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Q15067

- ACOX1_HUMAN

UniProt

Q15067 - ACOX1_HUMAN

Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

ACOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (20 Feb 2007)
      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 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.2 Publications

    Catalytic activityi

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

    Cofactori

    FAD.1 Publication

    Kineticsi

    1. KM=73 µM for palmitoyl-CoA (isoform 1)1 Publication
    2. KM=90 µM for palmitoyl-CoA (isoform 2)1 Publication

    pH dependencei

    Optimum pH is 8.5 for isoform 1 and 7.5-8.5 for isoform 2.1 Publication

    Temperature dependencei

    Optimum temperature for isoform 1 at pH 7.5 is 40 degrees Celsius with no activity at 50 degrees Celsius. Optimum temperature for isoform 2 at pH 7.5 is 47.5 degrees Celsius with 57% activity retained at 50 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei139 – 1391FADBy similarity
    Binding sitei178 – 1781FAD; via amide nitrogenBy similarity
    Active sitei421 – 4211Proton acceptorBy similarity

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: InterPro
    2. acyl-CoA oxidase activity Source: UniProtKB
    3. FAD binding Source: UniProtKB
    4. fatty acid binding Source: Ensembl
    5. flavin adenine dinucleotide binding Source: InterPro
    6. palmitoyl-CoA oxidase activity Source: UniProtKB
    7. PDZ domain binding Source: MGI
    8. protein N-terminus binding Source: UniProtKB
    9. receptor binding Source: UniProtKB

    GO - Biological processi

    1. alpha-linolenic acid metabolic process Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation using acyl-CoA oxidase Source: BHF-UCL
    4. fatty acid oxidation Source: UniProtKB
    5. generation of precursor metabolites and energy Source: UniProtKB
    6. lipid homeostasis Source: UniProtKB
    7. lipid metabolic process Source: UniProtKB
    8. peroxisome fission Source: UniProtKB
    9. positive regulation of cholesterol homeostasis Source: UniProtKB
    10. prostaglandin metabolic process Source: UniProtKB
    11. small molecule metabolic process Source: Reactome
    12. spermatogenesis Source: Ensembl
    13. unsaturated fatty acid metabolic process Source: Reactome
    14. very long-chain fatty acid metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08589-MONOMER.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    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
    Straight-chain acyl-CoA oxidase
    Short name:
    SCOX
    Gene namesi
    Name:ACOX1
    Synonyms:ACOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:119. ACOX1.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. mitochondrion Source: Ensembl
    3. peroxisomal matrix Source: Reactome
    4. peroxisomal membrane Source: Ensembl
    5. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD) [MIM:264470]: A peroxisomal single-enzyme disorder of fatty acid beta-oxidation, resulting in clinical manifestations that remind neonatal adrenoleukodystrophy. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly, hearing deficit. Pseudo-NALD is characterized by increased plasma levels of very-long chain fatty acids, due to decreased or absent peroxisome acyl-CoA oxidase activity. Peroxisomes are intact and functioning.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi264470. phenotype.
    Orphaneti2971. Peroxisomal acyl-CoA oxidase deficiency.
    PharmGKBiPA21.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Peroxisomal acyl-coenzyme A oxidase 1PRO_0000204677Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Phosphoserine2 Publications
    Modified residuei89 – 891N6-succinyllysineBy similarity
    Modified residuei90 – 901N6-succinyllysineBy similarity
    Modified residuei216 – 2161N6-acetyllysineBy similarity
    Modified residuei241 – 2411N6-succinyllysineBy similarity
    Modified residuei255 – 2551N6-acetyllysine1 Publication
    Modified residuei267 – 2671N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysineBy similarity
    Modified residuei349 – 3491N6-succinyllysineBy similarity
    Modified residuei437 – 4371N6-acetyllysine; alternate1 Publication
    Modified residuei437 – 4371N6-succinyllysine; alternateBy similarity
    Modified residuei446 – 4461N6-acetyllysine; alternateBy similarity
    Modified residuei446 – 4461N6-succinyllysine; alternateBy similarity
    Modified residuei500 – 5001N6-acetyllysine1 Publication
    Modified residuei504 – 5041N6-acetyllysine1 Publication
    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 residuei651 – 6511N6-acetyllysineBy similarity
    Modified residuei654 – 6541N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15067.
    PaxDbiQ15067.
    PeptideAtlasiQ15067.
    PRIDEiQ15067.

    PTM databases

    PhosphoSiteiQ15067.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels of isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 levels are higher in brain, lung, muscle, white adipose tissue and testis. Levels are almost equal in heart.2 Publications

    Gene expression databases

    ArrayExpressiQ15067.
    BgeeiQ15067.
    CleanExiHS_ACOX1.
    GenevestigatoriQ15067.

