Search by BoMiProt ID - Bomi18


Primary Information

BoMiProt ID Bomi18
Protein Name Actin, cytoplasmic 1
Organism Bos taurus
Uniprot IDP60712
Milk FractionWhey
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.