ACBP_RAT
ID ACBP_RAT Reviewed; 87 AA.
AC P11030; Q2V4X5; Q63160;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
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;
DE Contains:
DE RecName: Full=Triakontatetraneuropeptide;
DE Short=TTN;
DE Contains:
DE RecName: Full=Octadecaneuropeptide;
DE Short=ODN;
GN Name=Dbi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3463960; DOI=10.1073/pnas.83.19.7221;
RA Mocchetti I., Einstein R., Brosius J.;
RT "Putative diazepam binding inhibitor peptide: cDNA clones from rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7221-7225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2821429; DOI=10.1016/0028-3908(87)90063-3;
RA Gray P.W.;
RT "Molecular biology of diazepam binding inhibitor.";
RL Neuropharmacology 26:863-865(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=1469708; DOI=10.1016/0022-2836(92)90888-q;
RA Mandrup S., Hummel R., Ravn S., Jensen G., Andreasen P.H., Gregersen N.,
RA Knudsen J., Kristiansen K.;
RT "Acyl-CoA-binding protein/diazepam-binding inhibitor gene and pseudogenes.
RT A typical housekeeping gene family.";
RL J. Mol. Biol. 228:1011-1022(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8964506; DOI=10.1016/0378-1119(96)00214-4;
RA Kroell J.B., Nohr J., Gregersen N., Kristiansen K., Mandrup S.;
RT "Structure of the rat gene encoding the multifunctional acyl-CoA-binding
RT protein: conservation of intron 1 sequences in rodents and man.";
RL Gene 173:239-240(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RX PubMed=7690962; DOI=10.1073/pnas.90.18.8439;
RA Kolmer M., Alho H., Costa E., Pani L.;
RT "Cloning and tissue-specific functional characterization of the promoter of
RT the rat diazepam binding inhibitor, a peptide with multiple biological
RT actions.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8439-8443(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-87, AND ACETYLATION AT SER-2.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2803267; DOI=10.1042/bj2620513;
RA Knudsen J., Hoejrup P., Hansen H.O., Hansen H.F., Roepstorff P.;
RT "Acyl-CoA-binding protein in the rat. Purification, binding
RT characteristics, tissue concentrations and amino acid sequence.";
RL Biochem. J. 262:513-519(1989).
RN [8]
RP PROTEIN SEQUENCE OF 18-51.
RC TISSUE=Brain;
RX PubMed=2769267; DOI=10.1111/j.1471-4159.1989.tb07425.x;
RA Slobodyansky E., Guidotti A., Wambebe C., Berkovich A., Costa E.;
RT "Isolation and characterization of a rat brain triakontatetraneuropeptide,
RT a posttranslational product of diazepam binding inhibitor: specific action
RT at the Ro 5-4864 recognition site.";
RL J. Neurochem. 53:1276-1284(1989).
RN [9]
RP PROTEIN SEQUENCE OF 34-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
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 -!- SUBUNIT: Monomer.
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; M14201; AAA41078.1; -; mRNA.
DR EMBL; M20268; AAA41079.1; -; mRNA.
DR EMBL; Z11991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S51442; AAA12824.1; -; Genomic_DNA.
DR EMBL; S51427; AAA12824.1; JOINED; Genomic_DNA.
DR EMBL; S51426; AAA12824.1; JOINED; Genomic_DNA.
DR EMBL; X96560; CAA65396.1; -; Genomic_DNA.
DR EMBL; BC084717; AAH84717.1; -; mRNA.
DR EMBL; Z21846; CAA79894.1; -; Genomic_DNA.
DR PIR; S27345; NZRT.
DR RefSeq; NP_114054.1; NM_031853.4.
DR AlphaFoldDB; P11030; -.
DR SMR; P11030; -.
DR BioGRID; 247122; 1.
DR DIP; DIP-1164N; -.
DR IntAct; P11030; 2.
DR STRING; 10116.ENSRNOP00000066874; -.
DR iPTMnet; P11030; -.
DR PhosphoSitePlus; P11030; -.
DR jPOST; P11030; -.
DR PaxDb; P11030; -.
DR PRIDE; P11030; -.
DR GeneID; 25045; -.
DR KEGG; rno:25045; -.
DR CTD; 1622; -.
DR RGD; 2490; Dbi.
DR VEuPathDB; HostDB:ENSRNOG00000046889; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P11030; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR PRO; PR:P11030; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000046889; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; P11030; baseline and differential.
DR Genevisible; P11030; RN.
DR GO; GO:0043292; C:contractile fiber; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032994; C:protein-lipid complex; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030156; F:benzodiazepine receptor binding; IDA:RGD.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; ISO:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; TAS:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0031670; P:cellular response to nutrient; IEP:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0014009; P:glial cell proliferation; IDA:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0021670; P:lateral ventricle development; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IDA:RGD.
DR GO; GO:1903060; P:negative regulation of protein lipidation; ISO:RGD.
DR GO; GO:0030157; P:pancreatic juice secretion; IEP:RGD.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:RGD.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IDA:RGD.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; ISO:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:RGD.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IDA:MGI.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; TAS:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
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 Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Hydroxylation; Lipid-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2803267"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000045273"
FT PEPTIDE 18..51
FT /note="Triakontatetraneuropeptide"
FT /evidence="ECO:0000269|PubMed:2769267"
FT /id="PRO_0000000288"
FT PEPTIDE 34..51
FT /note="Octadecaneuropeptide"
FT /id="PRO_0000000289"
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: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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2803267"
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 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"
SQ SEQUENCE 87 AA; 10027 MW; C6B231C903098CDE CRC64;
MSQADFDKAA EEVKRLKTQP TDEEMLFIYS HFKQATVGDV NTDRPGLLDL KGKAKWDSWN
KLKGTSKENA MKTYVEKVEE LKKKYGI
