Acyl-CoA-binding protein (DBI)
The protein contains 87 amino acids for an estimated molecular weight of 10044 Da.
Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able 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. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs8192504 | |
| dbSNP:rs8192506 | |
| dbSNP:rs8192507 |
Biological Process
Acyl-CoA metabolic process
Behavioral fear response
Hair follicle development
Lateral ventricle development
Learning or memory
Long-term synaptic potentiation
Negative regulation of protein lipidation
Phosphatidylcholine acyl-chain remodeling
Positive regulation of CoA-transferase activity
Positive regulation of phospholipid transport
Transport
Triglyceride metabolic process
The reference OMIM entry for this protein is 125950
Diazepam binding inhibitor; dbi
Acyl-coa binding protein; acbp
Cholecystokinin-releasing peptide, trypsin-sensitive
DESCRIPTION
Benzodiazepines modulate signal transduction at type A GABA (gamma-aminobutyric acid) receptors (137160) located in brain synapses. GABA is the predominant inhibitory neurotransmitter of the mammalian central nervous system. This receptor binds GABA, beta-carbolines, and benzodiazepines with high affinity and a chloride ion channel. Benzodiazepines prolong the chloride ion channel opening burst elicited by GABA and thereby enhance GABA-mediated inhibitory responses. This facilitation plays a role in reducing pathologic anxiety. An endogenous ligand has been identified that is recognized by the beta-carboline/benzodiazepine recognition site located in the GABA receptor. This ligand, diazepam binding inhibitor (DBI), is a protein of about 11 kD that displaces beta-carbolines and benzodiazepines bound to brain membrane fractions in vitro. DBI or a derivative small neuropeptide is thought to downregulate the effects of GABA (summary by Gray et al., 1986).CLONING
Gray et al. (1986) isolated a cDNA clone that encodes human DBI. A polypeptide related to DBI, with similar binding activity to diazepam, has been isolated from human and bovine brain. This protein, called endozepine, contains 86 amino residues. Webb et al. (1987) cloned endozepine cDNAs from bovine and human libraries and found 93% homology in the coding regions of the bovine and human forms. The message is 650 nucleotides long. Northern analysis using the cloned cDNA demonstrated that the message is expressed in heart, liver, and spleen, in addition to brain. Diazepam binding inhibitor is also known as acyl-CoA-binding protein (ACBP). Rose et al. (1992) cloned the homologous gene from the budding yeast Saccharomyces cerevisiae. The yeast gene contains no introns and encodes a polypeptide of 87 amino acids (including the initiating methionine), identical in length to the human gene product with 48% conservation of amino acid residues. The most highly conserved domain comprises 7 contiguous residues that are identical in all known protein species from yeast, birds, and mammals. This domain constitutes the hydrophobic binding site for acyl-CoA esters and is located within the second helical region of the molecule. The presence of a highly conserved gene in a primitive organism such as yeast supports its basic biologic role as an acyl-CoA-binding protein and suggests that many of the biologic functions attributed to it in higher organisms may result from its ability to interact with acyl-CoA. Rose et al. (1992) designated the yeast gene ACB, for acyl-CoA binding.GENE FUNCTION
Benzodiazepine receptors unassociated with the GABA receptor complex, and distinct from those seen in association with the central nervous system, have been identified in peripheral tissues. Anholt et al. (1986) presented evidence that these peripheral receptors are localized on the mitochondrial outer membrane. Webb et al. (1987) speculated that the role of endozepine in peripheral tissues is to interact with this receptor. Herzig et al. (1996) isolated a trypsin-sensitive cholecystokinin (CCK; 118440)-releasing peptide (CCK-RP) from porcine and rat intestinal mucosa. At the same time, Spannagel et al. (1996) purified a luminal CCK-releasing factor from rat intestinal secretions. Herzig et al. (1996) found that the amino acid sequence of CCK-RP was identical to that of diazepam-binding inhibitor. Li et al. (2000) demonstrated that DBI mediates the feedback regulatio ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for DBI
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 125950 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed