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Q8BWT1 (THIM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase, mitochondrial
EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Mitochondrial 3-oxoacyl-CoA thiolase
Gene names
Name:Acaa2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

Function

Abolishes BNIP3-mediated apoptosis and mitochondrial damage By similarity.

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homotetramer. Interacts with BNIP3 By similarity.

Subcellular location

Mitochondrion By similarity. Note: Colocalizes with BNIP3 in the mitochondria By similarity.

Sequence similarities

Belongs to the thiolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3973973-ketoacyl-CoA thiolase, mitochondrial
PRO_0000223300
Transit peptide1 – 1616Mitochondrion; not cleaved By similarity

Sites

Active site921Acyl-thioester intermediate By similarity
Active site3521Proton acceptor By similarity
Active site3821Proton acceptor By similarity

Amino acid modifications

Modified residue1191Phosphothreonine By similarity
Modified residue1211Phosphoserine By similarity
Modified residue1271Phosphotyrosine By similarity
Modified residue1371N6-acetyllysine Ref.4
Modified residue2701N6-acetyllysine Ref.4
Modified residue3441Phosphoserine Ref.5

Experimental info

Sequence conflict3971A → V in AAH28901. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BWT1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 856840546F5CB8DA

FASTA39741,830
        10         20         30         40         50         60 
MALLRGVFIV AAKRTPFGAY GGLLKDFSAT DLTEFAARAA LSAGKVPPET IDSVIVGNVM 

        70         80         90        100        110        120 
QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV SGCQEICSKD AEVVLCGGTE 

       130        140        150        160        170        180 
SMSQSPYCVR NVRFGTKFGL DLKLEDTLWA GLTDQHVKLP MGMTAENLAA KYNISREDCD 

       190        200        210        220        230        240 
RYALQSQQRW KAANEAGYFN EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPSVFK 

       250        260        270        280        290        300 
KDGTVTAGNA SGVSDGAGAV IIASEDAVKK HNFTPLARVV GYFVSGCDPT IMGIGPVPAI 

       310        320        330        340        350        360 
NGALKKAGLS LKDMDLIDVN EAFAPQFLSV QKALDLDPSK TNVSGGAIAL GHPLGGSGSR 

       370        380        390 
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA LIIQNTA

« Hide

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: Amnion, Heart and Liver.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Strain: FVB/N.
Tissue: Liver.
[4]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-270, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK050101 mRNA. Translation: BAC34067.1.
AK167567 mRNA. Translation: BAE39630.1.
AK167715 mRNA. Translation: BAE39757.1.
AK169359 mRNA. Translation: BAE41108.1.
CH466528 Genomic DNA. Translation: EDL09521.1.
BC028901 mRNA. Translation: AAH28901.1.
IPIIPI00226430.
RefSeqNP_803421.1. NM_177470.3.
UniGeneMm.245724.

3D structure databases

ProteinModelPortalQ8BWT1.
SMRQ8BWT1. Positions 4-393.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8BWT1. 4 interactions.

PTM databases

PhosphoSiteQ8BWT1.

2D gel databases

REPRODUCTION-2DPAGEQ8BWT1.

Proteomic databases

PaxDbQ8BWT1.
PRIDEQ8BWT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041053; ENSMUSP00000037348; ENSMUSG00000036880.
GeneID52538.
KEGGmmu:52538.

Organism-specific databases

CTD10449.
MGIMGI:1098623. Acaa2.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidQ3TIT9.
KOK07508.
OMAMSQSPYC.
OrthoDBEOG4H19VX.

Enzyme and pathway databases

UniPathwayUPA00199.

Gene expression databases

BgeeQ8BWT1.
GenevestigatorQ8BWT1.
GermOnlineENSMUSG00000036880. Mus musculus.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. 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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio309107.
SOURCESearch...

Entry information

Entry nameTHIM_MOUSE
AccessionPrimary (citable) accession number: Q8BWT1
Secondary accession number(s): Q3TIT9, Q8JZR8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents