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Spermine oxidase (EC 1.5.3.16) (Polyamine oxidase 1) (PAO-1) (PAOh1)

 SMOX_MOUSE              Reviewed;         555 AA.
Q99K82; A2ANQ8; A2ANQ9; A2ANR0; A2ANR1; A2ANR2; Q70LA3; Q70LA4;
Q70LA5; Q70LA7; Q70LA8; Q70LA9; Q70LB0; Q8CJ56; Q8CJ57;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Spermine oxidase;
EC=1.5.3.16;
AltName: Full=Polyamine oxidase 1;
Short=PAO-1;
Short=PAOh1;
Name=Smox; Synonyms=Smo;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7 AND 10), TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=DBA/2J; TISSUE=Brain;
PubMed=14764092; DOI=10.1111/j.1432-1033.2004.03979.x;
Cervelli M., Bellini A., Bianchi M., Marcocci L., Nocera S.,
Polticelli F., Federico R., Amendola R., Mariottini P.;
"Mouse spermine oxidase gene splice variants. Nuclear subcellular
localization of a novel active isoform.";
Eur. J. Biochem. 271:760-770(2004).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS 1; 8 AND 9).
TISSUE=Liver;
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-320.
PubMed=12141946; DOI=10.1042/BJ20020720;
Vujcic S., Diegelman P., Bacchi C.J., Kramer D.L., Porter C.W.;
"Identification and characterization of a novel flavin-containing
spermine oxidase of mammalian cell origin.";
Biochem. J. 367:665-675(2002).
-!- FUNCTION: Flavoenzyme which catalyzes the oxidation of spermine to
spermidine. Can also use N(1)-acetylspermine and spermidine as
substrates, with different affinity depending on the isoform
(isozyme) and on the experimental conditions. 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. May contribute to
beta-alanine production via aldehyde dehydrogenase conversion of
3-amino-propanal.
-!- CATALYTIC ACTIVITY: Spermine + O(2) + H(2)O = spermidine + 3-
aminopropanal + H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- PATHWAY: Amine and polyamine degradation; spermine degradation.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14764092}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1; Synonyms=Alpha, Polyamine oxidase-l;
IsoId=Q99K82-1; Sequence=Displayed;
Note=Major isoform.;
Name=2; Synonyms=Mu;
IsoId=Q99K82-2; Sequence=VSP_011137;
Note=Active. Nuclear and cytoplasmic.;
Name=3; Synonyms=Eta;
IsoId=Q99K82-3; Sequence=VSP_011131;
Name=4; Synonyms=Omega;
IsoId=Q99K82-4; Sequence=VSP_011128, VSP_011132;
Name=5; Synonyms=Phi;
IsoId=Q99K82-5; Sequence=VSP_011130;
Name=6; Synonyms=Beta;
IsoId=Q99K82-6; Sequence=VSP_011136, VSP_011138;
Name=7; Synonyms=Gamma;
IsoId=Q99K82-7; Sequence=VSP_011135, VSP_011138;
Note=No detectable activity. Cytoplasmic.;
Name=8; Synonyms=Polyamine oxidase-m;
IsoId=Q99K82-8; Sequence=VSP_011134;
Name=9; Synonyms=Polyamine oxidase-s;
IsoId=Q99K82-9; Sequence=VSP_011129, VSP_011133;
Name=10; Synonyms=Delta;
IsoId=Q99K82-10; Sequence=VSP_011127;
Note=No detectable activity. Cytoplasmic.;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are
expressed at higher level in brain and skeletal muscle. Isoform 7
is found in brain and spleen, isoform 10 is widely expressed but
found at lower level in heart, kidney, liver and lung.
{ECO:0000269|PubMed:14764092}.
-!- INDUCTION: By antitumor polyamine analogs. {ECO:0000305}.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ567473; CAD98866.1; -; mRNA.
EMBL; AJ567474; CAD98867.1; -; mRNA.
EMBL; AJ567475; CAD98868.1; -; mRNA.
EMBL; AJ567476; CAD98869.1; -; mRNA.
EMBL; AJ567477; CAD98870.1; -; mRNA.
EMBL; AJ567478; CAD98871.1; -; mRNA.
EMBL; AJ567479; CAD98872.1; -; mRNA.
EMBL; AJ567480; CAD98873.1; -; mRNA.
EMBL; AF495851; AAN32908.1; -; mRNA.
EMBL; AF495852; AAN32909.1; -; mRNA.
EMBL; AF495853; AAN32910.1; -; mRNA.
EMBL; AF498364; AAN32915.1; -; Genomic_DNA.
EMBL; AL831781; CAM20374.1; -; Genomic_DNA.
EMBL; AL831731; CAM20374.1; JOINED; Genomic_DNA.
EMBL; AL831781; CAM20375.1; -; Genomic_DNA.
