Primary Information |
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| BoMiProt ID | Bomi75 |
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| Protein Name | Acyl-CoA synthetase long-chain family member 1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q0VCZ8 |
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| Milk Fraction | MFGM, Exosome |
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| Ref Sequence ID | NP_001069553.1 |
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| Aminoacid Length | 699 |
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| Molecular Weight | 78281 |
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| FASTA Sequence |
Download |
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| Gene Name | ACSL1 |
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| Gene ID | 537161 |
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| Protein Existence Status | Unreviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | activate the major long-chain fatty acids (FAs) of 16–22 carbons; regulate transcription by modulating the intracellular content of FA
and acyl-CoA; required for complex lipid synthesis in rapidly growing cells; necessary for fatty acid degradation, phospholipid remodeling, and the production of long acyl-CoA esters that regulate many physiological processes |
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| Biochemical Properties | membrane-bound enzymes act on non-polar hydrophobic substrates; as extracted from bovine mammary galnd, purified
fatty acid synthetase has a specific activity of 875 _+ 82 (S.E.) units/mg; At 4 ºC, the isolated enzyme was unstable in a 0.25 M potassium
phosphate buffer (pH 7.0) 10^-3 M with EDTA and dithiothreitol, but stable in the
same buffer at - 95 ºC for at least 2 months; the enzyme was therefore stored at
-95ºC; enzyme activity
was found to be highly dependent on the presence of NADPH.; |
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| Significance in milk | synthesized both long and
short chain fatty acids present in milk |
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| PTMs | As found in liver and brown
adipose tissue of mice, universal Nterminal acetylation, 15 acetylated lysines, and 25 phosphorylation sites on ACSL1 was identified |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Significance of PTMs | ACSL1 directs its acyl-CoA product towards both
triacylglycerol synthesis and β-oxidation in liver, but only towards β-oxidation in
adipocytes and heart , it is likely that some of the modifications, rather than altering
enzyme activity, might affect ACSL1 protein stability or protein-protein interactions |
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| Linking IDs | |
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| Bibliography | 1. Frahm, J. L., Li, L. O., Grevengoed, T. J., & Coleman, R. A. (2011). Phosphorylation and Acetylation of Acyl-Coa Synthetase-I. Journal of Proteomics and Bioinformatics, 4(7), 129–137. https://doi.org/10.4172/jpb.1000180.
2. Knudsen, J. (1972). Fatty acid synthetase from cow mammary gland tissue cells. Biochimica et Biophysica Acta, 280(3), 408–414. https://doi.org/10.1016/0005-2760(72)90246-9.
3. Soupene, E., Dinh, N. P., Siliakus, M., & Kuypers, F. A. (2010). Activity of the acyl-CoA synthetase ACSL6 isoforms: role of the fatty acid Gate-domains. BMC Biochemistry, 11, 18. https://doi.org/10.1186/1471-2091-11-18.
4. Watkins, P. A., Maiguel, D., Jia, Z., & Pevsner, J. (2007). Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. Journal of Lipid Research, 48(12), 2736–2750. https://doi.org/10.1194/jlr.M700378-JLR200. |
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