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P17764 (THIL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA acetyltransferase, mitochondrial

EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene names
Name:Acat1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a major role in ketone body metabolism.

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Enzyme regulation

Activated by potassium ions, but not sodium ions By similarity.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion.

Post-translational modification

Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Potassium
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadipose tissue development

Inferred from expression pattern PubMed 2866764. Source: RGD

brain development

Inferred from expression pattern PubMed 4721608. Source: RGD

liver development

Inferred from expression pattern PubMed 5166591. Source: RGD

metanephric proximal convoluted tubule development

Inferred from expression pattern PubMed 7733320. Source: RGD

protein homooligomerization

Inferred from direct assay PubMed 11988101. Source: RGD

response to hormone

Inferred from expression pattern PubMed 6144148. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 6489337. Source: RGD

response to starvation

Inferred from expression pattern PubMed 2985752. Source: RGD

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from direct assay PubMed 11988101. Source: RGD

mitochondrion

Inferred from direct assay PubMed 17180682. Source: UniProtKB

   Molecular_functionacetyl-CoA C-acetyltransferase activity

Inferred from direct assay Ref.1. Source: RGD

coenzyme binding

Inferred from physical interaction PubMed 1672610. Source: RGD

enzyme binding

Inferred from physical interaction PubMed 1684101. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay PubMed 11988101. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Ref.1
Chain31 – 424394Acetyl-CoA acetyltransferase, mitochondrial
PRO_0000034088

Regions

Region255 – 2573Coenzyme A binding By similarity

Sites

Active site1231Acyl-thioester intermediate By similarity
Active site3821Proton acceptor By similarity
Active site4101Proton acceptor By similarity
Metal binding2161Potassium By similarity
Metal binding2771Potassium; via carbonyl oxygen By similarity
Metal binding2781Potassium; via carbonyl oxygen By similarity
Metal binding2801Potassium; via carbonyl oxygen By similarity
Metal binding3781Potassium; via carbonyl oxygen By similarity
Binding site2161Coenzyme A By similarity
Binding site2601Coenzyme A By similarity
Binding site2811Coenzyme A By similarity

Amino acid modifications

Modified residue631N6-acetyllysine; alternate By similarity
Modified residue631N6-succinyllysine; alternate By similarity
Modified residue751N6-succinyllysine By similarity
Modified residue1711N6-acetyllysine; alternate By similarity
Modified residue1711N6-succinyllysine; alternate By similarity
Modified residue1781N6-acetyllysine; alternate By similarity
Modified residue1781N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine; alternate By similarity
Modified residue1871N6-succinyllysine; alternate By similarity
Modified residue1991N6-acetyllysine; alternate By similarity
Modified residue1991N6-succinyllysine; alternate By similarity
Modified residue2201N6-acetyllysine; alternate By similarity
Modified residue2201N6-succinyllysine; alternate By similarity
Modified residue2271N6-acetyllysine; alternate By similarity
Modified residue2271N6-succinyllysine; alternate By similarity
Modified residue2401N6-succinyllysine By similarity
Modified residue2421N6-acetyllysine; alternate By similarity
Modified residue2421N6-succinyllysine; alternate By similarity
Modified residue2481N6-acetyllysine By similarity
Modified residue2541N6-acetyllysine By similarity
Modified residue2601N6-acetyllysine; alternate By similarity
Modified residue2601N6-succinyllysine; alternate By similarity
Modified residue2631N6-succinyllysine By similarity
Modified residue2651N6-succinyllysine By similarity
Modified residue2701N6-acetyllysine By similarity
Modified residue3351N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P17764 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 79E8881DB242EFEE

FASTA42444,695
        10         20         30         40         50         60 
MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG SFLGSLASQP 

        70         80         90        100        110        120 
ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP TRQATLGAGL PIATPCTTVN 

       130        140        150        160        170        180 
KVCASGMKAI MMASQSLMCG HQDVMVAGGM ESMSNVPYVM SRGATPYGGV KLEDLIVKDG 

       190        200        210        220        230        240 
LTDVYNKIHM GNCAENTAKK LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK 

       250        260        270        280        290        300 
GKPDVVVKED EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR 

       310        320        330        340        350        360 
LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN EAFSVVVLAN 

       370        380        390        400        410        420 
IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK QGEFGLASIC NGGGGASAVL 


IEKL 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat mitochondrial acetoacetyl-CoA thiolase."
Fukao T., Kamijo K., Osumi T., Fujiki Y., Yamaguchi S., Orii T., Hashimoto T.
J. Biochem. 106:197-204(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00512 mRNA. Translation: BAA00401.1. Sequence problems.
D13921 mRNA. Translation: BAA03016.1.
PIRXXRTAC. JU0072.
RefSeqNP_058771.2. NM_017075.2.
UniGeneRn.4054.

3D structure databases

ProteinModelPortalP17764.
SMRP17764. Positions 32-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17764. 3 interactions.
MINTMINT-4588676.
STRING10116.ENSRNOP00000010573.

Chemistry

BindingDBP17764.
GuidetoPHARMACOLOGY2435.

PTM databases

PhosphoSiteP17764.

Proteomic databases

PaxDbP17764.
PRIDEP17764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862.
GeneID25014.
KEGGrno:25014.
UCSCRGD:2016. rat.

Organism-specific databases

CTD38.
RGD2016. Acat1.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidP17764.
KOK00626.
OMASNVPYTM.
OrthoDBEOG7JQBNG.
PhylomeDBP17764.
TreeFamTF300650.

Enzyme and pathway databases

SABIO-RKP17764.

Gene expression databases

GenevestigatorP17764.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605101.
PROP17764.

Entry information

Entry nameTHIL_RAT
AccessionPrimary (citable) accession number: P17764
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 11, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families