Reviewed, UniProtKB/Swiss-Prot Q8C0L6 (PAOX_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
    EC=1.5.3.11
Alternative name(s):
    Polyamine oxidase

Gene names

Name:	Paox
Synonyms:	Pao

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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 > N(1),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 activity	N(1)-acetylspermine + O(2) + H(2)O = N(1)-acetylspermidine + 3-aminopropanal + H(2)O(2).
Cofactor	FAD.
Pathway	Amine and polyamine metabolism; spermine metabolism.
Subunit structure	Monomer.
Subcellular location	PeroxisomeBy similarity. CytoplasmBy similarity.
Tissue specificity	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.
Developmental stage	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.
Induction	By polyamine analogs.
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. 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.
Sequence similarities	Belongs to the flavin monoamine oxidase family.

Ontologies

Keywords
Cellular component	Cytoplasm Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW polyamine catabolic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro polyamine oxidase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8C0L6-1)

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.

Isoform 2 (identifier: Q8C0L6-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 504	503	Peroxisomal N(1)-acetyl-spermine/spermidine oxidase		PRO_0000099876
Regions
	Motif	502 – 504	3	Microbody targeting signal Potential
Natural variations
	Alternative sequence	1 – 280	280	Missing in isoform 2.		VSP_011263
	Alternative sequence	281 – 282	2	PL → ME in isoform 2.		VSP_011264

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B40BD34C7A0B98F1	FASTA	504	55,447
	10 20 30 40 50 60 MAFPGPRVLV VGSGIAGLGA AQKLCSHRAA PHLRVLEATA SAGGRIRSER CFGGVVELGA 70 80 90 100 110 120 HWIHGPSQDN PVFQLAAEFG LLGEKELSEE NQLVDTGGHV ALPSMIWSSS GTSVSLELMT 130 140 150 160 170 180 EMARLFYGLI ERTREFLNES ETPMASVGEF LKKEISQQVA SWTEDDEDTR KRKLAILNTF 190 200 210 220 230 240 FNIECCVSGT HSMDLVALAP FGEYTVLPGL DCILAGGYQG LTDRILASLP KDTVAFDKPV 250 260 270 280 290 300 KTIHWNGSFQ EAAFPGETFP VLVECEDGAR LPAHHVIVTV PLGFLKEHQD TFFEPPLPAK 310 320 330 340 350 360 KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS PLQDTALSLQ DTWFKKLIGF 370 380 390 400 410 420 LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL RRVTGNPQLP AAKSVRRSQW 430 440 450 460 470 480 HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP EDGTGTQLQV LFAGEATHRT FYSTTHGALL 490 500 SGWREADRLV SLWDSQVEQS RPRL
	Isoform 2 [UniParc]. Checksum: 840DF789F62CFE3F		224	25,262
	10 20 30 40 50 60 MEGFLKEHQD TFFEPPLPAK KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS 70 80 90 100 110 120 PLQDTALSLQ DTWFKKLIGF LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL 130 140 150 160 170 180 RRVTGNPQLP AAKSVRRSQW HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP EDGTGTQLQV 190 200 210 220 LFAGEATHRT FYSTTHGALL SGWREADRLV SLWDSQVEQS RPRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12660232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, COFACTOR.
[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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: FVB/N. Tissue: Colon and Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF226656 mRNA. Translation: AAN40705.2. AK030664 mRNA. Translation: BAC27070.1. BC033913 mRNA. Translation: AAH33913.1. BC082783 mRNA. Translation: AAH82783.1.
RefSeq	NP_722478.2.
UniGene	Mm.44197
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000025464. Mus musculus. [Contig view]
GeneID	212503.
KEGG	mmu:212503.
Organism-specific databases
MGI	MGI:1916983. Paox.
Phylogenomic databases
HOGENOM	Q8C0L6.
HOVERGEN	Q8C0L6.
Gene expression databases
CleanEx	MM_PAOX.
GermOnline	ENSMUSG00000025464. Mus musculus.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	373584.
SOURCE	Search...

Entry information

Entry name

PAOX_MOUSE

Accession

Primary (citable) accession number: Q8C0L6
Secondary accession number(s): Q8K254

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 45 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)