ACBP_CANLF
ID ACBP_CANLF Reviewed; 87 AA.
AC Q9TQX6;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE OF 2-87.
RX PubMed=8609609; DOI=10.1006/jmbi.1996.0076;
RA Kragelund B.B., Hoejrup P., Jensen M.S., Schjerling C.K., Juul E.,
RA Knudsen J., Poulsen F.M.;
RT "Fast and one-step folding of closely and distantly related homologous
RT proteins of a four-helix bundle family.";
RL J. Mol. Biol. 256:187-200(1996).
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.
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 PIR; S63592; S63592.
DR RefSeq; NP_001183976.1; NM_001197047.1.
DR AlphaFoldDB; Q9TQX6; -.
DR SMR; Q9TQX6; -.
DR STRING; 9615.ENSCAFP00000050070; -.
DR PaxDb; Q9TQX6; -.
DR Ensembl; ENSCAFT00030037948; ENSCAFP00030033107; ENSCAFG00030020618.
DR Ensembl; ENSCAFT00040014563; ENSCAFP00040012591; ENSCAFG00040007752.
DR Ensembl; ENSCAFT00845051008; ENSCAFP00845039987; ENSCAFG00845028816.
DR GeneID; 476115; -.
DR KEGG; cfa:476115; -.
DR CTD; 1622; -.
DR VEuPathDB; HostDB:ENSCAFG00845028816; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000154846; -.
DR InParanoid; Q9TQX6; -.
DR OrthoDB; 1588000at2759; -.
DR Reactome; R-CFA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Proteomes; UP000002254; Chromosome 19.
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 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:0000250|UniProtKB:P07107,
FT ECO:0000269|PubMed:8609609"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214002"
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 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 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; 9978 MW; BC92C669E389CB52 CRC64;
MSQAEFDKAA EDVKHLKTKP ADDEMLYIYS HYKQATVGDI NTERPGLLDL RGKAKWDAWN
QLKGTSKEDA MKAYVNKVED LKKKYGI
