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Protein

Acyl-CoA-binding protein

Gene

ACB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511Acyl-CoABy similarity
Binding sitei55 – 551Acyl-CoABy similarity
Binding sitei74 – 741Acyl-CoABy similarity

GO - Molecular functioni

  • fatty-acyl-CoA binding Source: SGD
  • lipid binding Source: UniProtKB-KW
  • long-chain fatty acid transporter activity Source: SGD

GO - Biological processi

  • chronological cell aging Source: SGD
  • long-chain fatty acid transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30758-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding protein
Short name:
ACBP
Gene namesi
Name:ACB1
Synonyms:ACB
Ordered Locus Names:YGR037C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR037C.
SGDiS000003269. ACB1.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787Acyl-CoA-binding proteinPRO_0000214013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki51 – 51Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki72 – 72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP31787.

Interactioni

Protein-protein interaction databases

BioGridi33282. 63 interactions.
IntActiP31787. 17 interactions.
MINTiMINT-2788579.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311Combined sources
Helixi22 – 3716Combined sources
Helixi50 – 6011Combined sources
Turni61 – 655Combined sources
Helixi66 – 8520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ST7NMR-A2-87[»]
ProteinModelPortaliP31787.
SMRiP31787. Positions 2-87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8786ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 335Acyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the ACBP family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129776.
HOGENOMiHOG000261845.
InParanoidiP31787.
OMAiRYKFEAW.
OrthoDBiEOG7J70TR.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSQLFEEKA KAVNELPTKP STDELLELYA LYKQATVGDN DKEKPGIFNM
60 70 80
KDRYKWEAWE NLKGKSQEDA EKEYIALVDQ LIAKYSS
Length:87
Mass (Da):10,061
Last modified:January 23, 2007 - v3
Checksum:i686B186195EA02FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99489 Genomic DNA. Translation: AAA34384.1.
Y08687 Genomic DNA. Translation: CAA69944.1.
Y08689 Genomic DNA. Translation: CAA69947.1.
DQ115390 Genomic DNA. Translation: AAZ22453.1.
Z72822 Genomic DNA. Translation: CAA97025.1.
BK006941 Genomic DNA. Translation: DAA08135.1.
PIRiS31247.
RefSeqiNP_011551.3. NM_001181166.3.

Genome annotation databases

EnsemblFungiiYGR037C; YGR037C; YGR037C.
GeneIDi852925.
KEGGisce:YGR037C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99489 Genomic DNA. Translation: AAA34384.1.
Y08687 Genomic DNA. Translation: CAA69944.1.
Y08689 Genomic DNA. Translation: CAA69947.1.
DQ115390 Genomic DNA. Translation: AAZ22453.1.
Z72822 Genomic DNA. Translation: CAA97025.1.
BK006941 Genomic DNA. Translation: DAA08135.1.
PIRiS31247.
RefSeqiNP_011551.3. NM_001181166.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ST7NMR-A2-87[»]
ProteinModelPortaliP31787.
SMRiP31787. Positions 2-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33282. 63 interactions.
IntActiP31787. 17 interactions.
MINTiMINT-2788579.

Proteomic databases

MaxQBiP31787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR037C; YGR037C; YGR037C.
GeneIDi852925.
KEGGisce:YGR037C.

Organism-specific databases

EuPathDBiFungiDB:YGR037C.
SGDiS000003269. ACB1.

Phylogenomic databases

GeneTreeiENSGT00840000129776.
HOGENOMiHOG000261845.
InParanoidiP31787.
OMAiRYKFEAW.
OrthoDBiEOG7J70TR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30758-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP31787.
PROiP31787.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the gene for the yeast homolog (ACB) of diazepam binding inhibitor/endozepine/acyl-CoA-binding protein."
    Rose T.M., Schultz E.R., Todaro G.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:11287-11291(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Saccharomyces carlsbergensis contains two functional genes encoding the acyl-CoA binding protein, one similar to the ACB1 gene from S. cerevisiae and one identical to the ACB1 gene from S. monacensis."
    Borsting C., Hummel R., Schultz E.R., Rose T.M., Pedersen M.B., Knudsen J., Kristiansen K.
    Yeast 13:1409-1421(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26109 / X2180.
  3. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SK1.
  4. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles."
    Teilum K., Thormann T., Caterer N.R., Poulsen H.I., Jensen P.H., Knudsen J., Kragelund B.B., Poulsen F.M.
    Proteins 59:80-90(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiACBP_YEAST
AccessioniPrimary (citable) accession number: P31787
Secondary accession number(s): D6VUH4, Q45U46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.