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    Paox polyamine oxidase (exo-N4-amino) [ Mus musculus (house mouse) ]

    Gene ID: 212503, updated on 12-May-2024

    Summary

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    Official Symbol
    Paoxprovided by MGI
    Official Full Name
    polyamine oxidase (exo-N4-amino)provided by MGI
    Primary source
    MGI:MGI:1916983
    See related
    Ensembl:ENSMUSG00000025464 AllianceGenome:MGI:1916983
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    Pao; 2410012F02Rik
    Summary
    Enables polyamine oxidase activity. Acts upstream of or within polyamine catabolic process. Predicted to be located in peroxisomal matrix. Is expressed in several structures, including central nervous system; genitourinary system; gut; hemolymphoid system gland; and integumental system. Orthologous to human PAOX (polyamine oxidase). [provided by Alliance of Genome Resources, Apr 2022]
    Expression
    Ubiquitous expression in liver adult (RPKM 11.4), ovary adult (RPKM 8.2) and 28 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Paox in Genome Data Viewer
    Location:
    7 F4; 7 85.14 cM
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 7 NC_000073.7 (139693182..139714249)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 7 NC_000073.6 (140115735..140134334)

    Chromosome 7 - NC_000073.7Genomic Context describing neighboring genes Neighboring gene proline-rich acidic protein 1 Neighboring gene fucose mutarotase Neighboring gene enoyl Coenzyme A hydratase, short chain, 1, mitochondrial Neighboring gene STARR-positive B cell enhancer ABC_E1747 Neighboring gene mitochondrial ribosome-associated GTPase 1 Neighboring gene shadow of prion protein Neighboring gene olfactory receptor family 6 subfamily AE member 1

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

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    Related articles in PubMed

    1. Mechanistic studies of para-substituted N,N'-dibenzyl-1,4-diaminobutanes as substrates for a mammalian polyamine oxidase. Pozzi MH, et al. Biochemistry, 2009 Dec 29. PMID 19911805, Free PMC Article
    2. Inhibition of polyamine and spermine oxidases by polyamine analogues. Bianchi M, et al. FEBS J, 2006 Mar. PMID 16519678
    3. Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate. Royo M, et al. Biochemistry, 2005 May 10. PMID 15865452, Free PMC Article
    4. Mechanistic studies of the role of a conserved histidine in a mammalian polyamine oxidase. Tormos JR, et al. Arch Biochem Biophys, 2012 Dec 1. PMID 22959971, Free PMC Article
    5. A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase. Henderson Pozzi M, et al. Arch Biochem Biophys, 2010 Jun 15. PMID 20417173, Free PMC Article

    See all (26) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Steady-state kinetics of His64 mutant proteins shows that the mutations result in a decrease of ~15-fold in the rate constant for amine oxidation.
      Title: Mechanistic studies of the role of a conserved histidine in a mammalian polyamine oxidase.
    2. N,N'-dibenzyl-1,4-diaminobutanes, with only two nitrogens, are also substrates of polyamine oxidase.
      Title: Mechanistic studies of para-substituted N,N'-dibenzyl-1,4-diaminobutanes as substrates for a mammalian polyamine oxidase.
    3. translated amino acid sequences of mpao and bpao have a -Pro-Arg-Leu peroxisomal targeting signal at the extreme C termini and a beta-alpha-beta FAD-binding motif is present in the N-terminal portion of mPAO.
      Title: Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.
    4. new mechanism for pathogen-induced oxidative stress in macrophages in which activation of PAO1 leads to H(2)O(2) release and apoptosis by a mitochondrial-dependent cell death pathway
      Title: Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization.
    Submit: New GeneRIF Correction

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Endonuclease-mediated (2) 
    • Targeted (2) 

