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P31786 (ACBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length87 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Monomer.

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Note: Golgi localization is dependent on ligand binding By similarity.

Sequence similarities

Belongs to the ACBP family.

Contains 1 ACB (acyl-CoA-binding) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 8786Acyl-CoA-binding protein
PRO_0000214005

Regions

Domain2 – 8786ACB
Region29 – 335Acyl-CoA binding By similarity

Sites

Binding site141Acyl-CoA By similarity
Binding site511Acyl-CoA By similarity
Binding site551Acyl-CoA By similarity
Binding site741Acyl-CoA By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue81N6-acetyllysine By similarity
Modified residue291Phosphotyrosine Ref.7
Modified residue551N6-acetyllysine; alternate Probable
Modified residue551N6-malonyllysine; alternate By similarity
Modified residue771N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P31786 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 86F725C998785675

FASTA8710,000
        10         20         30         40         50         60 
MSQAEFDKAA EEVKRLKTQP TDEEMLFIYS HFKQATVGDV NTDRPGLLDL KGKAKWDSWN 

        70         80 
KLKGTSKESA MKTYVEKVDE LKKKYGI

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of the murine diazepam binding inhibitor."
Owens G.P., Sinha A.K., Sikela J.M., Hahn W.E.
Brain Res. Mol. Brain Res. 6:101-108(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A collection of cDNA clones with specific expression patterns in mouse brain."
Kato K.
Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c.
Tissue: Brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 34-51, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X61431 mRNA. Translation: CAA43673.1.
AK018720 mRNA. Translation: BAB31366.1.
AK027906 mRNA. Translation: BAC25658.1.
BC028874 mRNA. Translation: AAH28874.1.
IPIIPI00667117.
PIRA60059.
RefSeqNP_031856.1. NM_007830.4.
UniGeneMm.2785.

3D structure databases

ProteinModelPortalP31786.
SMRP31786. Positions 2-87.
ModBaseSearch...

PTM databases

PhosphoSiteP31786.

2D gel databases

SWISS-2DPAGEP31786.

Proteomic databases

PaxDbP31786.
PRIDEP31786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027634; ENSMUSP00000027634; ENSMUSG00000026385.
GeneID13167.
KEGGmmu:13167.

Organism-specific databases

CTD1622.
MGIMGI:94865. Dbi.

Phylogenomic databases

eggNOGCOG4281.
HOGENOMHOG000261845.
HOVERGENHBG000398.
KOK08762.
OrthoDBEOG4GF3GS.

Gene expression databases

ArrayExpressP31786.
BgeeP31786.
CleanExMM_DBI.
GenevestigatorP31786.
GermOnlineENSMUSG00000026385. Mus musculus.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
InterProIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
SUPFAMSSF47027. ACBP. 1 hit.
PROSITEPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDBI. mouse.
NextBio283250.
SOURCESearch...

Entry information

Entry nameACBP_MOUSE
AccessionPrimary (citable) accession number: P31786
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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