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Protein

Acyl-CoA-binding protein homolog

Gene

Dbi

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity). May be involved in energy metabolism in a manner that depends on the substrate used for energy production. Dbi and its metabolites are involved in the regulation of multiple biological processes.By similarity1 Publication

Sites

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

GO - Molecular functioni

  • fatty-acyl-CoA binding Source: FlyBase
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

  • cellular acyl-CoA homeostasis Source: FlyBase
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding protein homolog
Short name:
ACBP
Alternative name(s):
Diazepam-binding inhibitor homolog
Short name:
DBI
Gene namesi
Name:Dbi
ORF Names:CG8627
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0010387. Dbi.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8686Acyl-CoA-binding protein homologPRO_0000214010Add
BLAST

Proteomic databases

PaxDbiP42281.
PRIDEiP42281.

Expressioni

Tissue specificityi

Expressed in larval and pupal brains. In adults, expressed in cardia, part of the Malpighian tubules, fat body, and gametes of both sexes.1 Publication

Developmental stagei

Expressed from the larval stage onwards throughout the adult stage.1 Publication

Gene expression databases

BgeeiP42281.
GenevisibleiP42281. DM.

Interactioni

Protein-protein interaction databases

IntActiP42281. 1 interaction.
STRINGi7227.FBpp0076624.

Structurei

3D structure databases

ProteinModelPortaliP42281.
SMRiP42281. Positions 6-86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8685ACBPROSITE-ProRule annotationAdd
BLAST

Region

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

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.
InParanoidiP42281.
OMAiDTAKPGL.
OrthoDBiEOG7SN8G8.
PhylomeDBiP42281.

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.

P42281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSEQFNAAA EKVKSLTKRP SDDEFLQLYA LFKQASVGDN DTAKPGLLDL
60 70 80
KGKAKWEAWN KQKGKSSEAA QQEYITFVEG LVAKYA
Length:86
Mass (Da):9,557
Last modified:November 1, 1995 - v1
Checksum:i623986B5566228E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551K → S in CAA53268 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04822 Genomic DNA. Translation: AAA21649.1.
U04823 mRNA. Translation: AAA21650.1.
X75596 mRNA. Translation: CAA53268.1.
AE014296 Genomic DNA. Translation: AAF50607.1.
AE014296 Genomic DNA. Translation: AAN12074.1.
AY070704 mRNA. Translation: AAL48175.1.
PIRiA56041.
S38574.
RefSeqiNP_523952.2. NM_079228.3.
NP_729218.1. NM_168192.3.
UniGeneiDm.20425.

Genome annotation databases

EnsemblMetazoaiFBtr0076915; FBpp0076624; FBgn0010387.
FBtr0076916; FBpp0076625; FBgn0010387.
GeneIDi38784.
KEGGidme:Dmel_CG8627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04822 Genomic DNA. Translation: AAA21649.1.
U04823 mRNA. Translation: AAA21650.1.
X75596 mRNA. Translation: CAA53268.1.
AE014296 Genomic DNA. Translation: AAF50607.1.
AE014296 Genomic DNA. Translation: AAN12074.1.
AY070704 mRNA. Translation: AAL48175.1.
PIRiA56041.
S38574.
RefSeqiNP_523952.2. NM_079228.3.
NP_729218.1. NM_168192.3.
UniGeneiDm.20425.

3D structure databases

ProteinModelPortaliP42281.
SMRiP42281. Positions 6-86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42281. 1 interaction.
STRINGi7227.FBpp0076624.

Proteomic databases

PaxDbiP42281.
PRIDEiP42281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076915; FBpp0076624; FBgn0010387.
FBtr0076916; FBpp0076625; FBgn0010387.
GeneIDi38784.
KEGGidme:Dmel_CG8627.

Organism-specific databases

CTDi1622.
FlyBaseiFBgn0010387. Dbi.

Phylogenomic databases

eggNOGiKOG0817. Eukaryota.
COG4281. LUCA.
GeneTreeiENSGT00840000129776.
InParanoidiP42281.
OMAiDTAKPGL.
OrthoDBiEOG7SN8G8.
PhylomeDBiP42281.

Miscellaneous databases

ChiTaRSiDbi. fly.
GenomeRNAii38784.
PROiP42281.

Gene expression databases

BgeeiP42281.
GenevisibleiP42281. DM.

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. "Tissue-specific expression of the diazepam-binding inhibitor in Drosophila melanogaster: cloning, structure, and localization of the gene."
    Kolmer M., Roos C., Tirronen M., Myoehaenen S., Alho H.
    Mol. Cell. Biol. 14:6983-6995(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
  2. "Diazepam binding inhibitor/endozepine/acyl-CoA-binding homologue from Drosophila melanogaster."
    Lagueux M., Bulet P., Hetru C.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiACBP_DROME
AccessioniPrimary (citable) accession number: P42281
Secondary accession number(s): A4V1K8, Q9VS23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.