    Organism-specific databases

    HPAiCAB021094.
    HPA021192.
    HPA021195.
    HPA028759.

    Interactioni

    Protein-protein interaction databases

    BioGridi106567. 11 interactions.
    IntActiQ15067. 4 interactions.
    MINTiMINT-4717708.
    STRINGi9606.ENSP00000293217.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15067.
    SMRiQ15067. Positions 1-654.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi658 – 6603Microbody targeting signal

    Sequence similaritiesi

    Belongs to the acyl-CoA oxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG1960.
    HOVERGENiHBG050451.
    KOiK00232.
    OMAiVHESYKH.
    OrthoDBiEOG7D59MV.
    PhylomeDBiQ15067.
    TreeFamiTF300672.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15067-1) [UniParc]FASTAAdd to Basket

    Also known as: ACOX1a, SCOX-exon 3I

    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

    MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED    50
    LNFLTRSQRY EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV 100
    GLNYSMFIPT LLNQGTTAQK EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL 150
    ETTATYDPET QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITKGKCY 200
    GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL KMDNHRIPRE 250
    NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA 300
    IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE 350
    TYHRINEGIG QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG 400
    YSHCSGLPNI YVNFTPSCTF EGENTVMMLQ TARFLMKSYD QVHSGKLVCG 450
    MVSYLNDLPS QRIQPQQVAV WPTMVDINSP ESLTEAYKLR AARLVEIAAK 500
    NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS EKLLKIQDKA 550
    IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR 600
    SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY 650
    KHLKSLQSKL 660
    Length:660
    Mass (Da):74,424
    Last modified:February 20, 2007 - v3
    Checksum:iD713768A47374EA1
    GO
    Isoform 2 (identifier: Q15067-2) [UniParc]FASTAAdd to Basket

    Also known as: ACOX1b, SCOX-exon 3II

    The sequence of this isoform differs from the canonical sequence as follows:
         90-131: KLHLVNFVEP...KWLLSSKGLQ → NFVHRGRPEP...RFFMPAWNLE

    Show »
    Length:660
    Mass (Da):74,668
    Checksum:i761C97B5043F9068
    GO
    Isoform 3 (identifier: Q15067-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.
         90-131: KLHLVNFVEP...KWLLSSKGLQ → NFVHRGRPEP...RFFMPAWNLE

    Note: No experimental confirmation available.

    Show »
    Length:622
    Mass (Da):70,136
    Checksum:iFE52A881C050EB78
    GO

    Sequence cautioni

    The sequence CAD97622.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271P → L in CAA50574. (PubMed:8040306)Curated
    Sequence conflicti80 – 801A → R in CAA50574. (PubMed:8040306)Curated
    Sequence conflicti84 – 841E → D in CAD97622. (PubMed:17974005)Curated
    Sequence conflicti119 – 1191Q → E in AAB30019. (PubMed:8117268)Curated
    Sequence conflicti200 – 2001Y → H in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti212 – 2132IG → NR in AAA19113. (PubMed:8159712)Curated
    Sequence conflicti212 – 2132IG → NR in AAA19114. (PubMed:8159712)Curated
    Sequence conflicti212 – 2132IG → NR in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti264 – 2641T → P in AAA19113. (PubMed:8159712)Curated
    Sequence conflicti264 – 2641T → P in AAA19114. (PubMed:8159712)Curated
    Sequence conflicti264 – 2641T → P in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti332 – 3321F → L in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti449 – 4491C → R in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti490 – 4901R → L in BAF85654. (PubMed:14702039)Curated
    Sequence conflicti531 – 5311C → L in AAA19113. (PubMed:8159712)Curated
    Sequence conflicti531 – 5311C → L in AAA19114. (PubMed:8159712)Curated
    Sequence conflicti531 – 5311C → L in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti534 – 5352VV → GL in AAA19113. (PubMed:8159712)Curated
    Sequence conflicti534 – 5352VV → GL in AAA19114. (PubMed:8159712)Curated
    Sequence conflicti534 – 5352VV → GL in AAA18595. (PubMed:7876265)Curated
    Sequence conflicti615 – 6151V → A in CAA50574. (PubMed:8040306)Curated
    Sequence conflicti650 – 6501Y → YH in AAB30019. (PubMed:8117268)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641Missing in pseudo-NALD. 1 Publication
    VAR_067040
    Natural varianti101 – 1011G → S.
    Corresponds to variant rs3744032 [ dbSNP | Ensembl ].
    VAR_048182
    Natural varianti153 – 1531T → I.1 Publication
    Corresponds to variant rs17855420 [ dbSNP | Ensembl ].
    VAR_030619
    Natural varianti178 – 1781G → C in pseudo-NALD. 2 Publications
    VAR_025789
    Natural varianti184 – 1841S → L in pseudo-NALD. 1 Publication
    VAR_067041
    Natural varianti231 – 2311G → V in pseudo-NALD. 1 Publication
    VAR_067042
    Natural varianti278 – 2781M → V in pseudo-NALD. 2 Publications
    VAR_025790
    Natural varianti309 – 3091Q → R in pseudo-NALD. 1 Publication
    VAR_067043
    Natural varianti310 – 3101S → P in pseudo-NALD. 1 Publication
    VAR_067044
    Natural varianti312 – 3121I → M.5 Publications
    Corresponds to variant rs1135640 [ dbSNP | Ensembl ].
    VAR_021529

