Acyl-CoA-binding protein - Bos taurus (Bovine)

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P07107 (ACBP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acyl-CoA-binding protein
Short name=ACBP

Alternative name(s):
Diazepam-binding inhibitor
Short name=DBI
Endozepine
Short name=EP

Gene names

Name:

DBI

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	87 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Subunit structure	Monomer.
Subcellular location	Endoplasmic reticulum. Golgi apparatus. Note: Golgi localization is dependent on ligand binding. Ref.6
Sequence similarities	Belongs to the ACBP family. Contains 1 ACB (acyl-CoA-binding) domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Endoplasmic reticulum Golgi apparatus
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	hair follicle development Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara transport Inferred from electronic annotation. Source: UniProtKB-KW triglyceride metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	fatty-acyl-CoA binding Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3 Ref.4 Ref.5

Chain

2 – 87

Acyl-CoA-binding protein

PRO_0000214001

Regions

Domain

2 – 87

ACB

Region

29 – 33

Acyl-CoA binding

Sites

Binding site

Acyl-CoA

Binding site

Acyl-CoA

Binding site

Acyl-CoA

Binding site

Acyl-CoA

Amino acid modifications

Modified residue

N-acetylserine Ref.3

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

N6-acetyllysine; alternate By similarity

Modified residue

N6-malonyllysine; alternate By similarity

Modified residue

N6-acetyllysine By similarity

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07107 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B2922635F18CA0D8
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FASTA

10,044

        10         20         30         40         50         60 
MSQAEFDKAA EEVKHLKTKP ADEEMLFIYS HYKQATVGDI NTERPGMLDF KGKAKWDAWN 

        70         80 
ELKGTSKEDA MKAYIDKVEE LKKKYGI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 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 PALMITOYL-COENZYME A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15886 mRNA. Translation: AAA30495.1.
BC114181 mRNA. Translation: AAI14182.1.

IPI

IPI00695419.

PIR

NZBO. A26448.

RefSeq

NP_001106792.1. NM_001113321.1.

UniGene

Bt.46917.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ACA	NMR	-	A	2-87	[»]
1HB6	X-ray	2.00	A	2-86	[»]
1HB8	X-ray	2.00	A/B/C	2-86	[»]
1NTI	NMR	-	A	2-86	[»]
1NVL	NMR	-	A	2-87	[»]
2ABD	NMR	-	A	2-87	[»]

ProteinModelPortal

P07107.

SMR

P07107. Positions 2-87.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000012523.

Proteomic databases

PaxDb

P07107.

PRIDE

P07107.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000012523; ENSBTAP00000012523; ENSBTAG00000009517.

GeneID

768330.

KEGG

bta:768330.

Organism-specific databases

CTD

1622.

Phylogenomic databases

eggNOG

COG4281.

GeneTree

ENSGT00680000099745.

HOGENOM

HOG000261845.

HOVERGEN

HBG000398.

InParanoid

P07107.

K08762.

OMA

CNTDKPG.

OrthoDB

EOG4GF3GS.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.

InterPro

IPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]

Pfam

PF00887. ACBP. 1 hit.
[Graphical view]

PRINTS

PR00689. ACOABINDINGP.

SUPFAM

SSF47027. ACBP. 1 hit.

PROSITE

PS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07107.

NextBio

20918588.

Entry information

Entry name

ACBP_BOVIN

Accession

Primary (citable) accession number: P07107
Secondary accession number(s): Q29RG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents