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P17764

- THIL_RAT

UniProt

P17764 - THIL_RAT

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Protein
Acetyl-CoA acetyltransferase, mitochondrial
Gene
Acat1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231Acyl-thioester intermediate By similarity
Metal bindingi216 – 2161Potassium By similarity
Binding sitei216 – 2161Coenzyme A By similarity
Binding sitei260 – 2601Coenzyme A By similarity
Metal bindingi277 – 2771Potassium; via carbonyl oxygen By similarity
Metal bindingi278 – 2781Potassium; via carbonyl oxygen By similarity
Metal bindingi280 – 2801Potassium; via carbonyl oxygen By similarity
Binding sitei281 – 2811Coenzyme A By similarity
Metal bindingi378 – 3781Potassium; via carbonyl oxygen By similarity
Active sitei382 – 3821Proton acceptor By similarity
Active sitei410 – 4101Proton acceptor By similarity

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. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: RGD
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 Publication
Add
BLAST
Chaini31 – 424394Acetyl-CoA acetyltransferase, mitochondrial
PRO_0000034088Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP17764.
KOiK00626.
OMAiSNVPYTM.
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

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MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG    50
SFLGSLASQP ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP 100
TRQATLGAGL PIATPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM 150
ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK 200
LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK GKPDVVVKED 250
EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR 300
LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN 350
EAFSVVVLAN IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK 400
QGEFGLASIC NGGGGASAVL IEKL 424
Length:424
Mass (Da):44,695
Last modified:August 1, 1990 - v1
Checksum:i79E8881DB242EFEE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D00512 mRNA. Translation: BAA00401.1 . Sequence problems.
D13921 mRNA. Translation: BAA03016.1 .
PIRi JU0072. XXRTAC.
RefSeqi NP_058771.2. NM_017075.2.
UniGenei Rn.4054.

3D structure databases

ProteinModelPortali P17764.
SMRi P17764. Positions 32-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P17764. 3 interactions.
MINTi MINT-4588676.
STRINGi 10116.ENSRNOP00000010573.

Chemistry

BindingDBi P17764.
GuidetoPHARMACOLOGYi 2435.

PTM databases

PhosphoSitei P17764.

Proteomic databases

PaxDbi P17764.
PRIDEi P17764.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010573 ; ENSRNOP00000010573 ; ENSRNOG00000007862 .
GeneIDi 25014.
KEGGi rno:25014.
UCSCi RGD:2016. rat.

Organism-specific databases

CTDi 38.
RGDi 2016. Acat1.

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00390000009412.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
InParanoidi P17764.
KOi K00626.
OMAi SNVPYTM.
OrthoDBi EOG7JQBNG.
PhylomeDBi P17764.
TreeFami TF300650.

Enzyme and pathway databases

Reactomei REACT_203677. Synthesis of Ketone Bodies.
REACT_215799. Utilization of Ketone Bodies.
REACT_221218. Branched-chain amino acid catabolism.
SABIO-RK P17764.

Miscellaneous databases

NextBioi 605101.
PROi P17764.

Gene expression databases

Genevestigatori P17764.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. 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 ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 123 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

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