SMOX_MOUSE
ID SMOX_MOUSE Reviewed; 555 AA.
AC Q99K82; A2ANQ8; A2ANQ9; A2ANR0; A2ANR1; A2ANR2; Q70LA3; Q70LA4; Q70LA5;
AC Q70LA7; Q70LA8; Q70LA9; Q70LB0; Q8CJ56; Q8CJ57;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Spermine oxidase;
DE EC=1.5.3.16 {ECO:0000269|PubMed:12141946, ECO:0000269|PubMed:14764092};
DE AltName: Full=Polyamine oxidase 1;
DE Short=PAO-1;
DE Short=PAOh1;
GN Name=Smox; Synonyms=Smo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7 AND 10), CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=DBA/2J; TISSUE=Brain;
RX PubMed=14764092; DOI=10.1111/j.1432-1033.2004.03979.x;
RA Cervelli M., Bellini A., Bianchi M., Marcocci L., Nocera S., Polticelli F.,
RA Federico R., Amendola R., Mariottini P.;
RT "Mouse spermine oxidase gene splice variants. Nuclear subcellular
RT localization of a novel active isoform.";
RL Eur. J. Biochem. 271:760-770(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 8 AND 9).
RC TISSUE=Liver;
RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-320.
RX PubMed=12141946; DOI=10.1042/bj20020720;
RA Vujcic S., Diegelman P., Bacchi C.J., Kramer D.L., Porter C.W.;
RT "Identification and characterization of a novel flavin-containing spermine
RT oxidase of mammalian cell origin.";
RL Biochem. J. 367:665-675(2002).
CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of spermine to
CC spermidine. Can also use N(1)-acetylspermine and spermidine as
CC substrates, with different affinity depending on the isoform (isozyme)
CC and on the experimental conditions. Plays an important role in the
CC regulation of polyamine intracellular concentration and has the
CC potential to act as a determinant of cellular sensitivity to the
CC antitumor polyamine analogs. May contribute to beta-alanine production
CC via aldehyde dehydrogenase conversion of 3-amino-propanal.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine;
CC Xref=Rhea:RHEA:25804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:45725, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:58374; EC=1.5.3.16;
CC Evidence={ECO:0000269|PubMed:12141946, ECO:0000269|PubMed:14764092};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8C0L6};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q8C0L6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for spermine {ECO:0000269|PubMed:14764092};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000269|PubMed:14764092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14764092}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=Alpha, Polyamine oxidase-l;
CC IsoId=Q99K82-1; Sequence=Displayed;
CC Name=2; Synonyms=Mu;
CC IsoId=Q99K82-2; Sequence=VSP_011137;
CC Name=3; Synonyms=Eta;
CC IsoId=Q99K82-3; Sequence=VSP_011131;
CC Name=4; Synonyms=Omega;
CC IsoId=Q99K82-4; Sequence=VSP_011128, VSP_011132;
CC Name=5; Synonyms=Phi;
CC IsoId=Q99K82-5; Sequence=VSP_011130;
CC Name=6; Synonyms=Beta;
CC IsoId=Q99K82-6; Sequence=VSP_011136, VSP_011138;
CC Name=7; Synonyms=Gamma;
CC IsoId=Q99K82-7; Sequence=VSP_011135, VSP_011138;
CC Name=8; Synonyms=Polyamine oxidase-m;
CC IsoId=Q99K82-8; Sequence=VSP_011134;
CC Name=9; Synonyms=Polyamine oxidase-s;
CC IsoId=Q99K82-9; Sequence=VSP_011129, VSP_011133;
CC Name=10; Synonyms=Delta;
CC IsoId=Q99K82-10; Sequence=VSP_011127;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are
CC expressed at higher level in brain and skeletal muscle. Isoform 7 is
CC found in brain and spleen, isoform 10 is widely expressed but found at
CC lower level in heart, kidney, liver and lung.
CC {ECO:0000269|PubMed:14764092}.
CC -!- INDUCTION: By antitumor polyamine analogs. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: Active. Nuclear and cytoplasmic.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: No detectable activity. Cytoplasmic.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: No detectable activity. Cytoplasmic.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AJ567473; CAD98866.1; -; mRNA.
