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Q8CAY6 (THIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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, cytosolic

EC=2.3.1.9
Alternative name(s):
Cytosolic acetoacetyl-CoA thiolase
Gene names
Name:Acat2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the thiolase family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Acetyl-CoA acetyltransferase, cytosolic
PRO_0000206410

Sites

Active site921Acyl-thioester intermediate By similarity
Active site3531Proton acceptor By similarity
Active site3831Proton acceptor By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2001N6-acetyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue2351N6-acetyllysine By similarity

Experimental info

Sequence conflict1061I → L in AAH12496. Ref.2
Sequence conflict115 – 1195VAGGM → CLTGK Ref.3
Sequence conflict1251A → P in AAA76575. Ref.3
Sequence conflict1911H → T in AAA76575. Ref.3
Sequence conflict2301A → D in BAB28763. Ref.1
Sequence conflict2331K → T in AAA76575. Ref.3
Sequence conflict2621V → L in BAB28763. Ref.1
Sequence conflict2661K → E in BAC29776. Ref.1
Sequence conflict3401E → G in AAA76575. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8CAY6 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: AABC2DF22F4EE930

FASTA39741,298
        10         20         30         40         50         60 
MNAGSDPVVI VSAARTAIGS FNGALSTVPV HEMGTTVIKE VLQRAKVAPE EVSEVIFGHV 

        70         80         90        100        110        120 
LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAAQSIAMGD STIVVAGGME 

       130        140        150        160        170        180 
NMSKAPHLTH LRTGVRMGEV PLADSILCDG LTDAFHNYHM GITAENVAKK WQVSREAQDK 

       190        200        210        220        230        240 
VAVLSQNRAE HAQKAGHFDK EIVPVLVSSR KGLTEVKIDE FPRHGSNLEA MGKLKPYFLT 

       250        260        270        280        290        300 
DGTGTVTPAN ASGMNDGAAA VVLMKKTEAE RRMLKPLARI VSWSQAGVEP SVMGVGPIPA 

       310        320        330        340        350        360 
IKQAVAKAGW SLEDVDLFEI NEAFAAVSAA IAKELGLNPE KVNIDGGAIA LGHPLGASGC 

       370        380        390 
RILVTLLHTL ERVGGTRGVA ALCIGGGMGV AMCVQRG 

« Hide

References

« Hide 'large scale' references
[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. 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.
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(2004) [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(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-397.
Strain: C57BL/6J.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 342-372, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37437.1.
PIRA53174.
RefSeqNP_033364.2. NM_009338.3.
UniGeneMm.439711.

3D structure databases

ProteinModelPortalQ8CAY6.
SMRQ8CAY6. Positions 4-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CAY6. 2 interactions.
MINTMINT-1864806.

PTM databases

PhosphoSiteQ8CAY6.

2D gel databases

REPRODUCTION-2DPAGEQ8CAY6.

Proteomic databases

MaxQBQ8CAY6.
PaxDbQ8CAY6.
PRIDEQ8CAY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007005; ENSMUSP00000007005; ENSMUSG00000023832.
GeneID110460.
KEGGmmu:110460.
UCSCuc008alp.1. mouse.

Organism-specific databases

CTD39.
MGIMGI:87871. Acat2.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidQ8CAY6.
KOK00626.
OMAKRCLSRA.
OrthoDBEOG7JQBNG.
PhylomeDBQ8CAY6.
TreeFamTF300650.

Gene expression databases

ArrayExpressQ8CAY6.
BgeeQ8CAY6.
CleanExMM_ACAT2.
GenevestigatorQ8CAY6.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
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.
PROSITEPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio364019.
PROQ8CAY6.
SOURCESearch...

Entry information

Entry nameTHIC_MOUSE
AccessionPrimary (citable) accession number: Q8CAY6
Secondary accession number(s): Q3TJY7 expand/collapse secondary AC list , Q62292, Q96EB7, Q99K88, Q9CYV2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 100 of the entry and version 2 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