ACBP_YEAST
ID ACBP_YEAST Reviewed; 87 AA.
AC P31787; D6VUH4; Q45U46;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Acyl-CoA-binding protein;
DE Short=ACBP;
GN Name=ACB1; Synonyms=ACB; OrderedLocusNames=YGR037C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1454809; DOI=10.1073/pnas.89.23.11287;
RA Rose T.M., Schultz E.R., Todaro G.J.;
RT "Molecular cloning of the gene for the yeast homolog (ACB) of diazepam
RT binding inhibitor/endozepine/acyl-CoA-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11287-11291(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=9434347;
RX DOI=10.1002/(sici)1097-0061(199712)13:15<1409::aid-yea188>3.0.co;2-a;
RA Borsting C., Hummel R., Schultz E.R., Rose T.M., Pedersen M.B., Knudsen J.,
RA Kristiansen K.;
RT "Saccharomyces carlsbergensis contains two functional genes encoding the
RT acyl-CoA binding protein, one similar to the ACB1 gene from S. cerevisiae
RT and one identical to the ACB1 gene from S. monacensis.";
RL Yeast 13:1409-1421(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-72, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=15690348; DOI=10.1002/prot.20340;
RA Teilum K., Thormann T., Caterer N.R., Poulsen H.I., Jensen P.H.,
RA Knudsen J., Kragelund B.B., Poulsen F.M.;
RT "Different secondary structure elements as scaffolds for protein folding
RT transition states of two homologous four-helix bundles.";
RL Proteins 59:80-90(2005).
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 -!- MISCELLANEOUS: Present with 8500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; M99489; AAA34384.1; -; Genomic_DNA.
DR EMBL; Y08687; CAA69944.1; -; Genomic_DNA.
DR EMBL; Y08689; CAA69947.1; -; Genomic_DNA.
DR EMBL; DQ115390; AAZ22453.1; -; Genomic_DNA.
DR EMBL; Z72822; CAA97025.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08135.1; -; Genomic_DNA.
DR PIR; S31247; S31247.
DR RefSeq; NP_011551.3; NM_001181166.3.
DR PDB; 1ST7; NMR; -; A=2-87.
DR PDBsum; 1ST7; -.
DR AlphaFoldDB; P31787; -.
DR BMRB; P31787; -.
DR SMR; P31787; -.
DR BioGRID; 33282; 159.
DR IntAct; P31787; 17.
DR MINT; P31787; -.
DR STRING; 4932.YGR037C; -.
DR iPTMnet; P31787; -.
DR MaxQB; P31787; -.
DR PaxDb; P31787; -.
DR PRIDE; P31787; -.
DR EnsemblFungi; YGR037C_mRNA; YGR037C; YGR037C.
DR GeneID; 852925; -.
DR KEGG; sce:YGR037C; -.
DR SGD; S000003269; ACB1.
DR VEuPathDB; FungiDB:YGR037C; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000173845; -.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P31787; -.
DR OMA; RYKFEAW; -.
DR BioCyc; YEAST:G3O-30758-MON; -.
DR Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-SCE-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR EvolutionaryTrace; P31787; -.
DR PRO; PR:P31787; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P31787; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
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:0036042; F:long-chain fatty acyl-CoA binding; IMP:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:SGD.
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 3D-structure; Isopeptide bond; Lipid-binding; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214013"
FT DOMAIN 2..87
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
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 CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1ST7"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:1ST7"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1ST7"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:1ST7"
FT HELIX 66..85
FT /evidence="ECO:0007829|PDB:1ST7"
SQ SEQUENCE 87 AA; 10061 MW; 686B186195EA02FC CRC64;
MVSQLFEEKA KAVNELPTKP STDELLELYA LYKQATVGDN DKEKPGIFNM KDRYKWEAWE
NLKGKSQEDA EKEYIALVDQ LIAKYSS
