile cells
Biochemical Properties structure of nucleotide-free bovine actin related ptotein(Arp)2/3 complex showed minimal contacts between Arp2 and Arp3 compared with the close association of adjacent subunits in the helical actin filament; Activation of the Arp2/3 involves the complex binding an existing filament and a nucleation-promoting factor, such as WASp or Scar, that brings along an actin monomer; interactions are thermodynamically coupled, In the presence of a nucleation promoting factor, actin monomer, and mother filament, Arp2 hydrolyzes ATP with a rate constant > 0.05 s^1; Arp3 binds ATP, but appreciable hydrolysis of the nucleotide by this subunit was not detected in either the active or inactive Arp2/3 complex
Significance in milk Cytoskeletal proteins; found increased during infection
PDB ID 1K8K, 1TYQ, 1U2V, 2P9I, 2P9K, 2P9L, 2P9N, 2P9P, 2P9S, 2P9U, 3DXK, 3DXM, 3RSE, 3UKR, 3UKU, 3ULE, 4JD2, 4XEI, 4XF2, 6dec,
Bibliography 1. Addis, M. F. et al. (2013) ‘Production and Release of Antimicrobial and Immune Defense Proteins by Mammary Epithelial Cells following Streptococcus uberis Infection of Sheep’, Infection and Immunity. Edited by A. J. Bäumler, 81(9), pp. 3182–3197. doi: 10.1128/IAI.00291-13.
2. Wang, Y., Ajtai, K. and Burghardt, T. P. (2018) ‘Cardiac and skeletal actin substrates uniquely tune cardiac myosin strain-dependent mechanics’, Open Biology, 8(11), p. 180143. doi: 10.1098/rsob.180143.
3. VANDEKERCKHOVE, J. and WEBER, K. (1979) ‘The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle’, Differentiation, 14(1–3), pp. 123–133. doi: 10.1111/j.1432-0436.1979.tb01021.x.
4. Crawford, K. et al. (2002) ‘Mice lacking skeletal muscle actin show reduced muscle strength and growth deficits and die during the neonatal period.’, Molecular and cellular biology, 22(16), pp. 5887–96. doi: 10.1128/mcb.22.16.5887-5896.2002.
5. Kumar, A. et al. (1997) ‘Rescue of cardiac -actin-deficient mice by enteric smooth muscle -actin’, Proceedings of the National Academy of Sciences, 94(9), pp. 4406–4411. doi: 10.1073/pnas.94.9.4406.