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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

  1. acetyl-CoA C-acetyltransferase activity Source: MGI
  2. coenzyme binding Source: Ensembl
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiREACT_286913. Synthesis of Ketone Bodies.
REACT_305961. Branched-chain amino acid catabolism.
REACT_331447. Utilization 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
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:87870. Acat1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial matrix Source: Ensembl
  4. 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; alternate1 Publication
Modified residuei63 – 631N6-succinyllysine; alternate1 Publication
Modified residuei75 – 751N6-succinyllysine1 Publication
Modified residuei171 – 1711N6-acetyllysine; alternate2 Publications
Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
Modified residuei178 – 1781N6-acetyllysine; alternate1 Publication
Modified residuei178 – 1781N6-succinyllysine; alternate1 Publication
Modified residuei187 – 1871N6-acetyllysine; alternate1 Publication
Modified residuei187 – 1871N6-succinyllysine; alternate1 Publication
Modified residuei199 – 1991N6-acetyllysine; alternate1 Publication
Modified residuei199 – 1991N6-succinyllysine; alternate1 Publication
Modified residuei220 – 2201N6-acetyllysine; alternate1 Publication
Modified residuei220 – 2201N6-succinyllysine; alternate1 Publication
Modified residuei227 – 2271N6-acetyllysine; alternate1 Publication
Modified residuei227 – 2271N6-succinyllysine; alternate1 Publication
Modified residuei240 – 2401N6-succinyllysine1 Publication
Modified residuei242 – 2421N6-acetyllysine; alternate1 Publication
Modified residuei242 – 2421N6-succinyllysine; alternate1 Publication
Modified residuei248 – 2481N6-acetyllysine1 Publication
Modified residuei254 – 2541N6-acetyllysine1 Publication
Modified residuei260 – 2601N6-acetyllysine; alternate1 Publication
Modified residuei260 – 2601N6-succinyllysine; alternate1 Publication
Modified residuei263 – 2631N6-succinyllysine1 Publication
Modified residuei265 – 2651N6-succinyllysine1 Publication
Modified residuei270 – 2701N6-acetyllysine1 Publication
Modified residuei335 – 3351N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8QZT1.
PaxDbiQ8QZT1.
PRIDEiQ8QZT1.

2D gel databases

REPRODUCTION-2DPAGEQ8QZT1.

PTM databases

PhosphoSiteiQ8QZT1.

Expressioni

Gene expression databases

BgeeiQ8QZT1.
CleanExiMM_ACAT1.
GenevestigatoriQ8QZT1.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi225601. 1 interaction.
IntActiQ8QZT1. 6 interactions.
MINTiMINT-1840908.

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

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8QZT1.
KOiK00626.
OMAiMFTTAPV.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ8QZT1.
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.

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. 1 interaction.
IntActiQ8QZT1. 6 interactions.
MINTiMINT-1840908.

Chemistry

BindingDBiQ8QZT1.

PTM databases

PhosphoSiteiQ8QZT1.

2D gel databases

REPRODUCTION-2DPAGEQ8QZT1.

Proteomic databases

MaxQBiQ8QZT1.
PaxDbiQ8QZT1.
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

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8QZT1.
KOiK00626.
OMAiMFTTAPV.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ8QZT1.
TreeFamiTF300650.

Enzyme and pathway databases

ReactomeiREACT_286913. Synthesis of Ketone Bodies.
REACT_305961. Branched-chain amino acid catabolism.
REACT_331447. Utilization of Ketone Bodies.

Miscellaneous databases

ChiTaRSiAcat1. mouse.
NextBioi363999.
PROiQ8QZT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZT1.
CleanExiMM_ACAT1.
GenevestigatoriQ8QZT1.

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

« Hide 'large scale' publications
  1. "Species-specific differences in peroxisomal association of acetoacetyl-CoA synthase."
    Ghys K., Amery L., Van Veldhoven P.P.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head, Medulla oblongata and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 47-75; 85-121; 163-171; 179-187; 206-218; 228-254; 271-332 AND 363-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-265, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-75; LYS-171; LYS-178; LYS-187; LYS-199; LYS-220; LYS-227; LYS-240; LYS-242; LYS-260; LYS-263 AND LYS-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-171; LYS-178; LYS-187; LYS-199; LYS-220; LYS-227; LYS-242; LYS-248; LYS-254; LYS-260; LYS-270 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: April 1, 2015
This is version 107 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

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.