DR EMBL; AJ567474; CAD98867.1; -; mRNA.
DR EMBL; AJ567475; CAD98868.1; -; mRNA.
DR EMBL; AJ567476; CAD98869.1; -; mRNA.
DR EMBL; AJ567477; CAD98870.1; -; mRNA.
DR EMBL; AJ567478; CAD98871.1; -; mRNA.
DR EMBL; AJ567479; CAD98872.1; -; mRNA.
DR EMBL; AJ567480; CAD98873.1; -; mRNA.
DR EMBL; AF495851; AAN32908.1; -; mRNA.
DR EMBL; AF495852; AAN32909.1; -; mRNA.
DR EMBL; AF495853; AAN32910.1; -; mRNA.
DR EMBL; AF498364; AAN32915.1; -; Genomic_DNA.
DR EMBL; AL831731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004831; AAH04831.1; -; mRNA.
DR CCDS; CCDS16763.1; -. [Q99K82-1]
DR CCDS; CCDS50718.1; -. [Q99K82-8]
DR CCDS; CCDS50719.1; -. [Q99K82-2]
DR CCDS; CCDS50720.1; -. [Q99K82-6]
DR CCDS; CCDS50721.1; -. [Q99K82-7]
DR CCDS; CCDS50724.1; -. [Q99K82-5]
DR CCDS; CCDS50725.1; -. [Q99K82-10]
DR RefSeq; NP_001171304.1; NM_001177833.1. [Q99K82-2]
DR RefSeq; NP_001171305.1; NM_001177834.1. [Q99K82-6]
DR RefSeq; NP_001171306.1; NM_001177835.1. [Q99K82-7]
DR RefSeq; NP_001171307.1; NM_001177836.1. [Q99K82-8]
DR RefSeq; NP_001171309.1; NM_001177838.1. [Q99K82-5]
DR RefSeq; NP_001171310.1; NM_001177839.1.
DR RefSeq; NP_001171311.1; NM_001177840.1. [Q99K82-10]
DR RefSeq; NP_663508.1; NM_145533.2. [Q99K82-1]
DR RefSeq; XP_006499350.1; XM_006499287.3. [Q99K82-2]
DR RefSeq; XP_006499351.1; XM_006499288.2. [Q99K82-2]
DR AlphaFoldDB; Q99K82; -.
DR SMR; Q99K82; -.
DR STRING; 10090.ENSMUSP00000105815; -.
DR iPTMnet; Q99K82; -.
DR PhosphoSitePlus; Q99K82; -.
DR CPTAC; non-CPTAC-3385; -.
DR MaxQB; Q99K82; -.
DR PRIDE; Q99K82; -.
DR ProteomicsDB; 261445; -. [Q99K82-1]
DR ProteomicsDB; 261446; -. [Q99K82-2]
DR ProteomicsDB; 261447; -. [Q99K82-3]
DR ProteomicsDB; 261448; -. [Q99K82-4]
DR ProteomicsDB; 261449; -. [Q99K82-5]
DR ProteomicsDB; 261450; -. [Q99K82-6]
DR ProteomicsDB; 261451; -. [Q99K82-7]
DR ProteomicsDB; 261452; -. [Q99K82-8]
DR ProteomicsDB; 261453; -. [Q99K82-9]
DR ProteomicsDB; 261454; -. [Q99K82-10]
DR Antibodypedia; 23782; 129 antibodies from 19 providers.
DR DNASU; 228608; -.
DR Ensembl; ENSMUST00000028806; ENSMUSP00000028806; ENSMUSG00000027333. [Q99K82-1]
DR Ensembl; ENSMUST00000110180; ENSMUSP00000105809; ENSMUSG00000027333. [Q99K82-8]
DR Ensembl; ENSMUST00000110182; ENSMUSP00000105811; ENSMUSG00000027333. [Q99K82-10]
DR Ensembl; ENSMUST00000110183; ENSMUSP00000105812; ENSMUSG00000027333. [Q99K82-5]
DR Ensembl; ENSMUST00000110186; ENSMUSP00000105815; ENSMUSG00000027333. [Q99K82-2]
DR Ensembl; ENSMUST00000110188; ENSMUSP00000105817; ENSMUSG00000027333. [Q99K82-6]
DR Ensembl; ENSMUST00000110189; ENSMUSP00000105818; ENSMUSG00000027333. [Q99K82-7]
DR Ensembl; ENSMUST00000183947; ENSMUSP00000139278; ENSMUSG00000027333. [Q99K82-4]
DR GeneID; 228608; -.
