ACBP_RABIT
ID ACBP_RABIT Reviewed; 87 AA.
AC Q8WN94;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000312|EMBL:AAK98608.2};
RN [1] {ECO:0000312|EMBL:AAK98608.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Barmack N.H., Liu H., Qian Z., Bilderback T.;
RT "Localization of an endogenous diazepam ligand, acyl CoA binding protein,
RT to Muller cells in rabbit retina.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:P07107}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P07107}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF407578; AAK98608.2; -; mRNA.
DR RefSeq; NP_001075582.1; NM_001082113.1.
DR AlphaFoldDB; Q8WN94; -.
DR SMR; Q8WN94; -.
DR STRING; 9986.ENSOCUP00000003937; -.
DR iPTMnet; Q8WN94; -.
DR Ensembl; ENSOCUT00000004563; ENSOCUP00000003937; ENSOCUG00000004566.
DR GeneID; 100008823; -.
DR KEGG; ocu:100008823; -.
DR CTD; 1622; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000154846; -.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; Q8WN94; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR TreeFam; TF335802; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000004566; Expressed in prefrontal cortex and 16 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0032994; C:protein-lipid complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IEA:Ensembl.
DR GO; GO:1903060; P:negative regulation of protein lipidation; IEA:Ensembl.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IEA:Ensembl.
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 Acetylation; Endoplasmic reticulum; Golgi apparatus; Hydroxylation;
KW Lipid-binding; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214006"
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:0000250|UniProtKB:P07107"
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"
SQ SEQUENCE 87 AA; 9915 MW; 2C8A6A222934DE3E CRC64;
MSQAEFEKAA EEVKNLKTKP ADAEMLFIYS HYKQATVGDV NTERPGMLDL KGKAKWDAWN
ELKGTSKESA MRAYVDKVEE LKQKYGI
