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Reviewed, UniProtKB/Swiss-Prot P17764 (THIL_RAT)

Last modified November 3, 2009. Version 83. 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

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)
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.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Potassium
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionacetyl-CoA C-acetyltransferase activity Ref.1

Inferred from direct assay. Source: RGD

potassium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 residue801N6-acetyllysine By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1781N6-acetyllysine By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue2271N6-acetyllysine By similarity
Modified residue2481N6-acetyllysine By similarity
Modified residue2601N6-acetyllysine By similarity
Modified residue3351N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P17764-1 [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: 2478525] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50.

Cross-references

Sequence databases

D00512 mRNA. Translation: BAA00401.1. Sequence problems.
D13921 mRNA. Translation: BAA03016.1.
IPIIPI00324302.
PIRXXRTAC. JU0072.
RefSeqNP_058771.1.
UniGeneRn.4054

3D structure databases

HSSPHSSP built from PDB template 1M4T based on UniProtKB P07097.
SMRP17764. Positions 32-424.
ModBaseSearch...

Protein-protein interaction databases

STRINGP17764.

PTM databases

PhosphoSiteP17764.

Proteomic databases

PRIDEP17764.

Genome annotation databases

EnsemblENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862; Rattus norvegicus. [Genome view]
GeneID25014.
KEGGrno:25014.
UCSCNM_017075. rat.

Organism-specific databases

CTD25014.
RGD2016. Acat1.

Phylogenomic databases

HOVERGENP17764.
OMAAYAVPKV.

Enzyme and pathway databases

BRENDA2.3.1.9. 248.

Gene expression databases

ArrayExpressP17764.
GenevestigatorP17764.
GermOnlineENSRNOG00000007862. Rattus norvegicus.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
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 Resources

NextBio605101.

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: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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