Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisomal N(1)-acetyl-spermine/spermidine oxidase

Gene

Paox

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N1,N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.

Catalytic activityi

N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2.
N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2.
N1,N(12)-diacetylspermine + O2 + H2O = N(1)-acetylspermidine + 3-acetamidobutanal + H2O2.

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Kineticsi

  1. KM=1.78 µM for N(1)-acetylspermine1 Publication
  2. KM=36.8 µM for N(1)-acetylspermidine1 Publication
  3. KM=716 µM for spermine1 Publication
  4. KM=150 µM for N1,N(12)-diacetylspermine1 Publication

    Pathwayi: spermine metabolism

    This protein is involved in the pathway spermine metabolism, which is part of Amine and polyamine metabolism.
    View all proteins of this organism that are known to be involved in the pathway spermine metabolism and in Amine and polyamine metabolism.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14466.
    BRENDAi1.5.3.13. 3474.
    ReactomeiR-MMU-141334. PAOs oxidise polyamines to amines.
    R-MMU-351200. Interconversion of polyamines.
    UniPathwayiUPA00826.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC:1.5.3.13)
    Alternative name(s):
    Polyamine oxidase
    Gene namesi
    Name:Paox
    Synonyms:Pao
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 7

    Organism-specific databases

    MGIiMGI:1916983. Paox.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    Pathology & Biotechi

    Chemistry

    ChEMBLiCHEMBL3408.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 504504Peroxisomal N(1)-acetyl-spermine/spermidine oxidasePRO_0000099876Add
    BLAST

    Proteomic databases

    EPDiQ8C0L6.
    MaxQBiQ8C0L6.
    PaxDbiQ8C0L6.
    PeptideAtlasiQ8C0L6.
    PRIDEiQ8C0L6.

    PTM databases

    iPTMnetiQ8C0L6.
    PhosphoSiteiQ8C0L6.

    Expressioni

    Tissue specificityi

    Widely expressed at different developmental stages. Expressed at high level in the liver and the stomach, expressed at lower level in heart, spleen, thymus, small intestine, muscle, pancreas, uterus, and breast and expressed at very low level in brain, kidney, lung, testis, skin, adrenal gland and prostate gland.1 Publication

    Developmental stagei

    Expression increased during embryonic development: there is a gradual increase in the tissues on going from 8.5 to 19 day embryos. In the breast, expression is very low in virgin mouse and quite high in pregnant mouse, but decreases in lactating and involuting breasts.

    Inductioni

    By polyamine analogs.

    Gene expression databases

    BgeeiQ8C0L6.
    CleanExiMM_PAOX.
    ExpressionAtlasiQ8C0L6. baseline and differential.
    GenevisibleiQ8C0L6. MM.

    Interactioni

    Subunit structurei

    Monomer.

    GO - Molecular functioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000026537.

    Chemistry

    BindingDBiQ8C0L6.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C0L6.
    SMRiQ8C0L6. Positions 5-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi502 – 5043Microbody targeting signalSequence analysis

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Phylogenomic databases

    eggNOGiKOG0685. Eukaryota.
    ENOG410XQW0. LUCA.
    GeneTreeiENSGT00530000062888.
    HOGENOMiHOG000037651.
    HOVERGENiHBG053499.
    InParanoidiQ8C0L6.
    KOiK00308.
    OMAiLESEYME.
    OrthoDBiEOG751NFD.
    PhylomeDBiQ8C0L6.
    TreeFamiTF318348.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q8C0L6-1) [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

            10         20         30         40         50
    MAFPGPRVLV VGSGIAGLGA AQKLCSHRAA PHLRVLEATA SAGGRIRSER
    60 70 80 90 100
    CFGGVVELGA HWIHGPSQDN PVFQLAAEFG LLGEKELSEE NQLVDTGGHV
    110 120 130 140 150
    ALPSMIWSSS GTSVSLELMT EMARLFYGLI ERTREFLNES ETPMASVGEF
    160 170 180 190 200
    LKKEISQQVA SWTEDDEDTR KRKLAILNTF FNIECCVSGT HSMDLVALAP
    210 220 230 240 250
    FGEYTVLPGL DCILAGGYQG LTDRILASLP KDTVAFDKPV KTIHWNGSFQ
    260 270 280 290 300
    EAAFPGETFP VLVECEDGAR LPAHHVIVTV PLGFLKEHQD TFFEPPLPAK
    310 320 330 340 350
    KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS PLQDTALSLQ
    360 370 380 390 400
    DTWFKKLIGF LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL
    410 420 430 440 450
    RRVTGNPQLP AAKSVRRSQW HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP
    460 470 480 490 500
    EDGTGTQLQV LFAGEATHRT FYSTTHGALL SGWREADRLV SLWDSQVEQS

