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Reviewed, UniProtKB/Swiss-Prot Q8CAY6 (THIC_MOUSE)

Last modified November 3, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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 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

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Sequences

Sequence LengthMass (Da)Tools
Q8CAY6-1 [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

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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: 16141072] [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: 15489334] [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: 2055458] [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, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00228253.
PIRA53174.
RefSeqNP_033364.2.
UniGeneMm.439711

3D structure databases

HSSPHSSP built from PDB template 1M4T based on UniProtKB P07097.
SMRQ8CAY6. Positions 4-396.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CAY6.

2-D gel databases

REPRODUCTION-2DPAGEQ8CAY6.

Proteomic databases

PRIDEQ8CAY6.

Genome annotation databases

EnsemblENSMUST00000007005; ENSMUSP00000007005; ENSMUSG00000023832; Mus musculus. [Genome view]
GeneID110460.
KEGGmmu:110460.
NMPDRfig|10090.3.peg.26342.
UCSCuc008alp.1. mouse.

Organism-specific databases

CTD110460.
MGIMGI:87871. Acat2.

Phylogenomic databases

HOGENOMQ8CAY6.
HOVERGENQ8CAY6.
OMAVKIGEMP.

Enzyme and pathway databases

BRENDA2.3.1.9. 244.

Gene expression databases

ArrayExpressQ8CAY6.
BgeeQ8CAY6.
CleanExMM_ACAT2.
GenevestigatorQ8CAY6.
GermOnlineENSMUSG00000062480. Mus musculus.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. False negative.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio364019.
SOURCESearch...

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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: November 3, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents