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Protein

Acyl-CoA-binding protein

Gene

DBI

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141Acyl-CoA
Binding sitei51 – 511Acyl-CoA
Binding sitei55 – 551Acyl-CoA
Binding sitei74 – 741Acyl-CoA

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding protein
Short name:
ACBP
Alternative name(s):
Diazepam-binding inhibitor
Short name:
DBI
Endozepine
Short name:
EP
Gene namesi
Name:DBI
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 8786Acyl-CoA-binding proteinPRO_0000214001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei8 – 81N6-acetyllysine; alternateBy similarity
Modified residuei8 – 81N6-succinyllysine; alternateBy similarity
Modified residuei17 – 171N6-succinyllysineBy similarity
Modified residuei19 – 191N6-acetyllysineBy similarity
Modified residuei29 – 291PhosphotyrosineBy similarity
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
Modified residuei55 – 551N6-malonyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
Modified residuei77 – 771N6-acetyllysine; alternateBy similarity
Modified residuei77 – 771N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07107.
PeptideAtlasiP07107.
PRIDEiP07107.

PTM databases

iPTMnetiP07107.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012523.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi13 – 153Combined sources
Beta strandi16 – 183Combined sources
Helixi22 – 3615Combined sources
Helixi50 – 6112Combined sources
Turni62 – 643Combined sources
Helixi67 – 8519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACANMR-A2-87[»]
1HB6X-ray2.00A2-87[»]
1HB8X-ray2.00A/B/C2-87[»]
1NTINMR-A2-87[»]
1NVLNMR-A2-87[»]
2ABDNMR-A2-87[»]
ProteinModelPortaliP07107.
SMRiP07107. Positions 2-87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8786ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 335Acyl-CoA binding

Sequence similaritiesi

Belongs to the ACBP family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0817. Eukaryota.
COG4281. LUCA.
GeneTreeiENSGT00840000129776.
HOGENOMiHOG000261845.
HOVERGENiHBG000398.
InParanoidiP07107.
KOiK08762.
OMAiRYKFEAW.
OrthoDBiEOG7SN8G8.
TreeFamiTF335802.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAEFDKAA EEVKHLKTKP ADEEMLFIYS HYKQATVGDI NTERPGMLDF
60 70 80
KGKAKWDAWN ELKGTSKEDA MKAYIDKVEE LKKKYGI
Length:87
Mass (Da):10,044
Last modified:January 23, 2007 - v2
Checksum:iB2922635F18CA0D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15886 mRNA. Translation: AAA30495.1.
BC114181 mRNA. Translation: AAI14182.1.
PIRiA26448. NZBO.
RefSeqiNP_001106792.1. NM_001113321.1.
UniGeneiBt.46917.

Genome annotation databases

EnsembliENSBTAT00000012523; ENSBTAP00000012523; ENSBTAG00000009517.
GeneIDi768330.
KEGGibta:768330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15886 mRNA. Translation: AAA30495.1.
BC114181 mRNA. Translation: AAI14182.1.
PIRiA26448. NZBO.
RefSeqiNP_001106792.1. NM_001113321.1.
UniGeneiBt.46917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACANMR-A2-87[»]
1HB6X-ray2.00A2-87[»]
1HB8X-ray2.00A/B/C2-87[»]
1NTINMR-A2-87[»]
1NVLNMR-A2-87[»]
2ABDNMR-A2-87[»]
ProteinModelPortaliP07107.
SMRiP07107. Positions 2-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012523.

PTM databases

iPTMnetiP07107.

Proteomic databases

PaxDbiP07107.
PeptideAtlasiP07107.
PRIDEiP07107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000012523; ENSBTAP00000012523; ENSBTAG00000009517.
GeneIDi768330.
KEGGibta:768330.

Organism-specific databases

CTDi1622.

Phylogenomic databases

eggNOGiKOG0817. Eukaryota.
COG4281. LUCA.
GeneTreeiENSGT00840000129776.
HOGENOMiHOG000261845.
HOVERGENiHBG000398.
InParanoidiP07107.
KOiK08762.
OMAiRYKFEAW.
OrthoDBiEOG7SN8G8.
TreeFamiTF335802.

Miscellaneous databases

EvolutionaryTraceiP07107.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand."
    Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J., Lee D.C.
    DNA 6:71-79(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor."
    Marquardt H., Todaro G.J., Shoyab M.
    J. Biol. Chem. 261:9727-9731(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-87, ACETYLATION AT SER-2.
    Tissue: Brain.
  4. "Amino acid sequence of acyl-CoA-binding protein from cow liver."
    Mikkelsen J., Hoejrup P., Nielsen P.F., Roepstorff P., Knudsen J.
    Biochem. J. 245:857-861(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-87.
    Tissue: Liver.
  5. "Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver."
    Jensen M.S., Hoejrup P., Rasmussen J.T., Knudsen J.
    Biochem. J. 284:809-812(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-87.
    Tissue: Liver.
  6. "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells."
    Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.
    Biochem. J. 410:463-472(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The secondary structure in solution of acyl-coenzyme A binding protein from bovine liver using 1H nuclear magnetic resonance spectroscopy."
    Andersen K.V., Ludvigsen S., Mandrup S., Knudsen J., Poulsen F.M.
    Biochemistry 30:10654-10663(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  8. "Three-dimensional structure in solution of acyl-coenzyme A binding protein from bovine liver."
    Andersen K.V., Poulsen F.M.
    J. Mol. Biol. 226:1131-1141(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy."
    Andersen K.V., Poulsen F.M.
    J. Biomol. NMR 3:271-284(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A."
    Kragelund B.B., Andersen K.V., Madsen J.C., Knudsen J., Poulsen F.M.
    J. Mol. Biol. 230:1260-1277(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH THE ACYL-COA ANALOG COENZYME A AND PALMITIC ACID.
  11. "Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein."
    van Aalten D.M., Milne K.G., Zou J.Y., Kleywegt G.J., Bergfors T., Ferguson M.A., Knudsen J., Jones T.A.
    J. Mol. Biol. 309:181-192(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION.
  12. "RDC-refined NMR structure of bovine acyl-coenzyme A binding protein, ACBP, in complex with palmitoyl-coenzyme A."
    Lerche M.H., Kragelund B.B., Redfield C., Poulsen F.M.
    Submitted (FEB-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH THE ACYL-COA PALMITOYL-COENZYME A.

Entry informationi

Entry nameiACBP_BOVIN
AccessioniPrimary (citable) accession number: P07107
Secondary accession number(s): Q29RG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.