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P21775

- THIKA_RAT

UniProt

P21775 - THIKA_RAT

Protein

3-ketoacyl-CoA thiolase A, peroxisomal

Gene

Acaa1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231Acyl-thioester intermediateBy similarity
    Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotation
    Active sitei408 – 4081Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC
    2. palmitoyl-CoA oxidase activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB
    2. response to drug Source: RGD
    3. response to nutrient Source: RGD
    4. response to steroid hormone Source: RGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    SABIO-RKP21775.
    UniPathwayiUPA00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase A, peroxisomal (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase A
    Beta-ketothiolase A
    Peroxisomal 3-oxoacyl-CoA thiolase A
    Gene namesi
    Name:Acaa1a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi67379. Acaa1a.

    Subcellular locationi

    GO - Cellular componenti

    1. peroxisome Source: HGNC

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626Peroxisome1 PublicationAdd
    BLAST
    Chaini27 – 4243983-ketoacyl-CoA thiolase A, peroxisomalPRO_0000034070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei173 – 1731N6-acetyllysineBy similarity
    Modified residuei234 – 2341N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP21775.
    PRIDEiP21775.

    PTM databases

    PhosphoSiteiP21775.

    Expressioni

    Inductioni

    Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

    Gene expression databases

    GenevestigatoriP21775.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000041776.

    Structurei

    3D structure databases

    ProteinModelPortaliP21775.
    SMRiP21775. Positions 31-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    HOGENOMiHOG000012239.
    HOVERGENiHBG003112.
    InParanoidiP21775.
    KOiK07513.
    PhylomeDBiP21775.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21775-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MHRLQVVLGH LAGRPESSSA LQAAPCSATF PQASASDVVV VHGRRTPIGR    50
    AGRGGFKDTT PDELLSAVLT AVLQDVKLKP ECLGDISVGN VLEPGAGAVM 100
    ARIAQFLSGI PETVPLSAVN RQCSSGLQAV ANIAGGIRNG SYDIGMACGV 150
    ESMSLSNRGN PGNISSRLLE SDKARDCLIP MGITSENVAE RFGISRQKQD 200
    AFALASQQKA ASAQSKGCFR AEIVPVTTTV LDDKGDRKTI TVSQDEGVRP 250
    STTMEGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI 300
    LGVLRSYAVV GVPPDIMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS 350
    QALYCVEKLG IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR 400
    AYGVVSMCIG TGMGAAAVFE YPGN 424
    Length:424
    Mass (Da):43,833
    Last modified:August 30, 2005 - v2
    Checksum:iD987625F3FF94F1C
    GO
    Isoform 2 (identifier: P21775-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         334-424: LTVNDIDIFE...AAAVFEYPGN → PLLCGEAGNS...RSKAGGHAAQ

    Note: No experimental confirmation available.

    Show »
    Length:373
    Mass (Da):38,118
    Checksum:i4DA3FD8B35A6403B
    GO

    Sequence cautioni

    The sequence AAA41471.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH89821.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA14106.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291T → S in AAH89821. (PubMed:15489334)Curated
    Sequence conflicti235 – 2351G → S in AAH89821. (PubMed:15489334)Curated
    Sequence conflicti399 – 3991R → T in AAA41471. (PubMed:2210380)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei334 – 42491LTVND…EYPGN → PLLCGEAGNSCREGEPPGGC NSPGPPPGLHRSKAGGHAAQ in isoform 2. 1 PublicationVSP_023746Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32801 mRNA. Translation: AAA41471.1. Different initiation.
    D90058 Genomic DNA. Translation: BAA14106.1. Different initiation.
    BC089821 mRNA. Translation: AAH89821.1. Different initiation.
    PIRiA35725. XURTAA.
    RefSeqiNP_036621.1. NM_012489.2.
    UniGeneiRn.8913.

    Genome annotation databases

    GeneIDi24157.
    KEGGirno:24157.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32801 mRNA. Translation: AAA41471.1 . Different initiation.
    D90058 Genomic DNA. Translation: BAA14106.1 . Different initiation.
    BC089821 mRNA. Translation: AAH89821.1 . Different initiation.
    PIRi A35725. XURTAA.
    RefSeqi NP_036621.1. NM_012489.2.
    UniGenei Rn.8913.

    3D structure databases

    ProteinModelPortali P21775.
    SMRi P21775. Positions 31-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000041776.

    PTM databases

    PhosphoSitei P21775.

    Proteomic databases

    PaxDbi P21775.
    PRIDEi P21775.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24157.
    KEGGi rno:24157.

    Organism-specific databases

    CTDi 113868.
    RGDi 67379. Acaa1a.

    Phylogenomic databases

    eggNOGi COG0183.
    HOGENOMi HOG000012239.
    HOVERGENi HBG003112.
    InParanoidi P21775.
    KOi K07513.
    PhylomeDBi P21775.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .
    SABIO-RK P21775.

    Miscellaneous databases

    NextBioi 602445.
    PROi P21775.

    Gene expression databases

    Genevestigatori P21775.

    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. "Cloning and sequence determination of cDNA encoding a second rat liver peroxisomal 3-ketoacyl-CoA thiolase."
      Bodnar A.G., Rachubinski R.A.
      Gene 91:193-199(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
    2. "Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated genes."
      Hijikata M., Wen J.K., Osumi T., Hashimoto T.
      J. Biol. Chem. 265:4600-4606(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sprague-Dawley.
    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] (ISOFORM 2).
      Tissue: Lung.
    4. "A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase."
      Swinkels B.W., Gould S.J., Bodnar A.G., Rachubinski R.A., Subramani S.
      EMBO J. 10:3255-3262(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSIT PEPTIDE CLEAVAGE SITE.

    Entry informationi

    Entry nameiTHIKA_RAT
    AccessioniPrimary (citable) accession number: P21775
    Secondary accession number(s): Q5FVR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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