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Q8QZT1 (THIL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA acetyltransferase, mitochondrial

EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene names
Name:Acat1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a major role in ketone body metabolism By similarity.

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Enzyme regulation

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion By similarity.

Post-translational modification

Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5. Ref.5

Sequence similarities

Belongs to the thiolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 424394Acetyl-CoA acetyltransferase, mitochondrial
PRO_0000034087

Regions

Region255 – 2573Coenzyme A binding By similarity

Sites

Active site1231Acyl-thioester intermediate By similarity
Active site3821Proton acceptor By similarity
Active site4101Proton acceptor By similarity
Metal binding2161Potassium By similarity
Metal binding2771Potassium; via carbonyl oxygen By similarity
Metal binding2781Potassium; via carbonyl oxygen By similarity
Metal binding2801Potassium; via carbonyl oxygen By similarity
Metal binding3781Potassium; via carbonyl oxygen By similarity
Binding site2161Coenzyme A By similarity
Binding site2601Coenzyme A By similarity
Binding site2811Coenzyme A By similarity

Amino acid modifications

Modified residue631N6-acetyllysine; alternate
Modified residue631N6-succinyllysine; alternate
Modified residue751N6-succinyllysine
Modified residue1711N6-acetyllysine; alternate
Modified residue1711N6-succinyllysine; alternate
Modified residue1781N6-acetyllysine; alternate
Modified residue1781N6-succinyllysine; alternate
Modified residue1871N6-acetyllysine; alternate
Modified residue1871N6-succinyllysine; alternate
Modified residue1991N6-acetyllysine; alternate
Modified residue1991N6-succinyllysine; alternate
Modified residue2201N6-acetyllysine; alternate
Modified residue2201N6-succinyllysine; alternate
Modified residue2271N6-acetyllysine; alternate
Modified residue2271N6-succinyllysine; alternate
Modified residue2401N6-succinyllysine
Modified residue2421N6-acetyllysine; alternate
Modified residue2421N6-succinyllysine; alternate
Modified residue2481N6-acetyllysine Ref.6
Modified residue2541N6-acetyllysine Ref.6
Modified residue2601N6-acetyllysine; alternate
Modified residue2601N6-succinyllysine; alternate
Modified residue2631N6-succinyllysine
Modified residue2651N6-succinyllysine
Modified residue2701N6-acetyllysine Ref.6
Modified residue3351N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q8QZT1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 0F75A820E992BFD9

FASTA42444,816
        10         20         30         40         50         60 
MAALVALHGV VRRPLLRGLL QEVRCLERSY ASKPTLNEVV IVSAIRTPIG SFLGSLASQP 

        70         80         90        100        110        120 
ATKLGTAAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP TRQATLGAGL PISTPCTTVN 

       130        140        150        160        170        180 
KVCASGMKAI MMASQSLMCG HQDVMVAGGM ESMSNVPYVM SRGATPYGGV KLEDLIVKDG 

       190        200        210        220        230        240 
LTDVYNKIHM GNCAENTAKK MNISRQEQDT YALSSYTRSK EAWDAGKFAS EITPITISVK 

       250        260        270        280        290        300 
GKPDVVVKED EEYKRVDFSK VPKLKTVFQK ENGTITAANA STLNDGAAAL VLMTAEAAQR 

       310        320        330        340        350        360 
LNVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN EAFSVVVLAN 

       370        380        390        400        410        420 
IKMLEIDPQK VNIHGGAVSL GHPIGMSGAR IVVHMAHALK PGEFGLASIC NGGGGASALL 


IEKL 

« Hide

References

« Hide 'large scale' references
[1]"Species-specific differences in peroxisomal association of acetoacetyl-CoA synthase."
Ghys K., Amery L., Van Veldhoven P.P.
Submitted (OCT-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. expand/collapse author list , 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(2005) [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(2004) [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 (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 47-75; 85-121; 163-171; 179-187; 206-218; 228-254; 271-332 AND 363-390, 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(2013) [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(2013) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_659033.1. NM_144784.3.
UniGeneMm.293233.

3D structure databases

ProteinModelPortalQ8QZT1.
SMRQ8QZT1. Positions 32-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid225601. 1 interaction.
IntActQ8QZT1. 6 interactions.
MINTMINT-1840908.

Chemistry

BindingDBQ8QZT1.
ChEMBLCHEMBL2197.

PTM databases

PhosphoSiteQ8QZT1.

2D gel databases

REPRODUCTION-2DPAGEQ8QZT1.

Proteomic databases

PaxDbQ8QZT1.
PRIDEQ8QZT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034547; ENSMUSP00000034547; ENSMUSG00000032047.
GeneID110446.
KEGGmmu:110446.
UCSCuc009pmg.1. mouse.

Organism-specific databases

CTD38.
MGIMGI:87870. Acat1.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidQ8QZT1.
KOK00626.
OMAMFTTAPV.
OrthoDBEOG7JQBNG.
TreeFamTF300650.

Gene expression databases

BgeeQ8QZT1.
CleanExMM_ACAT1.
GenevestigatorQ8QZT1.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. 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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACAT1. mouse.
NextBio363999.
PROQ8QZT1.
SOURCESearch...

Entry information

Entry nameTHIL_MOUSE
AccessionPrimary (citable) accession number: Q8QZT1
Secondary accession number(s): Q3TE92
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2002
Last modified: March 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot