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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

Acat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role in ketone body metabolism.

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei123Acyl-thioester intermediateBy similarity1
Metal bindingi216PotassiumBy similarity1
Binding sitei216Coenzyme ABy similarity1
Binding sitei260Coenzyme ABy similarity1
Metal bindingi277Potassium; via carbonyl oxygenBy similarity1
Metal bindingi278Potassium; via carbonyl oxygenBy similarity1
Metal bindingi280Potassium; via carbonyl oxygenBy similarity1
Binding sitei281Coenzyme ABy similarity1
Metal bindingi378Potassium; via carbonyl oxygenBy similarity1
Active sitei382Proton acceptorPROSITE-ProRule annotation1
Active sitei410Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • acetyl-CoA C-acetyltransferase activity Source: RGD
  • coenzyme binding Source: RGD
  • enzyme binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • adipose tissue development Source: RGD
  • brain development Source: RGD
  • fatty acid beta-oxidation Source: GO_Central
  • liver development Source: RGD
  • metanephric proximal convoluted tubule development Source: RGD
  • protein homooligomerization Source: RGD
  • response to hormone Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-RNO-70895. Branched-chain amino acid catabolism.
R-RNO-77108. Utilization of Ketone Bodies.
R-RNO-77111. Synthesis of Ketone Bodies.
SABIO-RKP17764.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene namesi
Name:Acat1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi2016. Acat1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial matrix Source: RGD
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi2435.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000003408831 – 424Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateBy similarity1
Modified residuei63N6-succinyllysine; alternateBy similarity1
Modified residuei75N6-succinyllysineBy similarity1
Modified residuei171N6-acetyllysine; alternateBy similarity1
Modified residuei171N6-succinyllysine; alternateBy similarity1
Modified residuei178N6-acetyllysine; alternateBy similarity1
Modified residuei178N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysine; alternateBy similarity1
Modified residuei187N6-succinyllysine; alternateBy similarity1
Modified residuei199N6-acetyllysine; alternateBy similarity1
Modified residuei199N6-succinyllysine; alternateBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei220N6-acetyllysine; alternateBy similarity1
Modified residuei220N6-succinyllysine; alternateBy similarity1
Modified residuei227N6-acetyllysine; alternateBy similarity1
Modified residuei227N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-succinyllysineBy similarity1
Modified residuei242N6-acetyllysine; alternateBy similarity1
Modified residuei242N6-succinyllysine; alternateBy similarity1
Modified residuei248N6-acetyllysineBy similarity1
Modified residuei254N6-acetyllysineBy similarity1
Modified residuei260N6-acetyllysine; alternateBy similarity1
Modified residuei260N6-succinyllysine; alternateBy similarity1
Modified residuei263N6-succinyllysineBy similarity1
Modified residuei265N6-succinyllysineBy similarity1
Modified residuei270N6-acetyllysineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP17764.
PRIDEiP17764.

PTM databases

iPTMnetiP17764.
PhosphoSitePlusiP17764.

Expressioni

Gene expression databases

BgeeiENSRNOG00000007862.
GenevisibleiP17764. RN.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • enzyme binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP17764. 3 interactors.
MINTiMINT-4588676.
STRINGi10116.ENSRNOP00000010573.

Structurei

3D structure databases

ProteinModelPortaliP17764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni255 – 257Coenzyme A bindingBy similarity3

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1390. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP17764.
KOiK00626.
OMAiEPIDFPV.
OrthoDBiEOG091G09C6.
PhylomeDBiP17764.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17764-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG
60 70 80 90 100
SFLGSLASQP ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP
110 120 130 140 150
TRQATLGAGL PIATPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM
160 170 180 190 200
ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK
210 220 230 240 250
LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK GKPDVVVKED
260 270 280 290 300
EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR
310 320 330 340 350
LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN
360 370 380 390 400
EAFSVVVLAN IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK
410 420
QGEFGLASIC NGGGGASAVL IEKL
Length:424
Mass (Da):44,695
Last modified:August 1, 1990 - v1
Checksum:i79E8881DB242EFEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00512 mRNA. Translation: BAA00401.1. Sequence problems.
D13921 mRNA. Translation: BAA03016.1.
PIRiJU0072. XXRTAC.
RefSeqiNP_058771.2. NM_017075.2.
UniGeneiRn.4054.

Genome annotation databases

EnsembliENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862.
GeneIDi25014.
KEGGirno:25014.
UCSCiRGD:2016. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00512 mRNA. Translation: BAA00401.1. Sequence problems.
D13921 mRNA. Translation: BAA03016.1.
PIRiJU0072. XXRTAC.
RefSeqiNP_058771.2. NM_017075.2.
UniGeneiRn.4054.

3D structure databases

ProteinModelPortaliP17764.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17764. 3 interactors.
MINTiMINT-4588676.
STRINGi10116.ENSRNOP00000010573.

Chemistry databases

GuidetoPHARMACOLOGYi2435.

PTM databases

iPTMnetiP17764.
PhosphoSitePlusiP17764.

Proteomic databases

PaxDbiP17764.
PRIDEiP17764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862.
GeneIDi25014.
KEGGirno:25014.
UCSCiRGD:2016. rat.

Organism-specific databases

CTDi38.
RGDi2016. Acat1.

Phylogenomic databases

eggNOGiKOG1390. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP17764.
KOiK00626.
OMAiEPIDFPV.
OrthoDBiEOG091G09C6.
PhylomeDBiP17764.
TreeFamiTF300650.

Enzyme and pathway databases

ReactomeiR-RNO-70895. Branched-chain amino acid catabolism.
R-RNO-77108. Utilization of Ketone Bodies.
R-RNO-77111. Synthesis of Ketone Bodies.
SABIO-RKP17764.

Miscellaneous databases

PROiP17764.

Gene expression databases

BgeeiENSRNOG00000007862.
GenevisibleiP17764. RN.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIL_RAT
AccessioniPrimary (citable) accession number: P17764
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 140 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.