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Reviewed, UniProtKB/Swiss-Prot P13437 (THIM_RAT)

Last modified February 9, 2010. Version 80. 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:
    3-ketoacyl-CoA thiolase, mitochondrial
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Mitochondrial 3-oxoacyl-CoA thiolase
Gene names
Name: Acaa2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

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

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General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the thiolase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix Ref.1

Non-traceable author statement. Source: RGD

   Molecular functionacetyl-CoA C-acyltransferase 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 – 3973973-ketoacyl-CoA thiolase, mitochondrial
PRO_0000223301
Transit peptide1 – 1616Mitochondrion; not cleaved

Sites

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

Amino acid modifications

Modified residue251N6-acetyllysine By similarity
Modified residue1191Phosphothreonine By similarity
Modified residue1211Phosphoserine By similarity
Modified residue1271Phosphotyrosine By similarity
Modified residue1371N6-acetyllysine By similarity
Modified residue2701N6-acetyllysine By similarity
Modified residue3441Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P13437-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 8344FB7271C3E2E1

FASTA39741,871
        10         20         30         40         50         60 
MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET IDSVIVGNVM 

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

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

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

       250        260        270        280        290        300 
KEGTVTAGNA SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI 

       310        320        330        340        350        360 
TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL GHPLGGSGSR 

       370        380        390 
ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA

« Hide

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References

[1]"cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme."
Arakawa H., Takiguchi M., Amaya Y., Nagata S., Hayashi H., Mori M.
EMBO J. 6:1361-1366(1987) [PubMed: 3038520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X05341 mRNA. Translation: CAA28952.1.
IPIIPI00201413.
PIRXURT. A29452.
RefSeqNP_569117.1.
UniGeneRn.3786

3D structure databases

SMRP13437. Positions 6-395.
ModBaseSearch...

Protein-protein interaction databases

STRINGP13437.

2-D gel databases

Rat-heart-2DPAGEP13437.

Proteomic databases

PRIDEP13437.

Genome annotation databases

EnsemblENSRNOT00000064093; ENSRNOP00000062458; ENSRNOG00000013766; Rattus norvegicus. [Genome view]
ENSRNOT00000067018; ENSRNOP00000060140; ENSRNOG00000013766; Rattus norvegicus. [Genome view]
GeneID170465.
KEGGrno:170465.
UCSCNM_130433. rat.

Organism-specific databases

CTD170465.
RGD620482. Acaa2.

Phylogenomic databases

eggNOGroNOG15520.
HOVERGENP13437.
InParanoidP13437.

Enzyme and pathway databases

BRENDA2.3.1.16. 248.

Gene expression databases

ArrayExpressP13437.
GenevestigatorP13437.
GermOnlineENSRNOG00000013766. Rattus norvegicus.

Family and domain databases

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

Other Resources

NextBio620987.

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Entry information

Entry nameTHIM_RAT
AccessionPrimary (citable) accession number: P13437
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 9, 2010
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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