P42281 (ACBP_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	Dbi
ORF Names:	CG8627

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	86 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 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. Ref.1
Tissue specificity	Expressed in larval and pupal brains. In adults, expressed in cardia, part of the Malpighian tubules, fat body, and gametes of both sexes. Ref.1
Developmental stage	Expressed from the larval stage onwards throughout the adult stage. Ref.1
Sequence similarities	Belongs to the ACBP family. Contains 1 ACB (acyl-CoA-binding) domain.

Ontologies

Keywords
Biological process	Transport
Ligand	Lipid-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular acyl-CoA homeostasis Inferred from sequence or structural similarity Ref.1. Source: FlyBase transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	fatty-acyl-CoA binding Inferred from sequence or structural similarity Ref.1. Source: FlyBase 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
	Chain	1 – 86	86	Acyl-CoA-binding protein homolog		PRO_0000214010
Regions
	Domain	2 – 86	85	ACB
	Region	29 – 33	5	Acyl-CoA binding By similarity
Sites
	Binding site	14	1	Acyl-CoA By similarity
	Binding site	51	1	Acyl-CoA By similarity
	Binding site	55	1	Acyl-CoA By similarity
	Binding site	74	1	Acyl-CoA By similarity
Experimental info
	Sequence conflict	55	1	K → S in CAA53268. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P42281 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 623986B5566228E1	FASTA	86	9,557
	10 20 30 40 50 60 MVSEQFNAAA EKVKSLTKRP SDDEFLQLYA LFKQASVGDN DTAKPGLLDL KGKAKWEAWN 70 80 KQKGKSSEAA QQEYITFVEG LVAKYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A56041. S38574.
RefSeq	NP_523952.2. NM_079228.3. NP_729218.1. NM_168192.3.
UniGene	Dm.20425.
3D structure databases
ProteinModelPortal	P42281.
SMR	P42281. Positions 6-86.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42281. 1 interaction.
STRING	7227.FBpp0076625.
Proteomic databases
PaxDb	P42281.
PRIDE	P42281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076915; FBpp0076624; FBgn0010387. FBtr0076916; FBpp0076625; FBgn0010387.
GeneID	38784.
KEGG	dme:Dmel_CG8627.
Organism-specific databases
CTD	1622.
FlyBase	FBgn0010387. Dbi.
Phylogenomic databases
eggNOG	COG4281.
GeneTree	ENSGT00680000099745.
InParanoid	P42281.
OMA	GDNTTDK.
OrthoDB	EOG42549C.
PhylomeDB	P42281.
Gene expression databases
Bgee	P42281.
GermOnline	CG8627. Drosophila melanogaster.
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
ChiTaRS	DBI. drosophila.
GenomeRNAi	38784.
NextBio	810361.

Entry information

Entry name

ACBP_DROME

Accession

Primary (citable) accession number: P42281
Secondary accession number(s): A4V1K8, Q9VS23

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project