Reviewed, UniProtKB/Swiss-Prot Q8QZT1 (THIL_MOUSE)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase, mitochondrial
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase

Gene names

Name:

Acat1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Potassium
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI
Molecular function	acetyl-CoA C-acetyltransferase activity Inferred from direct assay. Source: MGI potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion By similarity
	Chain	31 – 424	394	Acetyl-CoA acetyltransferase, mitochondrial		PRO_0000034087
Regions
	Region	255 – 257	3	Coenzyme A binding By similarity
Sites
	Active site	123	1	Acyl-thioester intermediate By similarity
	Active site	382	1	Proton acceptor By similarity
	Active site	410	1	Proton acceptor By similarity
	Metal binding	216	1	Potassium By similarity
	Metal binding	277	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	278	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	280	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	378	1	Potassium; via carbonyl oxygen By similarity
	Binding site	216	1	Coenzyme A By similarity
	Binding site	260	1	Coenzyme A By similarity
	Binding site	281	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	80	1	N6-acetyllysine By similarity
	Modified residue	171	1	N6-acetyllysine Ref.5
	Modified residue	178	1	N6-acetyllysine By similarity
	Modified residue	187	1	N6-acetyllysine Ref.5
	Modified residue	227	1	N6-acetyllysine Ref.5
	Modified residue	248	1	N6-acetyllysine By similarity
	Modified residue	260	1	N6-acetyllysine By similarity
	Modified residue	335	1	N6-acetyllysine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8QZT1-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 0F75A820E992BFD9	FASTA	424	44,816
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171; LYS-187; LYS-227 AND LYS-335, MASS SPECTROMETRY. 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.
IPI	IPI00154054.
RefSeq	NP_659033.1.
UniGene	Mm.293233
3D structure databases
SMR	Q8QZT1. Positions 32-424.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8QZT1.
PTM databases
PhosphoSite	Q8QZT1.
2-D gel databases
REPRODUCTION-2DPAGE	Q8QZT1.
Proteomic databases
PRIDE	Q8QZT1.
Genome annotation databases
Ensembl	ENSMUST00000034547; ENSMUSP00000034547; ENSMUSG00000032047; Mus musculus. [Genome view]
GeneID	110446.
KEGG	mmu:110446.
UCSC	uc009pmg.1. mouse.
Organism-specific databases
CTD	110446.
MGI	MGI:87870. Acat1.
Phylogenomic databases
eggNOG	roNOG09735.
HOGENOM	HBG370930.
HOVERGEN	Q8QZT1.
InParanoid	Q8QZT1.
OMA	MSRGATP.
OrthoDB	EOG9B5RR3.
PhylomeDB	Q8QZT1.
Enzyme and pathway databases
BRENDA	2.3.1.9. 244.
Gene expression databases
ArrayExpress	Q8QZT1.
Bgee	Q8QZT1.
CleanEx	MM_ACAT1.
Genevestigator	Q8QZT1.
GermOnline	ENSMUSG00000032047. Mus musculus.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	363999.
SOURCE	Search...

Entry information

Entry name

THIL_MOUSE

Accession

Primary (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:	February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)