ACBP_PIG
ID ACBP_PIG Reviewed; 87 AA.
AC P12026; A7YB23; Q9TSG2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
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=DBI(32-86);
GN Name=DBI;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipose tissue;
RA Ramli N., Suzuki H., Karnuah A.B., Hamasima N.;
RT "Cloning of pig endozepine gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Dirisala V.R., Kim J., Park K., Kang I., Choi H., Park C.;
RT "Pig cSNP discovery using full-length enriched cDNA libraries from the
RT database and Korean native pigs.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-87, AND ACETYLATION AT SER-2.
RC TISSUE=Intestine;
RX PubMed=3289918; DOI=10.1111/j.1432-1033.1988.tb14088.x;
RA Chen Z.W., Agerberth B., Gell K., Andersson M., Mutt V., Oestenson C.G.,
RA Efendic S., Barros-Soederling J., Persson B., Joernvall H.;
RT "Isolation and characterization of porcine diazepam-binding inhibitor, a
RT polypeptide not only of cerebral occurrence but also common in intestinal
RT tissues and with effects on regulation of insulin release.";
RL Eur. J. Biochem. 174:239-245(1988).
RN [4]
RP PROTEIN SEQUENCE OF 33-87.
RC TISSUE=Intestine;
RX PubMed=8375398; DOI=10.1111/j.1432-1033.1993.tb18182.x;
RA Agerberth B., Boman A., Andersson M., Joernvall H., Mutt V., Boman H.G.;
RT "Isolation of three antibacterial peptides from pig intestine: gastric
RT inhibitory polypeptide (7-42), diazepam-binding inhibitor (32-86) and a
RT novel factor, peptide 3910.";
RL Eur. J. Biochem. 216:623-629(1993).
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 -!- FUNCTION: DBI(32-86) has antibacterial properties.
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; AB019792; BAA34531.1; -; mRNA.
DR EMBL; DQ885192; ABM30147.1; -; mRNA.
DR PIR; S00805; NZPG.
DR RefSeq; NP_999284.1; NM_214119.1.
DR AlphaFoldDB; P12026; -.
DR SMR; P12026; -.
DR STRING; 9823.ENSSSCP00000021888; -.
DR iPTMnet; P12026; -.
DR PaxDb; P12026; -.
DR PeptideAtlas; P12026; -.
DR PRIDE; P12026; -.
DR Ensembl; ENSSSCT00005003195; ENSSSCP00005001848; ENSSSCG00005002143.
DR Ensembl; ENSSSCT00070004160; ENSSSCP00070003430; ENSSSCG00070002226.
DR GeneID; 397212; -.
DR KEGG; ssc:397212; -.
DR CTD; 1622; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P12026; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR TreeFam; TF335802; -.
DR Reactome; R-SSC-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 15.
DR Genevisible; P12026; SS.
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:0042742; P:defense response to bacterium; 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; Antibiotic; Antimicrobial; 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:3289918"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000045199"
FT PEPTIDE 33..87
FT /note="DBI(32-86)"
FT /id="PRO_0000000287"
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:3289918"
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; 9896 MW; 3225B53E8307DE38 CRC64;
MSQAEFEKAA EEVKNLKTKP ADDEMLFIYS HYKQATVGDI NTERPGILDL KGKAKWDAWN
GLKGTSKEDA MKAYINKVEE LKKKYGI
