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Q8BWT1 (THIM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 residue251N6-acetyllysine; alternate Ref.6
Modified residue251N6-succinyllysine; alternate Ref.5
Modified residue281Phosphoserine Ref.4
Modified residue451N6-succinyllysine Ref.5
Modified residue1191Phosphothreonine By similarity
Modified residue1211Phosphoserine By similarity
Modified residue1271Phosphotyrosine By similarity
Modified residue1371N6-acetyllysine; alternate Ref.6
Modified residue1371N6-succinyllysine; alternate Ref.5
Modified residue1431N6-acetyllysine; alternate Ref.6
Modified residue1431N6-succinyllysine; alternate Ref.5
Modified residue1581N6-acetyllysine; alternate Ref.6
Modified residue1581N6-succinyllysine; alternate Ref.5
Modified residue1711N6-acetyllysine; alternate Ref.6
Modified residue1711N6-succinyllysine; alternate Ref.5
Modified residue1911N6-acetyllysine; alternate Ref.5 Ref.6
Modified residue1911N6-succinyllysine; alternate Ref.5
Modified residue2091N6-acetyllysine; alternate Ref.6
Modified residue2091N6-succinyllysine; alternate Ref.5
Modified residue2111N6-succinyllysine Ref.5
Modified residue2121N6-succinyllysine Ref.5
Modified residue2141N6-succinyllysine Ref.5
Modified residue2341N6-acetyllysine; alternate Ref.6
Modified residue2341N6-succinyllysine; alternate Ref.5
Modified residue2401N6-succinyllysine Ref.5
Modified residue2411N6-acetyllysine Ref.6
Modified residue2691N6-acetyllysine Ref.6
Modified residue2701N6-acetyllysine Ref.6
Modified residue3051N6-acetyllysine; alternate Ref.6
Modified residue3051N6-succinyllysine; alternate Ref.5
Modified residue3121N6-acetyllysine; alternate Ref.6
Modified residue3121N6-succinyllysine; alternate Ref.5
Modified residue3401N6-acetyllysine Ref.6
Modified residue3751N6-acetyllysine Ref.6

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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-45; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-211; LYS-212; LYS-214; LYS-234; LYS-240; LYS-305 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-234; LYS-241; LYS-269; LYS-270; LYS-305; LYS-312; LYS-340 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS29342.1.
RefSeqNP_803421.1. NM_177470.3.
UniGeneMm.245724.

3D structure databases

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

Protein-protein interaction databases

BioGrid206649. 3 interactions.
IntActQ8BWT1. 9 interactions.
MINTMINT-1839761.

PTM databases

PhosphoSiteQ8BWT1.

2D gel databases

REPRODUCTION-2DPAGEQ8BWT1.

Proteomic databases

MaxQBQ8BWT1.
PaxDbQ8BWT1.
PRIDEQ8BWT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041053; ENSMUSP00000037348; ENSMUSG00000036880.
GeneID52538.
KEGGmmu:52538.
UCSCuc008fpt.1. mouse.

Organism-specific databases

CTD10449.
MGIMGI:1098623. Acaa2.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidQ3TIT9.
KOK07508.
OMAQTLACAD.
OrthoDBEOG7JQBNG.
TreeFamTF105696.

Enzyme and pathway databases

UniPathwayUPA00199.

Gene expression databases

BgeeQ8BWT1.
GenevestigatorQ8BWT1.

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]
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.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio309107.
PROQ8BWT1.
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: July 9, 2014
This is version 93 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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