DR KEGG; mmu:228608; -.
DR UCSC; uc008mlm.2; mouse. [Q99K82-1]
DR UCSC; uc008mln.2; mouse. [Q99K82-2]
DR UCSC; uc008mlp.2; mouse. [Q99K82-8]
DR UCSC; uc008mls.2; mouse. [Q99K82-10]
DR UCSC; uc008mlt.2; mouse. [Q99K82-6]
DR UCSC; uc012cep.1; mouse. [Q99K82-7]
DR UCSC; uc012ceq.1; mouse. [Q99K82-5]
DR CTD; 54498; -.
DR MGI; MGI:2445356; Smox.
DR VEuPathDB; HostDB:ENSMUSG00000027333; -.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000157511; -.
DR HOGENOM; CLU_097972_0_0_1; -.
DR InParanoid; Q99K82; -.
DR OMA; IPKPHKV; -.
DR PhylomeDB; Q99K82; -.
DR TreeFam; TF318348; -.
DR BRENDA; 1.5.3.16; 3474.
DR Reactome; R-MMU-141334; PAOs oxidise polyamines to amines.
DR Reactome; R-MMU-351200; Interconversion of polyamines.
DR UniPathway; UPA00211; -.
DR BioGRID-ORCS; 228608; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Smox; mouse.
DR PRO; PR:Q99K82; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99K82; protein.
DR Bgee; ENSMUSG00000027333; Expressed in triceps brachii and 239 other tissues.
DR ExpressionAtlas; Q99K82; baseline and differential.
DR Genevisible; Q99K82; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; ISO:MGI.
DR GO; GO:0046208; P:spermine catabolic process; IDA:MGI.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; FAD; Flavoprotein; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..555
FT /note="Spermine oxidase"
FT /id="PRO_0000099878"
FT REGION 271..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 79..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 519
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 528..529
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT VAR_SEQ 146..510
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011127"
FT VAR_SEQ 204..510
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011130"
FT VAR_SEQ 204..243
FT /note="VESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVV -> GTPIYQNL
FT GESCAQPGAATHTSGVPIPTHRWAQVGRMWRS (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_011129"
FT VAR_SEQ 204..209
FT /note="VESCES -> SAMAMC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011128"
FT VAR_SEQ 205..555
FT /note="ESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPPHVIQ
FT LGKPVRCIHWDQASAHPRGPEIEPRGEGDHNHDTGEGGQSGENPQQGRWDEDEPWPVVV
FT ECEDCEVIPADHVIVTVSLGVLKRQYTSFFRPCLPTEKVAAIHRLGIGTTDKIFLEFEE
FT PFWGPECNSLQFVWEDEAESCTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEA
FT LVMERCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGA
FT DVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLF
FT QQGP -> SLLWSIDARVKKMNSGGVSVQSALLLRALVPCMA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011131"
FT VAR_SEQ 210..555
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011132"
FT VAR_SEQ 244..255
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_011133"
FT VAR_SEQ 282..417
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_011134"
FT VAR_SEQ 457..512
FT /note="GNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSK
FT TAPM -> AHAGALLRGGHTP (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011135"
FT VAR_SEQ 458..512
FT /note="NPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKT
FT APM -> GLKWGGCGEASQAPALHRELQDSAHAGALLRGGHTP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011136"
FT VAR_SEQ 510
FT /note="A -> AHRSSTEQQPGHLLPSKCPEQSLDPSRGSIK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011137"
FT VAR_SEQ 516..555
FT /note="FSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGP -> LHHPRCSA
FT LWPARGRPAHRDVPRPLPAGALKGVLTAKCVP (in isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:14764092"
FT /id="VSP_011138"
FT MUTAGEN 320
FT /note="C->R: No change in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12141946"
SQ 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
