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Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

ACOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

FAD1 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

    • acyl-CoA dehydrogenase activity Source: InterPro
    • acyl-CoA oxidase activity Source: UniProtKB
    • FAD binding Source: UniProtKB
    • fatty acid binding Source: Ensembl
    • flavin adenine dinucleotide binding Source: InterPro
    • palmitoyl-CoA oxidase activity Source: UniProtKB
    • PDZ domain binding Source: MGI
    • protein N-terminus binding Source: UniProtKB
    • receptor binding Source: UniProtKB

    GO - Biological processi

    • alpha-linolenic acid metabolic process Source: Reactome
    • cellular lipid metabolic process Source: Reactome
    • fatty acid beta-oxidation using acyl-CoA oxidase Source: BHF-UCL
    • fatty acid oxidation Source: UniProtKB
    • generation of precursor metabolites and energy Source: UniProtKB
    • lipid homeostasis Source: UniProtKB
    • lipid metabolic process Source: UniProtKB
    • peroxisome fission Source: UniProtKB
    • positive regulation of cholesterol homeostasis Source: UniProtKB
    • prostaglandin metabolic process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • spermatogenesis Source: Ensembl
    • unsaturated fatty acid metabolic process Source: Reactome
    • very long-chain fatty acid metabolic process Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08589-MONOMER.
    BRENDAi1.3.3.6. 2681.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    SABIO-RKQ15067.
    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 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:119. ACOX1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD)3 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:264470

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    Chemistry

    DrugBankiDB03147. Flavin adenine dinucleotide.

    Polymorphism and mutation databases

    BioMutaiACOX1.
    DMDMi126302511.

    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 – 261Phosphoserine3 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

    BgeeiQ15067.
    CleanExiHS_ACOX1.
    ExpressionAtlasiQ15067. baseline and differential.
    GenevestigatoriQ15067.

    Organism-specific databases

    HPAiCAB021094.
    HPA021192.
    HPA021195.
    HPA028759.

    Interactioni

    Protein-protein interaction databases

    BioGridi106567. 20 interactions.
    IntActiQ15067. 7 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.
    GeneTreeiENSGT00530000062919.
    HOVERGENiHBG050451.
    InParanoidiQ15067.
    KOiK00232.
    OMAiKSANMVK.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED
    60 70 80 90 100
    LNFLTRSQRY EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV
    110 120 130 140 150
    GLNYSMFIPT LLNQGTTAQK EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL
    160 170 180 190 200
    ETTATYDPET QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITKGKCY
    210 220 230 240 250
    GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL KMDNHRIPRE
    260 270 280 290 300
    NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA
    310 320 330 340 350
    IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE
    360 370 380 390 400
    TYHRINEGIG QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG
    410 420 430 440 450
    YSHCSGLPNI YVNFTPSCTF EGENTVMMLQ TARFLMKSYD QVHSGKLVCG
    460 470 480 490 500
    MVSYLNDLPS QRIQPQQVAV WPTMVDINSP ESLTEAYKLR AARLVEIAAK
    510 520 530 540 550
    NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS EKLLKIQDKA
    560 570 580 590 600
    IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR
    610 620 630 640 650
    SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY
    660
    KHLKSLQSKL
    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.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi106567. 20 interactions.
    IntActiQ15067. 7 interactions.
    MINTiMINT-4717708.
    STRINGi9606.ENSP00000293217.

    Chemistry

    DrugBankiDB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSiteiQ15067.

    Polymorphism and mutation databases

    BioMutaiACOX1.
    DMDMi126302511.

    Proteomic databases

    MaxQBiQ15067.
    PaxDbiQ15067.
    PeptideAtlasiQ15067.
    PRIDEiQ15067.

    Protocols and materials databases

    DNASUi51.
    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi51.
    GeneCardsiGC17M073937.
    HGNCiHGNC:119. ACOX1.
    HPAiCAB021094.
    HPA021192.
    HPA021195.
    HPA028759.
    MIMi264470. phenotype.
    609751. gene.
    neXtProtiNX_Q15067.
    Orphaneti2971. Peroxisomal acyl-CoA oxidase deficiency.
    PharmGKBiPA21.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1960.
    GeneTreeiENSGT00530000062919.
    HOVERGENiHBG050451.
    InParanoidiQ15067.
    KOiK00232.
    OMAiKSANMVK.
    OrthoDBiEOG7D59MV.
    PhylomeDBiQ15067.
    TreeFamiTF300672.

    Enzyme and pathway databases

    UniPathwayiUPA00661.
    BioCyciMetaCyc:HS08589-MONOMER.
    BRENDAi1.3.3.6. 2681.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    SABIO-RKQ15067.

    Miscellaneous databases

    ChiTaRSiACOX1. human.
    GeneWikiiACOX1.
    GenomeRNAii51.
    NextBioi199.
    PROiQ15067.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ15067.
    CleanExiHS_ACOX1.
    ExpressionAtlasiQ15067. baseline and differential.
    GenevestigatoriQ15067.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. Cited for: VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
    18. "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: April 29, 2015
    This is version 160 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.