EMBL; AL831731; CAM20375.1; JOINED; Genomic_DNA.
EMBL; AL831781; CAM20376.1; -; Genomic_DNA.
EMBL; AL831731; CAM20376.1; JOINED; Genomic_DNA.
EMBL; AL831781; CAM20378.1; -; Genomic_DNA.
EMBL; AL831731; CAM20378.1; JOINED; Genomic_DNA.
EMBL; AL831781; CAM20379.1; -; Genomic_DNA.
EMBL; AL831731; CAM20379.1; JOINED; Genomic_DNA.
EMBL; AL831731; CAM24528.1; -; Genomic_DNA.
EMBL; AL831781; CAM24528.1; JOINED; Genomic_DNA.
EMBL; AL831731; CAM24529.1; -; Genomic_DNA.
EMBL; AL831781; CAM24529.1; JOINED; Genomic_DNA.
EMBL; AL831731; CAM24530.1; -; Genomic_DNA.
EMBL; AL831781; CAM24530.1; JOINED; Genomic_DNA.
EMBL; AL831731; CAM24531.1; -; Genomic_DNA.
EMBL; AL831781; CAM24531.1; JOINED; Genomic_DNA.
EMBL; AL831731; CAM24532.1; -; Genomic_DNA.
EMBL; AL831781; CAM24532.1; JOINED; Genomic_DNA.
EMBL; BC004831; AAH04831.1; -; mRNA.
CCDS; CCDS16763.1; -. [Q99K82-1]
CCDS; CCDS50718.1; -. [Q99K82-8]
CCDS; CCDS50719.1; -. [Q99K82-2]
CCDS; CCDS50720.1; -. [Q99K82-6]
CCDS; CCDS50721.1; -. [Q99K82-7]
CCDS; CCDS50724.1; -. [Q99K82-5]
CCDS; CCDS50725.1; -. [Q99K82-10]
RefSeq; NP_001171304.1; NM_001177833.1. [Q99K82-2]
RefSeq; NP_001171305.1; NM_001177834.1. [Q99K82-6]
RefSeq; NP_001171306.1; NM_001177835.1. [Q99K82-7]
RefSeq; NP_001171307.1; NM_001177836.1. [Q99K82-8]
RefSeq; NP_001171309.1; NM_001177838.1. [Q99K82-5]
RefSeq; NP_001171310.1; NM_001177839.1.
RefSeq; NP_001171311.1; NM_001177840.1. [Q99K82-10]
RefSeq; NP_663508.1; NM_145533.2. [Q99K82-1]
RefSeq; XP_006499350.1; XM_006499287.3. [Q99K82-2]
RefSeq; XP_006499351.1; XM_006499288.2. [Q99K82-2]
UniGene; Mm.136586; -.
ProteinModelPortal; Q99K82; -.
SMR; Q99K82; -.
iPTMnet; Q99K82; -.
PhosphoSitePlus; Q99K82; -.
PRIDE; Q99K82; -.
Ensembl; ENSMUST00000028806; ENSMUSP00000028806; ENSMUSG00000027333. [Q99K82-1]
Ensembl; ENSMUST00000110180; ENSMUSP00000105809; ENSMUSG00000027333. [Q99K82-8]
Ensembl; ENSMUST00000110182; ENSMUSP00000105811; ENSMUSG00000027333. [Q99K82-10]
Ensembl; ENSMUST00000110183; ENSMUSP00000105812; ENSMUSG00000027333. [Q99K82-5]
Ensembl; ENSMUST00000110186; ENSMUSP00000105815; ENSMUSG00000027333. [Q99K82-2]
Ensembl; ENSMUST00000110188; ENSMUSP00000105817; ENSMUSG00000027333. [Q99K82-6]
Ensembl; ENSMUST00000110189; ENSMUSP00000105818; ENSMUSG00000027333. [Q99K82-7]
Ensembl; ENSMUST00000183947; ENSMUSP00000139278; ENSMUSG00000027333. [Q99K82-4]
GeneID; 228608; -.
KEGG; mmu:228608; -.
UCSC; uc008mlm.2; mouse. [Q99K82-1]
UCSC; uc008mln.2; mouse. [Q99K82-2]
UCSC; uc008mlp.2; mouse. [Q99K82-8]
UCSC; uc008mls.2; mouse. [Q99K82-10]
UCSC; uc008mlt.2; mouse. [Q99K82-6]
UCSC; uc012cep.1; mouse. [Q99K82-7]
UCSC; uc012ceq.1; mouse. [Q99K82-5]
CTD; 54498; -.
MGI; MGI:2445356; Smox.
GeneTree; ENSGT00530000062888; -.
HOVERGEN; HBG053499; -.
InParanoid; Q99K82; -.
KO; K12259; -.
OMA; HTHSSFY; -.
OrthoDB; EOG091G06OV; -.
