PR00689

ACOABINDINGP

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameACOABINDINGP

Description
Imported from IPR000582

Acyl-CoA-binding protein (ACBP) is a small (10 Kd) protein that binds medium-and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters
[1]
. ACBP is also known as diazepam binding inhibitor (DBI) or endozepine (EP) because of its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor
[2]
.

ACBP is a highly conserved protein of about 90 residues that is found in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and in some eubacterial species
[3]
.

Although ACBP occurs as a completely independent protein, intact ACB domains have been identified in a number of large, multifunctional proteins in a variety of eukaryotic species. These include large membrane-associated proteins with N-terminal ACB domains, multifunctional enzymes with both ACB and peroxisomal enoyl-CoA Delta(3), Delta(2)-enoyl-CoA isomerase domains, and proteins with both an ACB domain and ankyrin repeats (
IPR002110
)
[3]
.

The ACB domain consists of four α-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. The ligand is bound through specific interactions with residues on the protein, most notably several conserved positive charges that interact with the phosphate group on the adenosine-3'phosphate moiety, and the acyl chain is sandwiched between the hydrophobic surfaces of CoA and the protein
[4]
.

Other proteins containing an ACB domain include:


 * Endozepine-like peptide (ELP) (gene DBIL5) from mouse
[5]
. ELP is a testis-specific ACBP homologue that may be involved in the energy metabolism of the mature sperm.
 * MA-DBI, a transmembrane protein of unknown function which has been found in mammals. MA-DBI contains a N-terminal ACB domain.
 * DRS-1
[6]
, a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain.

References
Imported from IPR000582

1.Molecular cloning of the gene for the yeast homolog (ACB) of diazepam binding inhibitor/endozepine/acyl-CoA-binding protein. Rose TM, Schultz ER, Todaro GJ. Proc. Natl. Acad. Sci. U.S.A. 89, 11287-91, (1992). View articlePMID: 1454809

2.Diazepam binding inhibitor (DBI): a peptide with multiple biological actions. Costa E, Guidotti A. Life Sci. 49, 325-44, (1991). View articlePMID: 1649940

3.Evolution of the acyl-CoA binding protein (ACBP). Burton M, Rose TM, Faergeman NJ, Knudsen J. Biochem. J. 392, 299-307, (2005). View articlePMID: 16018771

4.Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. J. Mol. Biol. 309, 181-92, (2001). View articlePMID: 11491287

5.A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells. Pusch W, Balvers M, Hunt N, Ivell R. Mol. Cell. Endocrinol. 122, 69-80, (1996). View articlePMID: 8898349

6.Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor. Suk K, Kim YH, Hwang DY, Ihm SH, Yoo HJ, Lee MS. Biochim. Biophys. Acta 1454, 126-31, (1999). View articlePMID: 10354522

Supplementary References

1. Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor. Marquardt H, Todaro GJ, Shoyab M. J. Biol. Chem. 261, 9727-31, (1986). View articlePMID: 3525533

2. Three-dimensional structure in solution of acyl-coenzyme A binding protein from bovine liver. Andersen KV, Poulsen FM. J. Mol. Biol. 226, 1131-41, (1992). View articlePMID: 1518047

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