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P07872

- ACOX1_RAT

UniProt

P07872 - ACOX1_RAT

Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

Acox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 1 shows optimum activity with a chain length of 10 carbons while isoform 2 exhibits optimum activity with 14 carbons.1 Publication

    Catalytic activityi

    Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei139 – 1391FAD
    Binding sitei178 – 1781FAD; via amide nitrogen
    Active sitei421 – 4211Proton acceptor2 Publications

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: InterPro
    2. acyl-CoA oxidase activity Source: UniProtKB
    3. FAD binding Source: Ensembl
    4. fatty acid binding Source: RGD
    5. palmitoyl-CoA oxidase activity Source: RGD

    GO - Biological processi

    1. fatty acid beta-oxidation using acyl-CoA oxidase Source: RGD
    2. fatty acid oxidation Source: UniProtKB
    3. generation of precursor metabolites and energy Source: UniProtKB
    4. lipid homeostasis Source: Ensembl
    5. lipid metabolic process Source: UniProtKB
    6. peroxisome fission Source: Ensembl
    7. positive regulation of cholesterol homeostasis Source: Ensembl
    8. prostaglandin metabolic process Source: UniProtKB
    9. spermatogenesis Source: Ensembl
    10. very long-chain fatty acid metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_196408. PPARA activates gene expression.
    REACT_198818. alpha-linolenic acid (ALA) metabolism.
    SABIO-RKP07872.
    UniPathwayiUPA00661.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal acyl-coenzyme A oxidase 1 (EC:1.3.3.6)
    Short name:
    AOX
    Alternative name(s):
    Palmitoyl-CoA oxidase
    Cleaved into the following 3 chains:
    Gene namesi
    Name:Acox1
    Synonyms:Acox
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619757. Acox1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. peroxisomal membrane Source: Ensembl
    3. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 661661Peroxisomal acyl-CoA oxidase 1, A chainPRO_0000000552Add
    BLAST
    Chaini1 – 438438Peroxisomal acyl-CoA oxidase 1, B chainPRO_0000000553Add
    BLAST
    Chaini439 – 661223Peroxisomal acyl-CoA oxidase 1, C chainPRO_0000000554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei65 – 651N6-acetyllysineBy similarity
    Modified residuei89 – 891N6-succinyllysineBy similarity
    Modified residuei90 – 901N6-succinyllysineBy similarity
    Modified residuei159 – 1591N6-succinyllysineBy similarity
    Modified residuei216 – 2161N6-acetyllysineBy similarity
    Modified residuei241 – 2411N6-succinyllysineBy similarity
    Modified residuei255 – 2551N6-acetyllysineBy similarity
    Modified residuei267 – 2671N6-acetyllysineBy similarity
    Modified residuei272 – 2721N6-acetyllysineBy similarity
    Modified residuei349 – 3491N6-succinyllysineBy similarity
    Modified residuei437 – 4371N6-acetyllysine; alternateBy similarity
    Modified residuei437 – 4371N6-succinyllysine; alternateBy similarity
    Modified residuei446 – 4461N6-acetyllysine; alternateBy similarity
    Modified residuei446 – 4461N6-succinyllysine; alternateBy similarity
    Modified residuei500 – 5001N6-acetyllysineBy similarity
    Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
    Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
    Modified residuei542 – 5421N6-succinyllysineBy similarity
    Modified residuei637 – 6371N6-acetyllysine; alternateBy similarity
    Modified residuei637 – 6371N6-succinyllysine; alternateBy similarity
    Modified residuei643 – 6431N6-succinyllysineBy similarity
    Modified residuei652 – 6521N6-acetyllysineBy similarity
    Modified residuei655 – 6551N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP07872.
    PRIDEiP07872.

    PTM databases

    PhosphoSiteiP07872.

    Miscellaneous databases

    PMAP-CutDBP07872.

    Expressioni

    Gene expression databases

    GenevestigatoriP07872.

    Interactioni

    Subunit structurei

    Homodimer. The enzyme contains three components A, B and C, the latter two being produced from the first by a proteolytic cleavage.2 Publications

    Protein-protein interaction databases

    IntActiP07872. 1 interaction.
    MINTiMINT-1775779.
    STRINGi10116.ENSRNOP00000042132.

    Structurei

    Secondary structure

    1
    661
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119
    Helixi16 – 249
    Helixi27 – 4115
    Helixi44 – 463
    Helixi51 – 533
    Helixi56 – 7621
    Helixi82 – 9312
    Helixi101 – 1055
    Helixi107 – 1115
    Helixi117 – 12812
    Beta strandi134 – 1374
    Beta strandi143 – 1453
    Helixi147 – 1493
    Beta strandi153 – 1575
    Turni158 – 1614
    Beta strandi162 – 1665
    Turni170 – 1723
    Beta strandi173 – 1753
    Turni178 – 1836
    Beta strandi185 – 19511
    Beta strandi198 – 20811
    Turni212 – 2143
    Beta strandi221 – 2255
    Beta strandi229 – 2313
    Beta strandi238 – 24811
    Helixi249 – 2513
    Helixi279 – 30628
    Helixi321 – 3233
    Helixi325 – 35329
    Turni360 – 3623
    Helixi367 – 39529
    Helixi398 – 4014
    Helixi403 – 4053
    Helixi407 – 4148
    Helixi415 – 4184
    Beta strandi420 – 4223
    Helixi424 – 44421
    Helixi450 – 4578
    Helixi480 – 50930
    Helixi512 – 5187
    Helixi520 – 54223
    Helixi543 – 5453
    Helixi549 – 56921
    Helixi571 – 5766
    Helixi582 – 59918
    Helixi600 – 6023
    Helixi603 – 6086
    Helixi614 – 6174
    Helixi628 – 63811
    Helixi640 – 6423
    Beta strandi643 – 6464
    Helixi648 – 6536

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IS2X-ray2.20A/B1-661[»]
    2DDHX-ray2.07A1-661[»]
    ProteinModelPortaliP07872.
    SMRiP07872. Positions 1-655.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07872.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi659 – 6613Microbody targeting signal

    Sequence similaritiesi

    Belongs to the acyl-CoA oxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000181256.
    HOVERGENiHBG050451.
    KOiK00232.
    PhylomeDBiP07872.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR029320. Acyl-CoA_ox_N.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.

