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P13437

- THIM_RAT

UniProt

P13437 - THIM_RAT

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Protein
3-ketoacyl-CoA thiolase, mitochondrial
Gene
Acaa2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Abolishes BNIP3-mediated apoptosis and mitochondrial damage By similarity.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediate By similarity
Active sitei352 – 3521Proton acceptor By similarity
Active sitei382 – 3821Proton acceptor By similarity

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: RGD

GO - Biological processi

  1. acetyl-CoA metabolic process Source: RGD
  2. fatty acid beta-oxidation Source: RGD
  3. negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

SABIO-RKP13437.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Acaa2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620482. Acaa2.

Subcellular locationi

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

GO - Cellular componenti

  1. mitochondrial matrix Source: RGD
  2. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrial
PRO_0000223301Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleaved
Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251N6-acetyllysine; alternate By similarity
Modified residuei25 – 251N6-succinyllysine; alternate By similarity
Modified residuei45 – 451N6-succinyllysine By similarity
Modified residuei119 – 1191Phosphothreonine By similarity
Modified residuei121 – 1211Phosphoserine By similarity
Modified residuei127 – 1271Phosphotyrosine By similarity
Modified residuei137 – 1371N6-acetyllysine; alternate By similarity
Modified residuei137 – 1371N6-succinyllysine; alternate By similarity
Modified residuei143 – 1431N6-acetyllysine; alternate By similarity
Modified residuei143 – 1431N6-succinyllysine; alternate By similarity
Modified residuei158 – 1581N6-acetyllysine; alternate By similarity
Modified residuei158 – 1581N6-succinyllysine; alternate By similarity
Modified residuei171 – 1711N6-acetyllysine; alternate By similarity
Modified residuei171 – 1711N6-succinyllysine; alternate By similarity
Modified residuei191 – 1911N6-acetyllysine; alternate By similarity
Modified residuei191 – 1911N6-succinyllysine; alternate By similarity
Modified residuei209 – 2091N6-acetyllysine; alternate By similarity
Modified residuei209 – 2091N6-succinyllysine; alternate By similarity
Modified residuei211 – 2111N6-succinyllysine By similarity
Modified residuei212 – 2121N6-succinyllysine By similarity
Modified residuei214 – 2141N6-succinyllysine By similarity
Modified residuei240 – 2401N6-succinyllysine By similarity
Modified residuei241 – 2411N6-acetyllysine By similarity
Modified residuei269 – 2691N6-acetyllysine By similarity
Modified residuei270 – 2701N6-acetyllysine By similarity
Modified residuei305 – 3051N6-acetyllysine; alternate By similarity
Modified residuei305 – 3051N6-succinyllysine; alternate By similarity
Modified residuei312 – 3121N6-acetyllysine; alternate By similarity
Modified residuei312 – 3121N6-succinyllysine; alternate By similarity
Modified residuei340 – 3401N6-acetyllysine By similarity
Modified residuei375 – 3751N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP13437.
PRIDEiP13437.

Expressioni

Gene expression databases

GenevestigatoriP13437.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3 By similarity.

Protein-protein interaction databases

IntActiP13437. 1 interaction.
STRINGi10116.ENSRNOP00000060140.

Structurei

3D structure databases

ProteinModelPortaliP13437.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP13437.
KOiK07508.
PhylomeDBiP13437.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13437-1 [UniParc]FASTAAdd to Basket

« Hide

MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET    50
IDSVIVGNVM QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV 100
SGCQEICSKD AEVVLCGGTE SMSQSPYSVR NVRFGTKFGL DLKLEDTLWA 150
GLTDQHVKLP MGMTAENLAA KYNISREDCD RYALQSQQRW KAANEAGYFN 200
EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQNLPPVFK KEGTVTAGNA 250
SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI 300
TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL 350
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA 397
Length:397
Mass (Da):41,871
Last modified:January 1, 1990 - v1
Checksum:i8344FB7271C3E2E1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05341 mRNA. Translation: CAA28952.1.
PIRiA29452. XURT.
RefSeqiNP_569117.1. NM_130433.1.
UniGeneiRn.3786.

Genome annotation databases

GeneIDi170465.
KEGGirno:170465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05341 mRNA. Translation: CAA28952.1 .
PIRi A29452. XURT.
RefSeqi NP_569117.1. NM_130433.1.
UniGenei Rn.3786.

3D structure databases

ProteinModelPortali P13437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13437. 1 interaction.
STRINGi 10116.ENSRNOP00000060140.

Proteomic databases

PaxDbi P13437.
PRIDEi P13437.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 170465.
KEGGi rno:170465.

Organism-specific databases

CTDi 10449.
RGDi 620482. Acaa2.

Phylogenomic databases

eggNOGi COG0183.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
InParanoidi P13437.
KOi K07508.
PhylomeDBi P13437.

Enzyme and pathway databases

UniPathwayi UPA00199 .
SABIO-RK P13437.

Miscellaneous databases

NextBioi 620987.
PROi P13437.

Gene expression databases

Genevestigatori P13437.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. 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 ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiTHIM_RAT
AccessioniPrimary (citable) accession number: P13437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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