ID   ACBP_ANAPL              Reviewed;         103 AA.
AC   P45882;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acyl-CoA-binding protein;
DE            Short=ACBP;
DE   AltName: Full=Diazepam-binding inhibitor;
DE            Short=DBI;
DE   AltName: Full=Endozepine;
DE            Short=EP;
GN   Name=DBI;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8024707; DOI=10.1089/dna.1994.13.669;
RA   Rose T.M., Schultz E.R., Sasaki G.C., Kolattukudy P.E., Shoyab M.;
RT   "Nucleotide sequence and genomic structure of duck acyl-CoA binding
RT   protein/diazepam-binding inhibitor: co-localization with S-acyl fatty acid
RT   synthase thioesterase.";
RL   DNA Cell Biol. 13:669-678(1994).
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. It is also able to displace diazepam from the benzodiazepine
CC       (BZD) recognition site located on the GABA type A receptor. It is
CC       therefore possible that this protein also acts as a neuropeptide to
CC       modulate the action of the GABA receptor (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P07108}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on
CC       ligand binding. {ECO:0000250|UniProtKB:P07108}.
CC   -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR   EMBL; S73733; AAB31268.1; -; Genomic_DNA.
DR   PIR; I51248; I51248.
DR   AlphaFoldDB; P45882; -.
DR   SMR; P45882; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Golgi apparatus; Lipid-binding; Transport.
FT   CHAIN           1..103
FT                   /note="Acyl-CoA-binding protein"
FT                   /id="PRO_0000214007"
FT   DOMAIN          18..103
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   BINDING         30
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..49
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   103 AA;  11777 MW;  EBFDB78076894269 CRC64;
     MFQAHLLRGT LTLSFFLHQA DFDEAAEEVK KLKTRPTDEE LKELYGFYKQ ATVGDINIEC
     PGMLDLKGKA KWEAWNLKKG ISKEDAMNAY ISKAKTMVEK YGI