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_046129Add
    BLAST
    Alternative sequencei90 – 13142KLHLV…SKGLQ → NFVHRGRPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LE in isoform 2 and isoform 3. 4 PublicationsVSP_000146Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03268
    , U03254, U03255, U03256, U03258, U03259, U03260, U03261, U03263, U03264, U03265, U03266, U03267 Genomic DNA. Translation: AAA19113.1.
    U03268
    , U03254, U03255, U03257, U03258, U03259, U03260, U03261, U03263, U03264, U03265, U03266, U03267 Genomic DNA. Translation: AAA19114.1.
    U07866 mRNA. Translation: AAA18595.1.
    X71440 mRNA. Translation: CAA50574.1.
    S69189 mRNA. Translation: AAB30019.2.
    AK291793 mRNA. Translation: BAF84482.1.
    AK292965 mRNA. Translation: BAF85654.1.
    AK296409 mRNA. Translation: BAG59073.1.
    BX537380 mRNA. Translation: CAD97622.1. Different initiation.
    AC040980 Genomic DNA. No translation available.
    AC087289 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89351.1.
    BC008767 mRNA. Translation: AAH08767.1.
    BC010425 mRNA. Translation: AAH10425.1.
    CCDSiCCDS11734.1. [Q15067-2]
    CCDS11735.1. [Q15067-1]
    PIRiA54942.
    B54942.
    I38095.
    RefSeqiNP_001171968.1. NM_001185039.1. [Q15067-3]
    NP_004026.2. NM_004035.6. [Q15067-2]
    NP_009223.2. NM_007292.5. [Q15067-1]
    UniGeneiHs.464137.

    Genome annotation databases

    EnsembliENST00000293217; ENSP00000293217; ENSG00000161533. [Q15067-2]
    ENST00000301608; ENSP00000301608; ENSG00000161533. [Q15067-1]
    GeneIDi51.
    KEGGihsa:51.
    UCSCiuc002jqe.3. human. [Q15067-2]
    uc002jqf.3. human. [Q15067-1]

    Polymorphism databases

    DMDMi126302511.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03268
    , U03254 , U03255 , U03256 , U03258 , U03259 , U03260 , U03261 , U03263 , U03264 , U03265 , U03266 , U03267 Genomic DNA. Translation: AAA19113.1 .
    U03268
    , U03254 , U03255 , U03257 , U03258 , U03259 , U03260 , U03261 , U03263 , U03264 , U03265 , U03266 , U03267 Genomic DNA. Translation: AAA19114.1 .
    U07866 mRNA. Translation: AAA18595.1 .
    X71440 mRNA. Translation: CAA50574.1 .
    S69189 mRNA. Translation: AAB30019.2 .
    AK291793 mRNA. Translation: BAF84482.1 .
    AK292965 mRNA. Translation: BAF85654.1 .
    AK296409 mRNA. Translation: BAG59073.1 .
    BX537380 mRNA. Translation: CAD97622.1 . Different initiation.
    AC040980 Genomic DNA. No translation available.
    AC087289 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89351.1 .
    BC008767 mRNA. Translation: AAH08767.1 .
    BC010425 mRNA. Translation: AAH10425.1 .
    CCDSi CCDS11734.1. [Q15067-2 ]
    CCDS11735.1. [Q15067-1 ]
    PIRi A54942.
    B54942.
    I38095.
    RefSeqi NP_001171968.1. NM_001185039.1. [Q15067-3 ]
    NP_004026.2. NM_004035.6. [Q15067-2 ]
    NP_009223.2. NM_007292.5. [Q15067-1 ]
    UniGenei Hs.464137.

    3D structure databases

    ProteinModelPortali Q15067.
    SMRi Q15067. Positions 1-654.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106567. 11 interactions.
    IntActi Q15067. 4 interactions.
    MINTi MINT-4717708.
    STRINGi 9606.ENSP00000293217.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei Q15067.