    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: P07872-1) [UniParc]FASTAAdd to Basket

    Also known as: ACO-I

    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

    MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED    50
    YNFLTRSQRY EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV 100
    GLNYSMFIPT LLNQGTTAQQ EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL 150
    ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITQGECY 200
    GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE 250
    NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA 300
    IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE 350
    TYLRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG 400
    YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVRSGKLVGG 450
    MVSYLNDLPS QRIQPQQVAV WPTMVDINSL EGLTEAYKLR AARLVEIAAK 500
    NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS DKLPKIQDKA 550
    VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR 600
    PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY 650
    HKHLKPLQSK L 661
    Length:661
    Mass (Da):74,679
    Last modified:August 1, 1988 - v1
    Checksum:i24B1F10DF066C29E
    GO
    Isoform 2 (identifier: P07872-2) [UniParc]FASTAAdd to Basket

    Also known as: ACO-II

    The sequence of this isoform differs from the canonical sequence as follows:
         90-133: KLYLANFVEP...MRPSQELQII → NSVHRGHPEP...FMPAWNLEIT

    Show »
    Length:661
    Mass (Da):74,691
    Checksum:i23EBDE0CDEE70559
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei90 – 13344KLYLA…ELQII → NSVHRGHPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LEIT in isoform 2. 1 PublicationVSP_000147Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02752 mRNA. Translation: AAA40666.1.
    BC085743 mRNA. Translation: AAH85743.1.
    J02753 Genomic DNA. Translation: AAA40667.1.
    PIRiA29328. OXRTA1.
    B29328. OXRTA2.
    RefSeqiNP_059036.1. NM_017340.2. [P07872-1]
    UniGeneiRn.31796.

    Genome annotation databases

    GeneIDi50681.
    KEGGirno:50681.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02752 mRNA. Translation: AAA40666.1 .
    BC085743 mRNA. Translation: AAH85743.1 .
    J02753 Genomic DNA. Translation: AAA40667.1 .
    PIRi A29328. OXRTA1.
    B29328. OXRTA2.
    RefSeqi NP_059036.1. NM_017340.2. [P07872-1 ]
    UniGenei Rn.31796.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IS2 X-ray 2.20 A/B 1-661 [» ]
    2DDH X-ray 2.07 A 1-661 [» ]
    ProteinModelPortali P07872.
    SMRi P07872. Positions 1-655.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07872. 1 interaction.
    MINTi MINT-1775779.
    STRINGi 10116.ENSRNOP00000042132.

    Chemistry

    BindingDBi P07872.
    ChEMBLi CHEMBL4632.

    PTM databases

    PhosphoSitei P07872.

    Proteomic databases

    PaxDbi P07872.
    PRIDEi P07872.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 50681.
    KEGGi rno:50681.

    Organism-specific databases

    CTDi 51.
    RGDi 619757. Acox1.

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000181256.
    HOVERGENi HBG050451.
    KOi K00232.
    PhylomeDBi P07872.

    Enzyme and pathway databases

    UniPathwayi UPA00661 .
    Reactomei REACT_196408. PPARA activates gene expression.
    REACT_198818. alpha-linolenic acid (ALA) metabolism.
    SABIO-RK P07872.

    Miscellaneous databases

    EvolutionaryTracei P07872.
    NextBioi 610520.
    PMAP-CutDB P07872.

    Gene expression databases

    Genevestigatori P07872.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR029320. Acyl-CoA_ox_N.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMi SSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase."
      Miyazawa S., Hayashi H., Hijikata M., Ishii N., Furuta S., Kagamiyama H., Osumi T., Hashimoto T.
      J. Biol. Chem. 262:8131-8137(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "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 1).
      Strain: Brown Norway.
      Tissue: Kidney.
    3. "Isolation and structural characterization of the rat acyl-CoA oxidase gene."
      Osumi T., Ishii N., Miyazawa S., Hashimoto T.
      J. Biol. Chem. 262:8138-8143(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    4. "Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities."
      Setoyama C., Tamaoki H., Nishina Y., Shiga K., Miura R.
      Biochem. Biophys. Res. Commun. 217:482-487(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase."
      Nakajima Y., Miyahara I., Hirotsu K., Nishina Y., Shiga K., Setoyama C., Tamaoki H., Miura R.
      J. Biochem. 131:365-374(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH A C12-FATTY ACID, SUBUNIT, ACTIVE SITE.
    6. "Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with a fatty acid: insights into substrate-recognition and reactivity toward molecular oxygen."
      Tokuoka K., Nakajima Y., Hirotsu K., Miyahara I., Nishina Y., Shiga K., Tamaoki H., Setoyama C., Tojo H., Miura R.
      J. Biochem. 139:789-795(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiACOX1_RAT
    AccessioniPrimary (citable) accession number: P07872
    Secondary accession number(s): P11354
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3