ID   PAOX_BOVIN              Reviewed;         512 AA.
AC   Q865R1; Q4PS79;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 3.
DT   25-NOV-2008, entry version 35.
DE   RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
DE            EC=1.5.3.11;
DE   AltName: Full=Polyamine oxidase;
DE   Flags: Precursor;
GN   Name=PAOX; Synonyms=PAO;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Ferretti L., Uboldi C., Del Vecchio I., Eggen A., Brunner R.,
RA   Iannuzzi L.;
RT   "Comparative mapping of the bovine SPRN locus.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 62-512, PROTEIN SEQUENCE OF 7-27; 57-76
RP   AND 497-511, AND CHARACTERIZATION.
RC   TISSUE=Liver;
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).
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.
CC   -!- CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O = N(1)-
CC       acetylspermidine + 3-aminopropanal + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). Cytoplasm (By
CC       similarity).
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   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
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DR   EMBL; DQ058607; AAY83881.1; -; mRNA.
DR   EMBL; DQ058602; AAY83877.1; -; Genomic_DNA.
DR   EMBL; AF226658; AAN40707.1; -; mRNA.
DR   RefSeq; NP_001013620.2; -.
DR   UniGene; Bt.36568; -.
DR   Ensembl; ENSBTAG00000018321; Bos taurus.
DR   GeneID; 282639; -.
DR   KEGG; bta:282639; -.
DR   HOVERGEN; Q865R1; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046592; F:polyamine oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW   Oxidoreductase; Peroxisome.
FT   PROPEP        1      6
FT                                /FTId=PRO_0000236802.
FT   CHAIN         7    512       Peroxisomal N(1)-acetyl-
FT                                spermine/spermidine oxidase.
FT                                /FTId=PRO_0000099874.
FT   MOTIF       510    512       Microbody targeting signal (Potential).
FT   CONFLICT      7      7       Q -> E (in Ref. 2; AA sequence).
FT   CONFLICT    482    482       T -> P (in Ref. 2; AAN40707).
SQ   SEQUENCE   512 AA;  56325 MW;  6164E3A77841F36F CRC64;
     MQSGGRQAEA PGRGPRVLVV GGGIAGLGAA QRLCRHPAFS HLRVLEATAR AGGRIRSEHS
     FGGVVEVGAH WIHGPSQGNP VFQLAAKYGL LGEKALSEEN QLIETGGHVG LPSVSYASSG
     VSVSLELVAE MASLFYSLID QTREFLQAAE TTPPSVGEYL KEKIRQHMAG WTEDEETKKL
     KLAILKNLFN VECCVSGTHS MDLVALAPFG EYTVLPGLDC TFPEGYQGLT DCIMASLPKD
     VMVFDKPVKT IHWNGSFREA SAPGETFPVL VECEDGDCFP AHHVVVTVPL GFFKKHLDTF
     FEPPLPTEKV EAIRKIGFGT NNKIFLEFEE PFWEPDCQHI QVVWEDMSPL EDTAPELQDA
     WFKKLIGFWV LPPFQASHVL CGFIAGLESE FMETLSDEDV LRSLTQVLRR VTGNPQLPAP
     RSMLRSCWHS APYTRGSYSY VAVGSSGDDM DRLAQPLPSD GKGAQLQVLF AGEATHRTFY
     STTHGALLSG WREADRLMTL WDPQAQWPEP RL
//