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Reviewed, UniProtKB/Swiss-Prot O88267 (ACOT1_RAT)

Last modified October 13, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A thioesterase 1
      Short name=Acyl-CoA thioesterase 1
    EC=3.1.2.2
Alternative name(s):
    Inducible cytosolic acyl-coenzyme A thioester hydrolase
    Long chain acyl-CoA thioester hydrolase
      Short name=Long chain acyl-CoA hydrolase
    CTE-I
    LACH2
      Short name=ACH2
Gene names
Name: Acot1
Synonyms: Cte1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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. Active towards fatty acyl-CoA with chain-lengths of C12-C16.

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in liver.

Induction

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

Sequence similarities

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

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Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Serine esterase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processacyl-CoA metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol Ref.3

Inferred from direct assay. Source: RGD

   Molecular functioncarboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

palmitoyl-CoA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Acyl-coenzyme A thioesterase 1
PRO_0000202157

Sites

Active site2321Charge relay system By similarity
Active site3241Charge relay system By similarity
Active site3581Charge relay system By similarity

Experimental info

Sequence conflict81E → G Ref.2
Sequence conflict81E → G Ref.3
Sequence conflict811I → L Ref.2
Sequence conflict811I → L Ref.3
Sequence conflict1131E → K Ref.2
Sequence conflict1131E → K Ref.3
Sequence conflict1621D → N Ref.2
Sequence conflict1621D → N Ref.3

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Sequences

Sequence LengthMass (Da)Tools
O88267-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6A0E828A08CEC7C9

FASTA41946,013
        10         20         30         40         50         60 
MEATLSLEPA GRSCWDEPLS ITVRGLVPEQ PVTLRAALRD EKGALFRARA LYRADAHGEL 

        70         80         90        100        110        120 
DLARAPALGG SFTGLEPMGL IWAMEPERPF WRLVKRDVQT PFVVELEVLD GHEPDGGRLL 

       130        140        150        160        170        180 
ARAVHERHFM APGVRRVPVR EGRVRATLFL PPEPGPFPGI IDLFGVGGGL LEYRASLLAG 

       190        200        210        220        230        240 
KGFAVMALAY YNYDDLPKTM ETMRIEYFEE AVNYLRGHPE VKGPGIGLLG ISKGGELGLA 

       250        260        270        280        290        300 
MASFLKGITA AVVINGSVAA VGNTICYKDE TIPPVTILRN QVKMTKDGLK DVVDALQSPL 

       310        320        330        340        350        360 
VEQKSFIPVE RSDTTFLFLV GQDDHNWKSE FYANEISKRL QAHGKEKPQI ICYPEAGHYI 

       370        380        390        400        410 
EPPYFPLCSA GMHLLVGANI TFGGEPKPHS VAQLDAWQQL QTFFHKQLGG KSHGVSPKI

« Hide

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References

[1]"cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol."
Yamada J., Suga K., Furihata T., Kitahara M., Watanabe T., Hosokawa M., Satoh T., Suga T.
Biochem. Biophys. Res. Commun. 248:608-612(1998) [PubMed: 9703974] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-34; 85-107; 187-198; 312-324 AND 374-338.
Tissue: Liver.
[2]"Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver."
Svensson L.T., Engberg S.T., Aoyama T., Usuda N., Alexson S.E.H., Hashimoto T.
Biochem. J. 329:601-608(1998) [PubMed: 9445388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-122.
Strain: Sprague-Dawley.
[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: 9490035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Purification and properties of long-chain acyl-CoA hydrolases from the liver cytosol of rats treated with peroxisome proliferator."
Yamada J., Matsumoto I., Furihata T., Sakuma M., Suga T.
Arch. Biochem. Biophys. 308:118-125(1994) [PubMed: 7906114] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB010428 mRNA. Translation: BAA32434.1.
Y09334 mRNA. Translation: CAA70514.1.
IPIIPI00326667.
PIRJE0267.
RefSeqNP_112605.1.
UniGeneRn.11326

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO88267.

Proteomic databases

PRIDEO88267.

Genome annotation databases

EnsemblENSRNOT00000013729; ENSRNOP00000013729; ENSRNOG00000028870; Rattus norvegicus. [Genome view]
GeneID50559.
KEGGrno:50559.
UCSCNM_031315. rat.

Organism-specific databases

CTD50559.
RGD70894. Acot1.

Phylogenomic databases

HOVERGENO88267.

Enzyme and pathway databases

BRENDA3.1.2.2. 248.
3.1.2.20. 248.

Gene expression databases

ArrayExpressO88267.
GenevestigatorO88267.
GermOnlineENSRNOG00000028870. Rattus norvegicus.

Family and domain databases

InterProIPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFPIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNetSearch...

Other Resources

NextBio610378.

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Entry information

Entry nameACOT1_RAT
AccessionPrimary (citable) accession number: O88267
Secondary accession number(s): O55161
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: October 13, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents