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Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene

Acat2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei353 – 3531Proton acceptorPROSITE-ProRule annotation
Active sitei383 – 3831Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA C-acetyltransferase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, cytosolic (EC:2.3.1.9)
Alternative name(s):
Cytosolic acetoacetyl-CoA thiolase
Gene namesi
Name:Acat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:87871. Acat2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrion Source: MGI
  4. nucleolus Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Acetyl-CoA acetyltransferase, cytosolicPRO_0000206410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei200 – 2001N6-acetyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei235 – 2351N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CAY6.
PaxDbiQ8CAY6.
PRIDEiQ8CAY6.

2D gel databases

REPRODUCTION-2DPAGEQ8CAY6.

PTM databases

PhosphoSiteiQ8CAY6.

Expressioni

Gene expression databases

BgeeiQ8CAY6.
CleanExiMM_ACAT2.
ExpressionAtlasiQ8CAY6. baseline and differential.
GenevestigatoriQ8CAY6.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ8CAY6. 2 interactions.
MINTiMINT-1864806.

Structurei

3D structure databases

ProteinModelPortaliQ8CAY6.
SMRiQ8CAY6. Positions 4-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8CAY6.
KOiK00626.
OMAiRTGQRMG.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ8CAY6.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CAY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAGSDPVVI VSAARTAIGS FNGALSTVPV HEMGTTVIKE VLQRAKVAPE
60 70 80 90 100
EVSEVIFGHV LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC
110 120 130 140 150
LAAQSIAMGD STIVVAGGME NMSKAPHLTH LRTGVRMGEV PLADSILCDG
160 170 180 190 200
LTDAFHNYHM GITAENVAKK WQVSREAQDK VAVLSQNRAE HAQKAGHFDK
210 220 230 240 250
EIVPVLVSSR KGLTEVKIDE FPRHGSNLEA MGKLKPYFLT DGTGTVTPAN
260 270 280 290 300
ASGMNDGAAA VVLMKKTEAE RRMLKPLARI VSWSQAGVEP SVMGVGPIPA
310 320 330 340 350
IKQAVAKAGW SLEDVDLFEI NEAFAAVSAA IAKELGLNPE KVNIDGGAIA
360 370 380 390
LGHPLGASGC RILVTLLHTL ERVGGTRGVA ALCIGGGMGV AMCVQRG
Length:397
Mass (Da):41,298
Last modified:September 12, 2004 - v2
Checksum:iAABC2DF22F4EE930
GO

Sequence cautioni

The sequence BAB28763.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061I → L in AAH12496 (PubMed:15489334).Curated
Sequence conflicti115 – 1195VAGGM → CLTGK (PubMed:2055458).Curated
Sequence conflicti125 – 1251A → P in AAA76575 (PubMed:2055458).Curated
Sequence conflicti191 – 1911H → T in AAA76575 (PubMed:2055458).Curated
Sequence conflicti230 – 2301A → D in BAB28763 (PubMed:16141072).Curated
Sequence conflicti233 – 2331K → T in AAA76575 (PubMed:2055458).Curated
Sequence conflicti262 – 2621V → L in BAB28763 (PubMed:16141072).Curated
Sequence conflicti266 – 2661K → E in BAC29776 (PubMed:16141072).Curated
Sequence conflicti340 – 3401E → G in AAA76575 (PubMed:2055458).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013275 mRNA. Translation: BAB28763.1. Different initiation.
AK037249 mRNA. Translation: BAC29776.1.
AK166813 mRNA. Translation: BAE39040.1.
AK167234 mRNA. Translation: BAE39358.1.
BC004823 mRNA. Translation: AAH04823.2.
BC012496 mRNA. Translation: AAH12496.2.
M35797 mRNA. Translation: AAA76575.1.
CCDSiCCDS37437.1.
PIRiA53174.
RefSeqiNP_033364.2. NM_009338.3.
UniGeneiMm.439711.

Genome annotation databases

EnsembliENSMUST00000007005; ENSMUSP00000007005; ENSMUSG00000023832.
GeneIDi110460.
KEGGimmu:110460.
UCSCiuc008alp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013275 mRNA. Translation: BAB28763.1. Different initiation.
AK037249 mRNA. Translation: BAC29776.1.
AK166813 mRNA. Translation: BAE39040.1.
AK167234 mRNA. Translation: BAE39358.1.
BC004823 mRNA. Translation: AAH04823.2.
BC012496 mRNA. Translation: AAH12496.2.
M35797 mRNA. Translation: AAA76575.1.
CCDSiCCDS37437.1.
PIRiA53174.
RefSeqiNP_033364.2. NM_009338.3.
UniGeneiMm.439711.

3D structure databases

ProteinModelPortaliQ8CAY6.
SMRiQ8CAY6. Positions 4-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CAY6. 2 interactions.
MINTiMINT-1864806.

PTM databases

PhosphoSiteiQ8CAY6.

2D gel databases

REPRODUCTION-2DPAGEQ8CAY6.

Proteomic databases

MaxQBiQ8CAY6.
PaxDbiQ8CAY6.
PRIDEiQ8CAY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007005; ENSMUSP00000007005; ENSMUSG00000023832.
GeneIDi110460.
KEGGimmu:110460.
UCSCiuc008alp.1. mouse.

Organism-specific databases

CTDi39.
MGIiMGI:87871. Acat2.

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8CAY6.
KOiK00626.
OMAiRTGQRMG.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ8CAY6.
TreeFamiTF300650.

Miscellaneous databases

NextBioi364019.
PROiQ8CAY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CAY6.
CleanExiMM_ACAT2.
ExpressionAtlasiQ8CAY6. baseline and differential.
GenevestigatoriQ8CAY6.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
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.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    Tissue: Blastocyst, Embryo and Skin.
  2. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Mammary gland and Retina.
  3. "Isolation and characterization of a cDNA clone corresponding to the mouse T-complex gene Tcp-1x."
    Dudley K., Shanahan F., Burtenshaw M., Evans E.P., Ruddy S., Lyon M.F.
    Genet. Res. 57:147-152(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-397.
    Strain: C57BL/6J.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 342-372, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiTHIC_MOUSE
AccessioniPrimary (citable) accession number: Q8CAY6
Secondary accession number(s): Q3TJY7
, Q62292, Q96EB7, Q99K88, Q9CYV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 12, 2004
Last sequence update: September 12, 2004
Last modified: March 3, 2015
This is version 105 of the entry and version 2 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.