ACBP_DROME
ID ACBP_DROME Reviewed; 86 AA.
AC P42281; A4V1K8; Q9VS23;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Acyl-CoA-binding protein homolog;
DE Short=ACBP;
DE AltName: Full=Diazepam-binding inhibitor homolog;
DE Short=DBI;
GN Name=Acbp2 {ECO:0000312|FlyBase:FBgn0010387};
GN Synonyms=Dbi {ECO:0000303|PubMed:7935415};
GN ORFNames=CG8627 {ECO:0000312|FlyBase:FBgn0010387};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=7935415; DOI=10.1128/mcb.14.10.6983-6995.1994;
RA Kolmer M., Roos C., Tirronen M., Myoehaenen S., Alho H.;
RT "Tissue-specific expression of the diazepam-binding inhibitor in Drosophila
RT melanogaster: cloning, structure, and localization of the gene.";
RL Mol. Cell. Biol. 14:6983-6995(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RA Lagueux M., Bulet P., Hetru C.;
RT "Diazepam binding inhibitor/endozepine/acyl-CoA-binding homologue from
RT Drosophila melanogaster.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity and may function as an intracellular carrier of acyl-CoA
CC esters (By similarity). May be involved in energy metabolism in a
CC manner that depends on the substrate used for energy production. Dbi
CC and its metabolites are involved in the regulation of multiple
CC biological processes. {ECO:0000250, ECO:0000269|PubMed:7935415}.
CC -!- TISSUE SPECIFICITY: Expressed in larval and pupal brains. In adults,
CC expressed in cardia, part of the Malpighian tubules, fat body, and
CC gametes of both sexes. {ECO:0000269|PubMed:7935415}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the larval stage onwards throughout
CC the adult stage. {ECO:0000269|PubMed:7935415}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; U04822; AAA21649.1; -; Genomic_DNA.
DR EMBL; U04823; AAA21650.1; -; mRNA.
DR EMBL; X75596; CAA53268.1; -; mRNA.
DR EMBL; AE014296; AAF50607.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12074.1; -; Genomic_DNA.
DR EMBL; AY070704; AAL48175.1; -; mRNA.
DR PIR; A56041; A56041.
DR PIR; S38574; S38574.
DR RefSeq; NP_523952.2; NM_079228.3.
DR RefSeq; NP_729218.1; NM_168192.3.
DR AlphaFoldDB; P42281; -.
DR SMR; P42281; -.
DR IntAct; P42281; 1.
DR STRING; 7227.FBpp0076624; -.
DR PaxDb; P42281; -.
DR PRIDE; P42281; -.
DR DNASU; 38784; -.
DR EnsemblMetazoa; FBtr0076915; FBpp0076624; FBgn0010387.
DR EnsemblMetazoa; FBtr0076916; FBpp0076625; FBgn0010387.
DR GeneID; 38784; -.
DR KEGG; dme:Dmel_CG8627; -.
DR CTD; 38784; -.
DR FlyBase; FBgn0010387; Acbp2.
DR VEuPathDB; VectorBase:FBgn0010387; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000173845; -.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P42281; -.
DR OMA; AAQQEYI; -.
DR OrthoDB; 1588000at2759; -.
DR PhylomeDB; P42281; -.
DR BioGRID-ORCS; 38784; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Dbi; fly.
DR GenomeRNAi; 38784; -.
DR PRO; PR:P42281; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010387; Expressed in crop (Drosophila) and 28 other tissues.
DR ExpressionAtlas; P42281; baseline and differential.
DR Genevisible; P42281; DM.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISS:FlyBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0042049; P:cellular acyl-CoA homeostasis; ISS:FlyBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd00435; ACBP; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 2: Evidence at transcript level;
KW Lipid-binding; Reference proteome; Transport.
FT CHAIN 1..86
FT /note="Acyl-CoA-binding protein homolog"
FT /id="PRO_0000214010"
FT DOMAIN 2..86
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 14
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 29..33
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="K -> S (in Ref. 2; CAA53268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 9557 MW; 623986B5566228E1 CRC64;
MVSEQFNAAA EKVKSLTKRP SDDEFLQLYA LFKQASVGDN DTAKPGLLDL KGKAKWEAWN
KQKGKSSEAA QQEYITFVEG LVAKYA
