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Protein

Acyl-coenzyme A thioesterase 1

Gene

Acot1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. True acyl-CoA thioesterase being highly specific for saturated C12-C20 acyl-CoAs, with only a very low activity with decanoyl-CoA as substrate. Most active on myristoyl- and palmitoyl-CoA. Introduction of one or two double bonds decreases the activity to about half. No detectable activity with bile acid CoAs such as choloyl-CoA and chenodeoxycholoyl-CoA.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Kineticsi

  1. KM=2.6 µM for palmitoyl-CoA1 Publication
  1. Vmax=1.2 µmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay system1 Publication
Active sitei324 – 3241Charge relay system1 Publication
Active sitei358 – 3581Charge relay system1 Publication

GO - Molecular functioni

GO - Biological processi

  • acyl-CoA metabolic process Source: MGI
  • long-chain fatty acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2. 3474.
ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKO55137.

Protein family/group databases

ESTHERimouse-acot1. Acyl-CoA_Thioesterase.
MEROPSiS09.A52.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 1 (EC:3.1.2.2)
Short name:
Acyl-CoA thioesterase 1
Alternative name(s):
CTE-I
Inducible cytosolic acyl-coenzyme A thioester hydrolase
Long chain acyl-CoA thioester hydrolase
Short name:
Long chain acyl-CoA hydrolase
Gene namesi
Name:Acot1
Synonyms:Cte1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1349396. Acot1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321S → A: Abolishes activity. 1 Publication
Mutagenesisi232 – 2321S → C: Retains 2% of the initial activity; deacylation of the acyl-enzyme intermediate becomes rate-limiting. 1 Publication
Mutagenesisi324 – 3241D → A: Abolishes activity. 1 Publication
Mutagenesisi358 – 3581H → Q: Abolishes activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3259489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 419418Acyl-coenzyme A thioesterase 1PRO_0000202156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei416 – 4161PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO55137.
MaxQBiO55137.
PaxDbiO55137.
PRIDEiO55137.

2D gel databases

UCD-2DPAGEO55137.

PTM databases

iPTMnetiO55137.
PhosphoSiteiO55137.

Expressioni

Tissue specificityi

Expressed in heart, kidney, brown adipose tissue, white adipose tissue, adrenal gland and muscle.2 Publications

Inductioni

In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours.1 Publication

Gene expression databases

BgeeiO55137.
CleanExiMM_ACOT1.
GenevisibleiO55137. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiO55137. 3 interactions.
MINTiMINT-4092493.
STRINGi10090.ENSMUSP00000126448.

Structurei

3D structure databases

ProteinModelPortaliO55137.
SMRiO55137. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOVERGENiHBG000331.
InParanoidiO55137.
KOiK01068.
OMAiASRLYQW.
OrthoDBiEOG75TMC9.
PhylomeDBiO55137.
TreeFamiTF314911.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55137-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATLNLEPS GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA
60 70 80 90 100
RYRADSHGEL DLARTPALGG SFSGLEPMGL LWAMEPDRPF WRLVKRDVQT
110 120 130 140 150
PFVVELEVLD GHEPDGGQRL AHAVHERHFL APGVRRVPVR EGRVRATLFL
160 170 180 190 200
PPEPGPFPGI IDLFGVGGGL LEYRASLLAG KGFAVMALAY YNYDDLPKNM
210 220 230 240 250
ETMHMEYFEE AVNYLRSHPE VKGPGIGLLG ISKGGELGLA MASFLKGITA
260 270 280 290 300
AVVINGSVAA VGNTISYKDE TIPPVTILRN QVKMTKDGLK DVVDALQSPL
310 320 330 340 350
VDKKSFIPVE RSDTTFLFLV GQDDHNWKSE FYADEISKRL QAHGKEKPQI
360 370 380 390 400
ICYPAAGHYI EPPYFPLCSA GMHLLVGANI TFGGEPKPHA MAQLDAWQQL
410
QTFFHKQLGS ECLHVSPKI
Length:419
Mass (Da):46,136
Last modified:June 1, 1998 - v1
Checksum:i57346B6177471CFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180795, AF180793, AF180794 Genomic DNA. Translation: AAF13870.1.
Y14004 mRNA. Translation: CAA74327.1.
BC028261 mRNA. Translation: AAH28261.1.
CCDSiCCDS36487.1.
RefSeqiNP_036136.1. NM_012006.2.
UniGeneiMm.1978.

Genome annotation databases

EnsembliENSMUST00000168120; ENSMUSP00000126448; ENSMUSG00000072949.
GeneIDi26897.
KEGGimmu:26897.
UCSCiuc007oeb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180795, AF180793, AF180794 Genomic DNA. Translation: AAF13870.1.
Y14004 mRNA. Translation: CAA74327.1.
BC028261 mRNA. Translation: AAH28261.1.
CCDSiCCDS36487.1.
RefSeqiNP_036136.1. NM_012006.2.
UniGeneiMm.1978.

3D structure databases

ProteinModelPortaliO55137.
SMRiO55137. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO55137. 3 interactions.
MINTiMINT-4092493.
STRINGi10090.ENSMUSP00000126448.

Chemistry

ChEMBLiCHEMBL3259489.

Protein family/group databases

ESTHERimouse-acot1. Acyl-CoA_Thioesterase.
MEROPSiS09.A52.

PTM databases

iPTMnetiO55137.
PhosphoSiteiO55137.

2D gel databases

UCD-2DPAGEO55137.

Proteomic databases

EPDiO55137.
MaxQBiO55137.
PaxDbiO55137.
PRIDEiO55137.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000168120; ENSMUSP00000126448; ENSMUSG00000072949.
GeneIDi26897.
KEGGimmu:26897.
UCSCiuc007oeb.1. mouse.

Organism-specific databases

CTDi641371.
MGIiMGI:1349396. Acot1.

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOVERGENiHBG000331.
InParanoidiO55137.
KOiK01068.
OMAiASRLYQW.
OrthoDBiEOG75TMC9.
PhylomeDBiO55137.
TreeFamiTF314911.

Enzyme and pathway databases

BRENDAi3.1.2.2. 3474.
ReactomeiR-MMU-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKO55137.

Miscellaneous databases

PROiO55137.
SOURCEiSearch...

Gene expression databases

BgeeiO55137.
CleanExiMM_ACOT1.
GenevisibleiO55137. MM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism."
    Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Alexson S.E.H.
    J. Biol. Chem. 274:34317-34326(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism."
    Hunt M.C., Lindquist P.J.G., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T., Aoyama T., Hashimoto T., Diczfalusy U., Alexson S.E.H.
    Cell Biochem. Biophys. 32:317-324(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION, TISSUE SPECIFICITY.
  3. "Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic acyl-CoA thioesterase from mouse and rat liver --recombinant expression in Escherichia coli, tissue expression, and nutritional regulation."
    Lindquist P.J.G., Svensson L.T., Alexson S.E.H.
    Eur. J. Biochem. 251:631-640(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  5. "The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase."
    Huhtinen K., O'Byrne J., Lindquist P.J.G., Contreras J.A., Alexson S.E.H.
    J. Biol. Chem. 277:3424-3432(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITES, MUTAGENESIS OF SER-232; ASP-324 AND HIS-358, BIOPHYSICOCHEMICAL PROPERTIES.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiACOT1_MOUSE
AccessioniPrimary (citable) accession number: O55137
Secondary accession number(s): Q549A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.