SMART: Pfam domain ACBP

The domain within your query sequence starts at position 4 and ends at position 88; the E-value for the ACBP domain shown below is 2.2e-33.

SQQDFENALNQVKLLKKDPGNEVKLRLYALYKQATEGPCNMPKPGMLDFVNKAKWDAWNA
LGSLPKETARQNYVDLVSSLSSSSE

ACBP

PFAM accession number:	PF00887
Interpro abstract (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 [ (PUBMED:1454809) ]. 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 [ (PUBMED:1649940) ]. 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 [ (PUBMED:16018771) ]. 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 ) [ (PUBMED:16018771) ]. The ACB domain consists of four alpha-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 [ (PUBMED:11491287) ]. Other proteins containing an ACB domain include: Endozepine-like peptide (ELP) (gene DBIL5) from mouse [ (PUBMED:8898349) ]. 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 [ (PUBMED:10354522) ], a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain.
GO function:	fatty-acyl-CoA binding (GO:0000062)

PFAM accession number:

PF00887

Interpro abstract (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 [ (PUBMED:1454809) ]. 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 [ (PUBMED:1649940) ].

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 [ (PUBMED:16018771) ].

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 ) [ (PUBMED:16018771) ].

The ACB domain consists of four alpha-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 [ (PUBMED:11491287) ].

Other proteins containing an ACB domain include:

Endozepine-like peptide (ELP) (gene DBIL5) from mouse [ (PUBMED:8898349) ]. 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 [ (PUBMED:10354522) ], a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain.

GO function:

fatty-acyl-CoA binding (GO:0000062)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ACBP