ACBP_PELRI
ID ACBP_PELRI Reviewed; 88 AA.
AC P45883;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Acyl-CoA-binding protein homolog;
DE Short=ACBP;
DE AltName: Full=Diazepam-binding inhibitor homolog;
DE Short=DBI;
OS Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8406;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-40 AND 59-88.
RC TISSUE=Brain;
RX PubMed=8041717; DOI=10.1073/pnas.91.15.6899;
RA Lihrmann I., Plaquevent J.-C., Tostivint H., Raijmakers R., Tonon M.-C.,
RA Conlon J.M., Vaudry H.;
RT "Frog diazepam-binding inhibitor: peptide sequence, cDNA cloning, and
RT expression in the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6899-6903(1994).
RN [2]
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=1341880; DOI=10.1016/0196-9781(92)90146-t;
RA Malagon M., Vaudry H., Vallarino M., Gracia-Navarro F., Tonon M.C.;
RT "Distribution and characterization of endozepine-like immunoreactivity in
RT the central nervous system of the frog Rana ridibunda.";
RL Peptides 13:99-107(1992).
CC -!- FUNCTION: May play important functions in the control of brain and
CC pituitary activities. May regulate GABA neurotransmission through a
CC paracrine and/or autocrine mechanism. May not bind acyl-CoA esters.
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 -!- TISSUE SPECIFICITY: Brain. Is selectively expressed in glial cells.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; U09205; AAB60606.1; -; mRNA.
DR PIR; A57711; A57711.
DR AlphaFoldDB; P45883; -.
DR SMR; P45883; -.
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; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Lipid-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8041717"
FT CHAIN 2..88
FT /note="Acyl-CoA-binding protein homolog"
FT /id="PRO_0000214009"
FT DOMAIN 3..88
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 15
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 30..34
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
SQ SEQUENCE 88 AA; 9808 MW; 4B2BCA61E8BD54C4 CRC64;
MSPQADFDKA AGDVKKLKTK PTDDELKELY GLYKQSTVGD INIECPGMLD LKGKAKWDAW
NLKKGLSKED AMSAYVSKAH ELIEKYGL
