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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231Acyl-thioester intermediateBy similarity
Metal bindingi216 – 2161PotassiumBy similarity
Binding sitei216 – 2161Coenzyme ABy similarity
Binding sitei260 – 2601Coenzyme ABy similarity
Metal bindingi277 – 2771Potassium; via carbonyl oxygenBy similarity
Metal bindingi278 – 2781Potassium; via carbonyl oxygenBy similarity
Metal bindingi280 – 2801Potassium; via carbonyl oxygenBy similarity
Binding sitei281 – 2811Coenzyme ABy similarity
Metal bindingi378 – 3781Potassium; via carbonyl oxygenBy similarity
Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation
Active sitei410 – 4101Proton acceptorPROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 424394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000034087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-acetyllysine; alternateCombined sources
Modified residuei63 – 631N6-succinyllysine; alternateCombined sources
Modified residuei75 – 751N6-succinyllysineCombined sources
Modified residuei171 – 1711N6-acetyllysine; alternateCombined sources
Modified residuei171 – 1711N6-succinyllysine; alternateCombined sources
Modified residuei178 – 1781N6-acetyllysine; alternateCombined sources
Modified residuei178 – 1781N6-succinyllysine; alternateCombined sources
Modified residuei187 – 1871N6-acetyllysine; alternateCombined sources
Modified residuei187 – 1871N6-succinyllysine; alternateCombined sources
Modified residuei199 – 1991N6-acetyllysine; alternateCombined sources
Modified residuei199 – 1991N6-succinyllysine; alternateCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei220 – 2201N6-acetyllysine; alternateCombined sources
Modified residuei220 – 2201N6-succinyllysine; alternateCombined sources
Modified residuei227 – 2271N6-acetyllysine; alternateCombined sources
Modified residuei227 – 2271N6-succinyllysine; alternateCombined sources
Modified residuei240 – 2401N6-succinyllysineCombined sources
Modified residuei242 – 2421N6-acetyllysine; alternateCombined sources
Modified residuei242 – 2421N6-succinyllysine; alternateCombined sources
Modified residuei248 – 2481N6-acetyllysineCombined sources
Modified residuei254 – 2541N6-acetyllysineCombined sources
Modified residuei260 – 2601N6-acetyllysine; alternateCombined sources
Modified residuei260 – 2601N6-succinyllysine; alternateCombined sources
Modified residuei263 – 2631N6-succinyllysineCombined sources
Modified residuei265 – 2651N6-succinyllysineCombined sources
Modified residuei270 – 2701N6-acetyllysineCombined sources
Modified residuei335 – 3351N6-acetyllysineCombined sources

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.
PhosphoSiteiQ8QZT1.
SwissPalmiQ8QZT1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032047.
CleanExiMM_ACAT1.
GenevisibleiQ8QZT1. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8QZT1.
SMRiQ8QZT1. Positions 32-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 2573Coenzyme A bindingBy similarity

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. Positions 32-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ8QZT1.
PhosphoSiteiQ8QZT1.
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: September 7, 2016
This is version 119 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.