Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)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

  1. acetyl-CoA C-acetyltransferase activity Source: RGD
  2. coenzyme binding Source: RGD
  3. enzyme binding Source: RGD
  4. metal ion binding Source: UniProtKB-KW
  5. protein homodimerization activity Source: RGD

GO - Biological processi

  1. adipose tissue development Source: RGD
  2. brain development Source: RGD
  3. liver development Source: RGD
  4. metanephric proximal convoluted tubule development Source: RGD
  5. protein homooligomerization Source: RGD
  6. response to hormone Source: RGD
  7. response to organic cyclic compound Source: RGD
  8. response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiREACT_203677. Synthesis of Ketone Bodies.
REACT_215799. Utilization of Ketone Bodies.
REACT_221218. Branched-chain amino acid catabolism.
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
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi2016. Acat1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: RGD
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
BLAST
Chaini31 – 424394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000034088Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP17764.
PRIDEiP17764.

PTM databases

PhosphoSiteiP17764.

Expressioni

Gene expression databases

GenevestigatoriP17764.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP17764.
SMRiP17764. 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

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP17764.
KOiK00626.
OMAiMFTTAPV.
OrthoDBiEOG7JQBNG.
PhylomeDBiP17764.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
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.
SMRiP17764. Positions 32-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP17764.
GuidetoPHARMACOLOGYi2435.

PTM databases

PhosphoSiteiP17764.

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

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP17764.
KOiK00626.
OMAiMFTTAPV.
OrthoDBiEOG7JQBNG.
PhylomeDBiP17764.
TreeFamiTF300650.

Enzyme and pathway databases

ReactomeiREACT_203677. Synthesis of Ketone Bodies.
REACT_215799. Utilization of Ketone Bodies.
REACT_221218. Branched-chain amino acid catabolism.
SABIO-RKP17764.

Miscellaneous databases

NextBioi605101.
PROiP17764.

Gene expression databases

GenevestigatoriP17764.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
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...

Publicationsi

  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.

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: January 7, 2015
This is version 126 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

External Data

Dasty 3

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 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.