    Polymorphism databases

    DMDMi 126302511.

    Proteomic databases

    MaxQBi Q15067.
    PaxDbi Q15067.
    PeptideAtlasi Q15067.
    PRIDEi Q15067.

    Protocols and materials databases

    DNASUi 51.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293217 ; ENSP00000293217 ; ENSG00000161533 . [Q15067-2 ]
    ENST00000301608 ; ENSP00000301608 ; ENSG00000161533 . [Q15067-1 ]
    GeneIDi 51.
    KEGGi hsa:51.
    UCSCi uc002jqe.3. human. [Q15067-2 ]
    uc002jqf.3. human. [Q15067-1 ]

    Organism-specific databases

    CTDi 51.
    GeneCardsi GC17M073937.
    HGNCi HGNC:119. ACOX1.
    HPAi CAB021094.
    HPA021192.
    HPA021195.
    HPA028759.
    MIMi 264470. phenotype.
    609751. gene.
    neXtProti NX_Q15067.
    Orphaneti 2971. Peroxisomal acyl-CoA oxidase deficiency.
    PharmGKBi PA21.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOVERGENi HBG050451.
    KOi K00232.
    OMAi VHESYKH.
    OrthoDBi EOG7D59MV.
    PhylomeDBi Q15067.
    TreeFami TF300672.

    Enzyme and pathway databases

    UniPathwayi UPA00661 .
    BioCyci MetaCyc:HS08589-MONOMER.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.

    Miscellaneous databases

    ChiTaRSi ACOX1. human.
    GeneWikii ACOX1.
    GenomeRNAii 51.
    NextBioi 199.
    PROi Q15067.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15067.
    Bgeei Q15067.
    CleanExi HS_ACOX1.
    Genevestigatori Q15067.

    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. "Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization."
      Varanasi U., Chu R., Chu S., Espinosa R., Lebeau M.M., Reddy J.K.
      Proc. Natl. Acad. Sci. U.S.A. 91:3107-3111(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    2. "Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells."
      Chu R., Varanasi U., Chu S., Lin Y., Usuda N., Rao M.S., Reddy J.K.
      J. Biol. Chem. 270:4908-4915(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy."
      Fourner B., Saudubray J.-M., Benichou B., Lyonnet S., Munnich A., Clevers H., Poll-The B.T.
      J. Clin. Invest. 94:526-531(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-312, INVOLVEMENT IN PSEUDO-NALD.
      Tissue: Liver.
    4. "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase."
      Aoyama T., Tsushima K., Souri M., Kamijo T., Suzuki Y., Shimozawa N., Orii T., Hashimoto T.
      Biochem. Biophys. Res. Commun. 198:1113-1118(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-312.
      Tissue: Liver.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT MET-312.
      Tissue: Placenta, Thalamus and Trachea.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-312.
      Tissue: Retina.
    7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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), VARIANTS ILE-153 AND MET-312.
      Tissue: Colon and Eye.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene."
      Oaxaca-Castillo D., Andreoletti P., Vluggens A., Yu S., van Veldhoven P.P., Reddy J.K., Cherkaoui-Malki M.
      Biochem. Biophys. Res. Commun. 360:314-319(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-267; LYS-437; LYS-500 AND LYS-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: TISSUE SPECIFICITY, REVERSAL OF ACOX1 NULL PHENOTYPE IN MOUSE.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
    17. "Clinical, biochemical, and mutational spectrum of peroxisomal acyl-coenzyme A oxidase deficiency."
      Ferdinandusse S., Denis S., Hogenhout E.M., Koster J., van Roermund C.W., Ijlst L., Moser A.B., Wanders R.J., Waterham H.R.
      Hum. Mutat. 28:904-912(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PSEUDO-NALD VAL-64 DEL; CYS-178; LEU-184; VAL-231; VAL-278; ARG-309 AND PRO-310, FUNCTION.

    Entry informationi

    Entry nameiACOX1_HUMAN
    AccessioniPrimary (citable) accession number: Q15067
    Secondary accession number(s): A8K6X8
    , A8KAA0, B4DK61, F5GYQ8, Q12863, Q15068, Q15101, Q16131, Q7Z3W5, Q9UD31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Isoform 1 and isoform 2 can reverse the Acox1 null phenotype in mouse which is characterized by severe microvesicular hepatic steatosis, sustained activation of Ppara, spontaneous massive peroxisome proliferation and eventual development of hepatocellular carcinomas. Isoform 2 is more effective in reversal of the phenotype than isoform 1 (PubMed:20195242).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3