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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

Acat1

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

Functioni

Plays a major role in ketone body metabolism.By similarity

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:87870. Acat1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30MitochondrionBy similarityAdd BLAST30
ChainiPRO_000003408731 – 424Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateCombined sources1
Modified residuei63N6-succinyllysine; alternateCombined sources1
Modified residuei75N6-succinyllysineCombined sources1
Modified residuei171N6-acetyllysine; alternateCombined sources1
Modified residuei171N6-succinyllysine; alternateCombined sources1
Modified residuei178N6-acetyllysine; alternateCombined sources1
Modified residuei178N6-succinyllysine; alternateCombined sources1
Modified residuei187N6-acetyllysine; alternateCombined sources1
Modified residuei187N6-succinyllysine; alternateCombined sources1
Modified residuei199N6-acetyllysine; alternateCombined sources1
Modified residuei199N6-succinyllysine; alternateCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei220N6-acetyllysine; alternateCombined sources1
Modified residuei220N6-succinyllysine; alternateCombined sources1
Modified residuei227N6-acetyllysine; alternateCombined sources1
Modified residuei227N6-succinyllysine; alternateCombined sources1
Modified residuei240N6-succinyllysineCombined sources1
Modified residuei242N6-acetyllysine; alternateCombined sources1
Modified residuei242N6-succinyllysine; alternateCombined sources1
Modified residuei248N6-acetyllysineCombined sources1
Modified residuei254N6-acetyllysineCombined sources1
Modified residuei260N6-acetyllysine; alternateCombined sources1
Modified residuei260N6-succinyllysine; alternateCombined sources1
Modified residuei263N6-succinyllysineCombined sources1
Modified residuei265N6-succinyllysineCombined sources1
Modified residuei270N6-acetyllysineCombined sources1
Modified residuei335N6-acetyllysineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8QZT1.
MaxQBiQ8QZT1.
PaxDbiQ8QZT1.
PeptideAtlasiQ8QZT1.
PRIDEiQ8QZT1.

2D gel databases

REPRODUCTION-2DPAGEQ8QZT1.

PTM databases

iPTMnetiQ8QZT1.
PhosphoSitePlusiQ8QZT1.
SwissPalmiQ8QZT1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032047.
CleanExiMM_ACAT1.
GenevisibleiQ8QZT1. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi225601. 2 interactors.
IntActiQ8QZT1. 6 interactors.
MINTiMINT-1840908.
STRINGi10090.ENSMUSP00000034547.

Structurei

3D structure databases

ProteinModelPortaliQ8QZT1.
SMRiQ8QZT1.
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.
InParanoidiQ8QZT1.
KOiK00626.
OMAiEPIDFPV.
OrthoDBiEOG091G09C6.
PhylomeDBiQ8QZT1.
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.

Q8QZT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALVALHGV VRRPLLRGLL QEVRCLERSY ASKPTLNEVV IVSAIRTPIG
60 70 80 90 100
SFLGSLASQP ATKLGTAAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP
110 120 130 140 150
TRQATLGAGL PISTPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM
160 170 180 190 200
ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK
210 220 230 240 250
MNISRQEQDT YALSSYTRSK EAWDAGKFAS EITPITISVK GKPDVVVKED
260 270 280 290 300
EEYKRVDFSK VPKLKTVFQK ENGTITAANA STLNDGAAAL VLMTAEAAQR
310 320 330 340 350
LNVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN
360 370 380 390 400
EAFSVVVLAN IKMLEIDPQK VNIHGGAVSL GHPIGMSGAR IVVHMAHALK
410 420
PGEFGLASIC NGGGGASALL IEKL
Length:424
Mass (Da):44,816
Last modified:June 1, 2002 - v1
Checksum:i0F75A820E992BFD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ510150 mRNA. Translation: CAD52869.1.
AK032097 mRNA. Translation: BAC27697.1.
AK081715 mRNA. Translation: BAC38304.1.
AK169771 mRNA. Translation: BAE41356.1.
BC024763 mRNA. Translation: AAH24763.1.
CCDSiCCDS23184.1.
RefSeqiNP_659033.1. NM_144784.3.
UniGeneiMm.293233.

Genome annotation databases

EnsembliENSMUST00000034547; ENSMUSP00000034547; ENSMUSG00000032047.
GeneIDi110446.
KEGGimmu:110446.
UCSCiuc009pmg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ510150 mRNA. Translation: CAD52869.1.
AK032097 mRNA. Translation: BAC27697.1.
AK081715 mRNA. Translation: BAC38304.1.
AK169771 mRNA. Translation: BAE41356.1.
BC024763 mRNA. Translation: AAH24763.1.
CCDSiCCDS23184.1.
RefSeqiNP_659033.1. NM_144784.3.
UniGeneiMm.293233.

3D structure databases

ProteinModelPortaliQ8QZT1.
SMRiQ8QZT1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225601. 2 interactors.
IntActiQ8QZT1. 6 interactors.
MINTiMINT-1840908.
STRINGi10090.ENSMUSP00000034547.

PTM databases

iPTMnetiQ8QZT1.
PhosphoSitePlusiQ8QZT1.
SwissPalmiQ8QZT1.

2D gel databases

REPRODUCTION-2DPAGEQ8QZT1.

Proteomic databases

EPDiQ8QZT1.
MaxQBiQ8QZT1.
PaxDbiQ8QZT1.
PeptideAtlasiQ8QZT1.
PRIDEiQ8QZT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034547; ENSMUSP00000034547; ENSMUSG00000032047.
GeneIDi110446.
KEGGimmu:110446.
UCSCiuc009pmg.1. mouse.

Organism-specific databases

CTDi38.
MGIiMGI:87870. Acat1.

Phylogenomic databases

eggNOGiKOG1390. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8QZT1.
KOiK00626.
OMAiEPIDFPV.
OrthoDBiEOG091G09C6.
PhylomeDBiQ8QZT1.
TreeFamiTF300650.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAcat1. mouse.
PROiQ8QZT1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032047.
CleanExiMM_ACAT1.
GenevisibleiQ8QZT1. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q8QZT1
Secondary accession number(s): Q3TE92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 122 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. 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.