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Primary Information | |
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| BoMiProt ID | Bomi227 |
| Protein Name | Actin-related protein 2 |
| Organism | Bos taurus |
| Uniprot ID | A7MB62 |
| Milk Fraction | Exosome |
| Ref Sequence ID | NP_001095683.1 |
| Aminoacid Length | 394 |
| Molecular Weight | 44761 |
| FASTA Sequence | Download |
| Gene Name | ACTR2 |
| Gene ID | 538486 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary 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 |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| SCOP | Class : Alpha and beta proteins (a/b) Fold : Ribonuclease H-like motif Superfamily : Actin-like ATPases Family : Actin/HSP70 Domain Name : 1K8K B:154-343 |
| CATH | Matched CATH superfamily 3.30.420.40 3.30.420.520 3.90.640.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| 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. |