Search by BoMiProt ID - Bomi3332


Primary Information

BoMiProt ID Bomi3332
Protein Name Actin, alpha cardiac muscle 1
Organism Bos taurus
Uniprot IdQ3ZC07
Milk FractionWhey
Ref Sequence Id NP_001029757.1
Amino Acid Lenth 377
Molecular Weight 42019
Fasta Sequence https://www.uniprot.org/uniprot/Q3ZC07.fasta
Gene Name ACTC1
Gene Id 533219
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondry 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
Linking IDs Bomi20
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.