    RPRL
    Length:504
    Mass (Da):55,447
    Last modified:January 23, 2007 - v3
    Checksum:iB40BD34C7A0B98F1
    GO
    Isoform 2 (identifier: Q8C0L6-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-280: Missing.
         281-282: PL → ME

    Show »
    Length:224
    Mass (Da):25,262
    Checksum:i840DF789F62CFE3F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 280280Missing in isoform 2. 1 PublicationVSP_011263Add
    BLAST
    Alternative sequencei281 – 2822PL → ME in isoform 2. 1 PublicationVSP_011264

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF226656 mRNA. Translation: AAN40705.2.
    AK030664 mRNA. Translation: BAC27070.1.
    BC033913 mRNA. Translation: AAH33913.1.
    BC082783 mRNA. Translation: AAH82783.1.
    CCDSiCCDS21965.1. [Q8C0L6-1]
    RefSeqiNP_722478.2. NM_153783.4. [Q8C0L6-1]
    UniGeneiMm.486735.

    Genome annotation databases

    EnsembliENSMUST00000026537; ENSMUSP00000026537; ENSMUSG00000025464. [Q8C0L6-1]
    GeneIDi212503.
    KEGGimmu:212503.
    UCSCiuc009kha.1. mouse. [Q8C0L6-2]
    uc009khb.1. mouse. [Q8C0L6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF226656 mRNA. Translation: AAN40705.2.
    AK030664 mRNA. Translation: BAC27070.1.
    BC033913 mRNA. Translation: AAH33913.1.
    BC082783 mRNA. Translation: AAH82783.1.
    CCDSiCCDS21965.1. [Q8C0L6-1]
    RefSeqiNP_722478.2. NM_153783.4. [Q8C0L6-1]
    UniGeneiMm.486735.

    3D structure databases

    ProteinModelPortaliQ8C0L6.
    SMRiQ8C0L6. Positions 5-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000026537.

    Chemistry

    BindingDBiQ8C0L6.
    ChEMBLiCHEMBL3408.

    PTM databases

    iPTMnetiQ8C0L6.
    PhosphoSiteiQ8C0L6.

    Proteomic databases

    EPDiQ8C0L6.
    MaxQBiQ8C0L6.
    PaxDbiQ8C0L6.
    PeptideAtlasiQ8C0L6.
    PRIDEiQ8C0L6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000026537; ENSMUSP00000026537; ENSMUSG00000025464. [Q8C0L6-1]
    GeneIDi212503.
    KEGGimmu:212503.
    UCSCiuc009kha.1. mouse. [Q8C0L6-2]
    uc009khb.1. mouse. [Q8C0L6-1]

    Organism-specific databases

    CTDi196743.
    MGIiMGI:1916983. Paox.

    Phylogenomic databases

    eggNOGiKOG0685. Eukaryota.
    ENOG410XQW0. LUCA.
    GeneTreeiENSGT00530000062888.
    HOGENOMiHOG000037651.
    HOVERGENiHBG053499.
    InParanoidiQ8C0L6.
    KOiK00308.
    OMAiLESEYME.
    OrthoDBiEOG751NFD.
    PhylomeDBiQ8C0L6.
    TreeFamiTF318348.

    Enzyme and pathway databases

    UniPathwayiUPA00826.
    BioCyciMetaCyc:MONOMER-14466.
    BRENDAi1.5.3.13. 3474.
    ReactomeiR-MMU-141334. PAOs oxidise polyamines to amines.
    R-MMU-351200. Interconversion of polyamines.

    Miscellaneous databases

    PROiQ8C0L6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8C0L6.
    CleanExiMM_PAOX.
    ExpressionAtlasiQ8C0L6. baseline and differential.
    GenevisibleiQ8C0L6. MM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase."
      Wu T., Yankovskaya V., McIntire W.S.
      J. Biol. Chem. 278:20514-20525(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Head.
    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] (ISOFORMS 1 AND 2).
      Strain: FVB/N.
      Tissue: Colon and Mammary gland.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

    Entry informationi

    Entry nameiPAOX_MOUSE
    AccessioniPrimary (citable) accession number: Q8C0L6
    Secondary accession number(s): Q8K254
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: January 23, 2007
    Last modified: July 6, 2016
    This is version 110 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Oxidizes N(1)-acetylated polyamines on the exo-side of their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side of the N(4)-nitrogen (By similarity).By similarity
    N-ethylated polyamines are also good substrates for this enzyme: they have been used for cancer clinical trials. They down-regulate polyamine biosynthetic enzymes, but dramatically up-regulate SSAT synthesis, which results in mammalian cells becoming apaptotic.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    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 one 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.