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Q8QZT1

- THIL_MOUSE

UniProt

Q8QZT1 - THIL_MOUSE

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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene
Acat1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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: 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

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: Chromosome 9

Organism-specific databases

MGIiMGI:87870. Acat1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial matrix Source: Ensembl
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion By 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 SIRT5.1 Publication

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.

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.
InParanoidiQ8QZT1.
KOiK00626.
OMAiDQVAIWE.
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

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MAALVALHGV VRRPLLRGLL QEVRCLERSY ASKPTLNEVV IVSAIRTPIG    50
SFLGSLASQP ATKLGTAAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP 100
TRQATLGAGL PISTPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM 150
ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK 200
MNISRQEQDT YALSSYTRSK EAWDAGKFAS EITPITISVK GKPDVVVKED 250
EEYKRVDFSK VPKLKTVFQK ENGTITAANA STLNDGAAAL VLMTAEAAQR 300
LNVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN 350
EAFSVVVLAN IKMLEIDPQK VNIHGGAVSL GHPIGMSGAR IVVHMAHALK 400
PGEFGLASIC NGGGGASALL IEKL 424
Length:424
Mass (Da):44,816
Last modified:June 1, 2002 - v1
Checksum:i0F75A820E992BFD9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23184.1.
RefSeqi NP_659033.1. NM_144784.3.
UniGenei Mm.293233.

3D structure databases

ProteinModelPortali Q8QZT1.
SMRi Q8QZT1. Positions 32-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225601. 1 interaction.
IntActi Q8QZT1. 6 interactions.
MINTi MINT-1840908.

Chemistry

BindingDBi Q8QZT1.

PTM databases

PhosphoSitei Q8QZT1.

2D gel databases

REPRODUCTION-2DPAGE Q8QZT1.

Proteomic databases

MaxQBi Q8QZT1.
PaxDbi Q8QZT1.
PRIDEi Q8QZT1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034547 ; ENSMUSP00000034547 ; ENSMUSG00000032047 .
GeneIDi 110446.
KEGGi mmu:110446.
UCSCi uc009pmg.1. mouse.

Organism-specific databases

CTDi 38.
MGIi MGI:87870. Acat1.

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00390000009412.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
InParanoidi Q8QZT1.
KOi K00626.
OMAi DQVAIWE.
OrthoDBi EOG7JQBNG.
PhylomeDBi Q8QZT1.
TreeFami TF300650.

Miscellaneous databases

ChiTaRSi ACAT1. mouse.
NextBioi 363999.
PROi Q8QZT1.
SOURCEi Search...

Gene expression databases

Bgeei Q8QZT1.
CleanExi MM_ACAT1.
Genevestigatori Q8QZT1.

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

« Hide 'large scale' publications
  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.
    , 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, 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(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.

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: July 9, 2014
This is version 100 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