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables polyamine oxidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables polyamine oxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables polyamine oxidase activity ISO
    Inferred from Sequence Orthology
    more info
    		 PubMed 
    enables spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables spermine:oxygen oxidoreductase (spermidine-forming) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within polyamine catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within polyamine catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		 PubMed 
    involved_in polyamine catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in positive regulation of spermidine biosynthetic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in putrescine biosynthetic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in putrescine catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in spermidine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in spermidine catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in spermine catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in peroxisomal matrix ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in peroxisome IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    peroxisomal N(1)-acetyl-spermine/spermidine oxidase
    Names
    exo-N4-amino
    peroxisomal N1-acetyl-spermine/spermidine oxidase
    NP_001333654.1
    NP_722478.2
    XP_006536229.4
    XP_006536230.1
    XP_006536231.1
    XP_011248141.1
    XP_011248143.3
    XP_017177591.1
    XP_017177592.1
    XP_030098194.1
    XP_036008771.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001346725.2 → NP_001333654.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform 2

      Status: VALIDATED

      Source sequence(s)
      AC109205
      Consensus CDS
      CCDS85452.1
      UniProtKB/TrEMBL
      Q3TXR6
      Related
      ENSMUSP00000095580.4, ENSMUST00000097967.4

    2. NM_153783.4 → NP_722478.2  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform 1

      See identical proteins and their annotated locations for NP_722478.2

      Status: VALIDATED

      Source sequence(s)
      AC109205
      Consensus CDS
      CCDS21965.1
      UniProtKB/Swiss-Prot
      Q8C0L6, Q8K254
      UniProtKB/TrEMBL
      Q4GX45
      Related
      ENSMUSP00000026537.6, ENSMUST00000026537.13
      Conserved Domains (2) summary
      PLN02568
      Location:6 → 490
      PLN02568; polyamine oxidase
      pfam13450
      Location:10 → 79
      NAD_binding_8; NAD(P)-binding Rossmann-like domain

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000073.7 Reference GRCm39 C57BL/6J

      Range
      139693182..139714249
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011249839.4 → XP_011248141.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X2

      See identical proteins and their annotated locations for XP_011248141.1

      UniProtKB/TrEMBL
      Q4GX45
      Conserved Domains (1) summary
      PLN02568
      Location:3 → 440
      PLN02568; polyamine oxidase

    2. XM_030242334.2 → XP_030098194.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X5

      Conserved Domains (1) summary
      PLN02568
      Location:42 → 386
      PLN02568; polyamine oxidase

    3. XM_011249841.4 → XP_011248143.3  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X6

      Conserved Domains (1) summary
      PLN02568
      Location:105 → 380
      PLN02568; polyamine oxidase

    4. XM_017322103.3 → XP_017177592.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X5

      Conserved Domains (1) summary
      PLN02568
      Location:42 → 386
      PLN02568; polyamine oxidase

    5. XM_006536166.4 → XP_006536229.4  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X1

      UniProtKB/TrEMBL
      Q4GX45
      Conserved Domains (1) summary
      PLN02568
      Location:141 → 485
      PLN02568; polyamine oxidase

    6. XM_036152878.1 → XP_036008771.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X2

      UniProtKB/TrEMBL
      Q4GX45
      Conserved Domains (1) summary
      PLN02568
      Location:3 → 440
      PLN02568; polyamine oxidase

    7. XM_006536167.5 → XP_006536230.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X4

      Conserved Domains (1) summary
      PLN02568
      Location:6 → 323
      PLN02568; polyamine oxidase

    8. XM_017322102.3 → XP_017177591.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X3

      Conserved Domains (1) summary
      PLN02568
      Location:6 → 323
      PLN02568; polyamine oxidase

    9. XM_006536168.4 → XP_006536231.1  peroxisomal N(1)-acetyl-spermine/spermidine oxidase isoform X5

      Conserved Domains (1) summary
      PLN02568
      Location:42 → 386
      PLN02568; polyamine oxidase

    RNA

    1. XR_001785516.3 RNA Sequence

    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q8C0L6.3 GenPept UniProtKB/Swiss-Prot:Q8C0L6

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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