Search by BoMiProt ID - Bomi207


Primary Information

BoMiProt ID Bomi207
Protein Name Acyl-CoA-binding protein
Organism Bos taurus
Uniprot IdP07107
Milk FractionExosome
Ref Sequence Id NP_001106792.1
Amino Acid Lenth 87
Molecular Weight 10044
Fasta Sequence https://www.uniprot.org/uniprot/P07107.fasta
Gene Name DBI
Gene Id 768330
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

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.