|Protein Name||Acyl-CoA-binding protein|
|Ref Sequence Id||NP_001106792.1|
|Amino Acid Lenth||87|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||mainly cytosolic, and the highest concentration is found in liver|
|Protein Function||potential role in acyl-CoA metabolism, the protein may have neurotransmitter activity; important role in intracellular acyl-CoA transport and pool formation and therefore also for the function of long chain acyl coA esters as metabolites and regulators of cellular functions; play a role in the sequestration, transport, and distribution of longchain acyl-CoAs in cells|
|Biochemical Properties||Bovine and rat liver acyl-CoA-binding proteins (ACBP) were found to exhibit a much higher affinity for long-chain acyl-CoA esters than both bovine hepatic and cardiac fatty-acid-binding proteins; bind acyl- CoA esters, but not fatty acids; bind saturated acyl-CoA esters with chain lengths from 8 to 18 carbon atoms with high affinity, but is unable to bind free fatty acids; FABP from bovine heart and liver exhibited much lower affinity for both [1-4C]hexadecanoyl-CoA and cis- 9-[1-14C]octadecenoyl-CoA than bovine and rat liver ACBP; bovine liver (l-ACBP) contains no cysteine; t-ACBP have now been isolated from three different species and all testes specific-ACBP contain three cysteine; The binding site is located in a hydrophobic groove on the surface of liver-ACBP; l-ACBP does not bind fatty acids, acyl carnitines, cholesterol and a number of nucleotides; the binding affinities decrease with increasing ionic strength of the buffer|
|Significance in milk||involved in acetate and FA activation and intracellular transport in mammary gland|
|PDB ID||1ACA, 1HB6, 1HB8, 1NTI, 1NVL, 2ABD,|
|Bibliography||1. Rosendal, J., Ertbjerg, P., & Knudsen, J. (1993). Characterization of ligand binding to acyl-CoA-binding protein. The Biochemical Journal, 290 ( Pt 2), 321–326. https://doi.org/10.1042/bj2900321. |
2. Shang, X., He, Y., Zhang, L., Chen, B., He, C. J., Cheng, H. H., & Zhou, R. J. (2006). Molecular cloning of the rice field Eel Nup93 with predominant expression in gonad and kidney. Acta Genetica Sinica, 33(1), 41–48. https://doi.org/10.1016/S0379-4172(06)60006-1.
3. Soupene, E., Serikov, V., & Kuypers, F. A. (2008). Characterization of an acyl-coenzyme A binding protein predominantly expressed in human primitive progenitor cells. Journal of Lipid Research, 49(5), 1103–1112. https://doi.org/10.1194/jlr.M800007-JLR200.
4. Bionaz, M., & Loor, J. J. (2008). Gene networks driving bovine milk fat synthesis.pdf. BioMed Central, 9, 366. https://doi.org/doi:10.1186/1471-2164-9-366.
5. Rasmussen, J. T., Börchers, T., & Knudsen, J. (1990). Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters. The Biochemical Journal, 265(3), 849–855. https://doi.org/10.1042/bj2650849.
6. Whetstone, H. D., Hurley, W. L., & Davis, C. L. (1986). Identification and characterization of a fatty acid binding protein in bovine mammary gland. Comparative Biochemistry and Physiology. B, Comparative Biochemistry, 85(3), 687–692. https://doi.org/10.1016/0305-0491(86)90068-4.
7. Mikkelsen, J., & Knudsen, J. (1987). Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution. The Biochemical Journal, 248(3), 709–714. https://doi.org/10.1042/bj2480709.