Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13437

- THIM_RAT

UniProt

P13437 - THIM_RAT

Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

Acaa2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 intermediateBy similarity
    Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
    Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

    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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000223301Add
    BLAST
    Transit peptidei1 – 1616Mitochondrion; not cleavedAdd
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP13437.
    PRIDEiP13437.

    Expressioni

    Gene expression databases

    GenevestigatoriP13437.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with BNIP3 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP13437. 1 interaction.
    STRINGi10116.ENSRNOP00000060140.

    Structurei

    3D structure databases

    ProteinModelPortaliP13437.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    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: October 1, 2014
    This is version 112 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