Primary Information | |
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BoMiProt ID | Bomi18 |
Protein Name | Actin, cytoplasmic 1 |
Organism | Bos taurus |
Uniprot ID | P60712 |
Milk Fraction | Whey |
Ref Sequence ID | NP_776404.2 |
Aminoacid Length | 375 |
Molecular Weight | 41737 |
FASTA Sequence | Download |
Gene Name | ACTB |
Gene ID | 280979 |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Protein Function | essential in cell division, migration, junction formation, chromatin remodeling, transcriptional regulation, vesicle trafficking, and cell shape regulation; Four isoforms, αskeletal-actin, αcardiac-actin, αsmooth-actin, and ɣ smooth-actin, are expressed primarily in skeletal, cardiac, and smooth muscle; two isoforms, bcyto-actin and ccyto-actin are ubiquitously expressed; |
Biochemical Properties | ßcyto-Actin and ɣcytoactin, which are exactly conserved from birds to mammals, only differ by four biochemically similar residues found in the 10 N-terminal residues; as found in mice sensory hair cells in the inner ear depend on stereocilia formed of bcyto-actin and ccyto-actin for proper function; |
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 : 2OAN C:4-371 |
CATH | Matched CATH superfamily 3.30.420.40 3.90.640.10 |
Predicted Disorder Regions | NA |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
PDB ID | 1HLU, 2BTF, 2OAN, 3U4L, 3UB5, 7PDZ, |
Linking IDs | |
Bibliography | 1. Belyantseva, I. A., Perrin, B. J., Sonnemann, K. J., Zhu, M., Stepanyan, R., McGee, J., … Ervasti, J. M. (2009). γ-Actin is required for cytoskeletal maintenance but not development. Proceedings of the National Academy of Sciences of the United States of America, 106(24), 9703–9708. https://doi.org/10.1073/pnas.0900221106. 2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021. 2. VANDEKERCKHOVE, J., & WEBER, K. (1979). The Complete Amino Acid Sequence of Actins from Bovine Aorta, Bovine Heart, Bovine Fast Skeletal Muscle, and Rabbit, Slow Skeletal Muscle: A Protein-Chemical Analysis of Muscle Actin Differentiation. Differentiation, 14(1–3), 123–133. https://doi.org/10.1111/j.1432-0436.1979.tb01021. 3. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13. |