PhylomeDB; Q99K82; -.
TreeFam; TF318348; -.
BRENDA; 1.5.3.16; 3474.
Reactome; R-MMU-141334; PAOs oxidise polyamines to amines.
Reactome; R-MMU-351200; Interconversion of polyamines.
UniPathway; UPA00211; -.
PRO; PR:Q99K82; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027333; -.
CleanEx; MM_SMO; -.
CleanEx; MM_SMOX; -.
ExpressionAtlas; Q99K82; baseline and differential.
Genevisible; Q99K82; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI.
GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0006598; P:polyamine catabolic process; ISO:MGI.
GO; GO:0046208; P:spermine catabolic process; IDA:MGI.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR036188; FAD/NAD-bd_sf.
Pfam; PF01593; Amino_oxidase; 2.
SUPFAM; SSF51905; SSF51905; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; FAD; Flavoprotein;
Nucleus; Oxidoreductase; Reference proteome.
CHAIN 1 555 Spermine oxidase.
/FTId=PRO_0000099878.
VAR_SEQ 146 510 Missing (in isoform 10).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011127.
VAR_SEQ 204 510 Missing (in isoform 5).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011130.
VAR_SEQ 204 243 VESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVV
-> GTPIYQNLGESCAQPGAATHTSGVPIPTHRWAQVGRMW
RS (in isoform 9). {ECO:0000305}.
/FTId=VSP_011129.
VAR_SEQ 204 209 VESCES -> SAMAMC (in isoform 4).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011128.
VAR_SEQ 205 555 ESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVVEL
LAEGIPPHVIQLGKPVRCIHWDQASAHPRGPEIEPRGEGDH
NHDTGEGGQSGENPQQGRWDEDEPWPVVVECEDCEVIPADH
VIVTVSLGVLKRQYTSFFRPCLPTEKVAAIHRLGIGTTDKI
FLEFEEPFWGPECNSLQFVWEDEAESCTLTYPPELWYRKIC
GFDVLYPPERYGHVLSGWICGEEALVMERCDDEAVAEICTE
MLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSG
ADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGA
LLSGQREAARLIEMYRDLFQQGP -> SLLWSIDARVKKMN
SGGVSVQSALLLRALVPCMA (in isoform 3).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011131.
VAR_SEQ 210 555 Missing (in isoform 4).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011132.
VAR_SEQ 244 255 Missing (in isoform 9). {ECO:0000305}.
/FTId=VSP_011133.
VAR_SEQ 282 417 Missing (in isoform 8). {ECO:0000305}.
/FTId=VSP_011134.
VAR_SEQ 457 512 GNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKL
AKPLPYTESSKTAPM -> AHAGALLRGGHTP (in
isoform 7).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011135.
VAR_SEQ 458 512 NPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLA
KPLPYTESSKTAPM -> GLKWGGCGEASQAPALHRELQDS
AHAGALLRGGHTP (in isoform 6).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011136.
VAR_SEQ 510 510 A -> AHRSSTEQQPGHLLPSKCPEQSLDPSRGSIK (in
isoform 2).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011137.
VAR_SEQ 516 555 FSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGP
-> LHHPRCSALWPARGRPAHRDVPRPLPAGALKGVLTAKC
VP (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:14764092}.
/FTId=VSP_011138.
MUTAGEN 320 320 C->R: No change in enzymatic activity.
{ECO:0000269|PubMed:12141946}.
SEQUENCE 555 AA; 61852 MW; A297E9DBD094EA74 CRC64;
MQSCESSGDS ADDPLSRGLR RRGQPRVVVI GAGLAGLAAA RALLEQGFTD VTVLEASSHI
GGRVQSVRLG DTTFELGATW IHGSHGNPIY QLAEANGLLE ETTDGERSVG RISLYSKNGV
ACYLTNRGCR IPKDVVEEFS DLYNEVYNMT QEFFRHGKPV NAESQNSVGV FTREKVRNRI
RDDPDDTEAT KRLKLAMIQQ YLKVESCESS SHSIDEVSLS AFGEWTEIPG AHHIIPSGFM
RVVELLAEGI PPHVIQLGKP VRCIHWDQAS AHPRGPEIEP RGEGDHNHDT GEGGQSGENP
QQGRWDEDEP WPVVVECEDC EVIPADHVIV TVSLGVLKRQ YTSFFRPCLP TEKVAAIHRL
GIGTTDKIFL EFEEPFWGPE CNSLQFVWED EAESCTLTYP PELWYRKICG FDVLYPPERY
GHVLSGWICG EEALVMERCD DEAVAEICTE MLRQFTGNPN IPKPRRILRS AWGSNPYFRG
SYSYTQVGSS GADVEKLAKP LPYTESSKTA PMQVLFSGEA THRKYYSTTH GALLSGQREA
ARLIEMYRDL FQQGP


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