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Primary Information | |
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| BoMiProt ID | Bomi3332 |
| Protein Name | Actin, alpha cardiac muscle 1 |
| Organism | Bos taurus |
| Uniprot ID | Q3ZC07 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_001029757.1 |
| Aminoacid Length | 377 |
| Molecular Weight | 42019 |
| FASTA Sequence | Download |
| Gene Name | ACTC1 |
| Gene ID | 533219 |
| Protein Existence Status | Reveiwed:Experimental evidence at transcript 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 |
| 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. |
| PTMs | N-Acetylation Cyst, N6-Methylation at Lys, Oxidation |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization.Monomethylation at Lys-86 (K86me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.Methylated at His-75 by SETD3. |