ID   PAOX_MOUSE              Reviewed;         504 AA.
AC   Q8C0L6; Q8K254;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
DE            EC=1.5.3.n3;
DE            EC=1.5.3.n4;
DE            EC=1.5.3.n10;
DE   AltName: Full=Polyamine oxidase;
GN   Name=Paox; Synonyms=Pao;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, COFACTOR,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=22662280; PubMed=12660232; DOI=10.1074/jbc.M302149200;
RA   Wu T., Yankovskaya V., McIntire W.S.;
RT   "Cloning, sequencing, and heterologous expression of the murine
RT   peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase.";
RL   J. Biol. Chem. 278:20514-20525(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-
CC       acetylspermine to spermidine and is thus involved in the polyamine
CC       back-conversion. Can also oxidize N(1)-acetylspermidine to
CC       putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-
CC       acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not
CC       oxidize spermidine. Plays an important role in the regulation of
CC       polyamine intracellular concentration and has the potential to act
CC       as a determinant of cellular sensitivity to the antitumor
CC       polyamine analogs.
CC   -!- CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O =
CC       spermidine + 3-acetamidopropanal + H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: N(1)-acetylspermidine + O(2) + H(2)O =
CC       putrescine + 3-acetamidopropanal + H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: N(1),N(12)-diacetylspermine + O(2) + H(2)O =
CC       N(1)-acetylspermidine + 3-acetamidobutanal + H(2)O(2).
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.78 uM for N(1)-acetylspermine;
CC         KM=36.8 uM for N(1)-acetylspermidine;
CC         KM=716 uM for spermine;
CC         KM=150 uM for N(1),N(12)-diacetylspermine;
CC   -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C0L6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0L6-2; Sequence=VSP_011263, VSP_011264;
CC   -!- TISSUE SPECIFICITY: Widely expressed at different developmental
CC       stages. Expressed at high level in the liver and the stomach,
CC       expressed at lower level in heart, spleen, thymus, small
CC       intestine, muscle, pancreas, uterus, and breast and expressed at
CC       very low level in brain, kidney, lung, testis, skin, adrenal gland
CC       and prostate gland.
CC   -!- DEVELOPMENTAL STAGE: Expression increased during embryonic
CC       development: there is a gradual increase in the tissues on going
CC       from 8.5 to 19 day embryos. In the breast, expression is very low
CC       in virgin mouse and quite high in pregnant mouse, but decreases in
CC       lactating and involuting breasts.
CC   -!- INDUCTION: By polyamine analogs.
CC   -!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side
CC       of their N(4)-amino groups. Plant PAO oxidizes spermine on the
CC       endo-side of the N(4)-nitrogen (By similarity).
CC   -!- MISCELLANEOUS: N-ethylated polyamines are also good substrates for
CC       this enzyme: they have been used for cancer clinical trials. They
CC       down-regulate polyamine biosynthetic enzymes, but dramatically up-
CC       regulate SSAT synthesis, which results in mammalian cells becoming
CC       apaptotic.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF226656; AAN40705.2; -; mRNA.
DR   EMBL; AK030664; BAC27070.1; -; mRNA.
DR   EMBL; BC033913; AAH33913.1; -; mRNA.
DR   EMBL; BC082783; AAH82783.1; -; mRNA.
DR   IPI; IPI00223861; -.
DR   IPI; IPI00279917; -.
DR   RefSeq; NP_722478.2; -.
DR   UniGene; Mm.44197; -.
DR   PRIDE; Q8C0L6; -.
DR   Ensembl; ENSMUSG00000025464; Mus musculus.
DR   GeneID; 212503; -.
DR   KEGG; mmu:212503; -.
DR   MGI; MGI:1916983; Paox.
DR   HOGENOM; Q8C0L6; -.
DR   HOVERGEN; Q8C0L6; -.
DR   OMA; Q8C0L6; VWEDTSP.
DR   BRENDA; 1.5.3.11; 244.
DR   NextBio; 373584; -.
DR   Bgee; Q8C0L6; -.
DR   CleanEx; MM_PAOX; -.
DR   GermOnline; ENSMUSG00000025464; Mus musculus.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006598; P:polyamine catabolic process; IDA:MGI.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Peroxisome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    504       Peroxisomal N(1)-acetyl-
FT                                spermine/spermidine oxidase.
FT                                /FTId=PRO_0000099876.
FT   MOTIF       502    504       Microbody targeting signal (Potential).
FT   VAR_SEQ       1    280       Missing (in isoform 2).
FT                                /FTId=VSP_011263.
FT   VAR_SEQ     281    282       PL -> ME (in isoform 2).
FT                                /FTId=VSP_011264.
SQ   SEQUENCE   504 AA;  55447 MW;  B40BD34C7A0B98F1 CRC64;
     MAFPGPRVLV VGSGIAGLGA AQKLCSHRAA PHLRVLEATA SAGGRIRSER CFGGVVELGA
     HWIHGPSQDN PVFQLAAEFG LLGEKELSEE NQLVDTGGHV ALPSMIWSSS GTSVSLELMT
     EMARLFYGLI ERTREFLNES ETPMASVGEF LKKEISQQVA SWTEDDEDTR KRKLAILNTF
     FNIECCVSGT HSMDLVALAP FGEYTVLPGL DCILAGGYQG LTDRILASLP KDTVAFDKPV
     KTIHWNGSFQ EAAFPGETFP VLVECEDGAR LPAHHVIVTV PLGFLKEHQD TFFEPPLPAK
     KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS PLQDTALSLQ DTWFKKLIGF
     LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL RRVTGNPQLP AAKSVRRSQW
     HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP EDGTGTQLQV LFAGEATHRT FYSTTHGALL
     SGWREADRLV SLWDSQVEQS RPRL
//