Search by BoMiProt ID - Bomi20


Primary Information

BoMiProt ID Bomi20
Protein Name Actin, aortic smooth muscle
Organism Bos taurus
Uniprot IdP62739
Milk FractionWhey
Ref Sequence Id NP_001029674.1
Aminoacid Length 377
Molecular Weight 42009
Fasta Sequence https://www.uniprot.org/uniprot/P62739.fasta
Gene Name ACTA2
Gene Id 515610
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; maintenance of the cytoskeleton, cell motility and muscle contraction
Biochemical Properties three components have different pIs; ratio of the three isoelectric species was calculated from a densitometric scan of the gel: α like 72%, ß-like 7%, and γ-like 21%; α like actin as the major smooth muscle actin in aorta tissue; both actin samples contained a small amount of the nonmuscle actins p and y with p expressed preferentially; actins from bovine and chicken aorta give an extremely similar ftngerprint pattern of their amino-terminal peptides labeled by C14-carboxymethylatio
Significance in milk Cytoskeletal proteins; found increased during infection
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Linking IDs Bomi3332
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.