ACBP_BOVIN
ID ACBP_BOVIN Reviewed; 87 AA.
AC P07107; Q29RG9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2881742; DOI=10.1089/dna.1987.6.71;
RA Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J.,
RA Lee D.C.;
RT "Bovine and human cDNA sequences encoding a putative benzodiazepine
RT receptor ligand.";
RL DNA 6:71-79(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-87, AND ACETYLATION AT SER-2.
RC TISSUE=Brain;
RX PubMed=3525533; DOI=10.1016/s0021-9258(18)67575-1;
RA Marquardt H., Todaro G.J., Shoyab M.;
RT "Complete amino acid sequences of bovine and human endozepines. Homology
RT with rat diazepam binding inhibitor.";
RL J. Biol. Chem. 261:9727-9731(1986).
RN [4]
RP PROTEIN SEQUENCE OF 2-87.
RC TISSUE=Liver;
RX PubMed=3663196; DOI=10.1042/bj2450857;
RA Mikkelsen J., Hoejrup P., Nielsen P.F., Roepstorff P., Knudsen J.;
RT "Amino acid sequence of acyl-CoA-binding protein from cow liver.";
RL Biochem. J. 245:857-861(1987).
RN [5]
RP PROTEIN SEQUENCE OF 2-87.
RC TISSUE=Liver;
RX PubMed=1622397; DOI=10.1042/bj2840809;
RA Jensen M.S., Hoejrup P., Rasmussen J.T., Knudsen J.;
RT "Purification and characterization of variants of acyl-CoA-binding protein
RT in the bovine liver.";
RL Biochem. J. 284:809-812(1992).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17953517; DOI=10.1042/bj20070559;
RA Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.;
RT "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and
RT Golgi in a ligand-dependent manner in mammalian cells.";
RL Biochem. J. 410:463-472(2008).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=1931985; DOI=10.1021/bi00108a008;
RA Andersen K.V., Ludvigsen S., Mandrup S., Knudsen J., Poulsen F.M.;
RT "The secondary structure in solution of acyl-coenzyme A binding protein
RT from bovine liver using 1H nuclear magnetic resonance spectroscopy.";
RL Biochemistry 30:10654-10663(1991).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=1518047; DOI=10.1016/0022-2836(92)91057-v;
RA Andersen K.V., Poulsen F.M.;
RT "Three-dimensional structure in solution of acyl-coenzyme A binding protein
RT from bovine liver.";
RL J. Mol. Biol. 226:1131-1141(1992).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=8358232; DOI=10.1007/bf00212514;
RA Andersen K.V., Poulsen F.M.;
RT "The three-dimensional structure of acyl-coenzyme A binding protein from
RT bovine liver: structural refinement using heteronuclear multidimensional
RT NMR spectroscopy.";
RL J. Biomol. NMR 3:271-284(1993).
RN [10]
RP STRUCTURE BY NMR IN COMPLEX WITH THE ACYL-COA ANALOG COENZYME A AND
RP PALMITIC ACID.
RX PubMed=8503960; DOI=10.1006/jmbi.1993.1240;
RA Kragelund B.B., Andersen K.V., Madsen J.C., Knudsen J., Poulsen F.M.;
RT "Three-dimensional structure of the complex between acyl-coenzyme A binding
RT protein and palmitoyl-coenzyme A.";
RL J. Mol. Biol. 230:1260-1277(1993).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND FUNCTION.
RX PubMed=11491287; DOI=10.1006/jmbi.2001.4749;
RA van Aalten D.M., Milne K.G., Zou J.Y., Kleywegt G.J., Bergfors T.,
RA Ferguson M.A., Knudsen J., Jones T.A.;
RT "Binding site differences revealed by crystal structures of Plasmodium
RT falciparum and bovine acyl-CoA binding protein.";
RL J. Mol. Biol. 309:181-192(2001).
RN [12]
RP STRUCTURE BY NMR IN COMPLEX WITH THE ACYL-COA PALMITOYL-COENZYME A.
RA Lerche M.H., Kragelund B.B., Redfield C., Poulsen F.M.;
RT "RDC-refined NMR structure of bovine acyl-coenzyme A binding protein, ACBP,
RT in complex with palmitoyl-coenzyme A.";
RL Submitted (FEB-2003) to the PDB data bank.
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.
CC {ECO:0000269|PubMed:11491287}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8503960, ECO:0000269|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:17953517}. Golgi apparatus
CC {ECO:0000269|PubMed:17953517}. 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; M15886; AAA30495.1; -; mRNA.
DR EMBL; BC114181; AAI14182.1; -; mRNA.
DR PIR; A26448; NZBO.
DR RefSeq; NP_001106792.1; NM_001113321.1.
DR PDB; 1ACA; NMR; -; A=2-87.
DR PDB; 1HB6; X-ray; 2.00 A; A=2-87.
DR PDB; 1HB8; X-ray; 2.00 A; A/B/C=2-87.
DR PDB; 1NTI; NMR; -; A=2-87.
DR PDB; 1NVL; NMR; -; A=2-87.
DR PDB; 2ABD; NMR; -; A=2-87.
DR PDBsum; 1ACA; -.
DR PDBsum; 1HB6; -.
DR PDBsum; 1HB8; -.
DR PDBsum; 1NTI; -.
DR PDBsum; 1NVL; -.
DR PDBsum; 2ABD; -.
DR AlphaFoldDB; P07107; -.
DR BMRB; P07107; -.
DR SMR; P07107; -.
DR STRING; 9913.ENSBTAP00000012523; -.
DR iPTMnet; P07107; -.
DR PaxDb; P07107; -.
DR PeptideAtlas; P07107; -.
DR PRIDE; P07107; -.
DR Ensembl; ENSBTAT00000012523; ENSBTAP00000012523; ENSBTAG00000009517.
DR GeneID; 768330; -.
DR KEGG; bta:768330; -.
DR CTD; 1622; -.
DR VEuPathDB; HostDB:ENSBTAG00000009517; -.
DR VGNC; VGNC:27889; DBI.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000154846; -.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P07107; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR TreeFam; TF335802; -.
DR EvolutionaryTrace; P07107; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009517; Expressed in caput epididymis and 105 other tissues.
DR ExpressionAtlas; P07107; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Endoplasmic reticulum; Golgi apparatus; Hydroxylation; Lipid-binding;
KW Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1622397,
FT ECO:0000269|PubMed:3525533, ECO:0000269|PubMed:3663196"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214001"
FT DOMAIN 2..87
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:0000269|PubMed:8503960, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1ACA, ECO:0007744|PDB:1NVL"
FT BINDING 29..33
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:8503960, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1ACA, ECO:0007744|PDB:1NVL"
FT BINDING 51
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:8503960, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1ACA, ECO:0007744|PDB:1NVL"
FT BINDING 55
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:8503960, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1ACA, ECO:0007744|PDB:1NVL"
FT BINDING 74
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:8503960, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1ACA, ECO:0007744|PDB:1NVL"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3525533"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 55
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 55
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 77
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07108"
FT MOD_RES 77
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1HB6"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1HB6"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1ACA"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1HB6"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1HB6"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1HB6"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:1HB6"
SQ SEQUENCE 87 AA; 10044 MW; B2922635F18CA0D8 CRC64;
MSQAEFDKAA EEVKHLKTKP ADEEMLFIYS HYKQATVGDI NTERPGMLDF KGKAKWDAWN
ELKGTSKEDA MKAYIDKVEE LKKKYGI
