SMOX_HUMAN
ID SMOX_HUMAN Reviewed; 555 AA.
AC Q9NWM0; A2A2P5; A2A2P6; A8BE87; D3DVZ4; Q5TE26; Q5TE27; Q6UY28; Q8IX00;
AC Q96LC3; Q96LC4; Q96QT3; Q9BW38; Q9H6H1; Q9NP51; Q9NPY1; Q9NPY2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Spermine oxidase;
DE EC=1.5.3.16 {ECO:0000269|PubMed:11454677, ECO:0000269|PubMed:12398765};
DE AltName: Full=Polyamine oxidase 1;
DE Short=PAO-1;
DE Short=PAOh1;
GN Name=SMOX; Synonyms=C20orf16, SMO; ORFNames=UNQ3039/PRO9854;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CATALYTIC ACTIVITY.
RC TISSUE=Placenta;
RX PubMed=11454677;
RA Wang Y., Devereux W., Woster P.M., Murray-Stewart T., Hacker A.,
RA Casero R.A. Jr.;
RT "Cloning and characterization of a human polyamine oxidase that is
RT inducible by polyamine analogue exposure.";
RL Cancer Res. 61:5370-5373(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC TISSUE=Lung carcinoma;
RX PubMed=12398765; DOI=10.1042/bj20021587;
RA Murray-Stewart T., Wang Y., Devereux W., Casero R.A. Jr.;
RT "Cloning and characterization of multiple human polyamine oxidase splice
RT variants that code for isoenzymes with different biochemical
RT characteristics.";
RL Biochem. J. 368:673-677(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18422650; DOI=10.1111/j.1742-4658.2008.06419.x;
RA Murray-Stewart T., Wang Y., Goodwin A., Hacker A., Meeker A.,
RA Casero R.A. Jr.;
RT "Nuclear localization of human spermine oxidase isoforms - possible
RT implications in drug response and disease etiology.";
RL FEBS J. 275:2795-2806(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-522.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Hepatoma, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-555 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP CHARACTERIZATION (ISOFORM 1).
RX PubMed=12727196; DOI=10.1016/s0006-291x(03)00636-3;
RA Wang Y., Murray-Stewart T., Devereux W., Hacker A., Frydman B.,
RA Woster P.M., Casero R.A. Jr.;
RT "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.";
RL Biochem. Biophys. Res. Commun. 304:605-611(2003).
RN [11]
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).
RN [12]
RP REVIEW.
RX PubMed=15221502; DOI=10.1007/s00726-004-0070-z;
RA Seiler N.;
RT "Catabolism of polyamines.";
RL Amino Acids 26:217-233(2004).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-340.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:11454677, ECO:0000269|PubMed:12141946,
CC ECO:0000269|PubMed:12398765};
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 -!- ACTIVITY REGULATION: Inhibited at more than 90% by SL-11144, SL-11150
CC and SL-11158, at concentrations less than 1 uM.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for spermine (isoform 1) {ECO:0000269|PubMed:12141946,
CC ECO:0000269|PubMed:12398765, ECO:0000269|PubMed:18422650};
CC KM=0.5 uM for spermine (isoform 6) {ECO:0000269|PubMed:12141946,
CC ECO:0000269|PubMed:12398765, ECO:0000269|PubMed:18422650};
CC KM=3.0 uM for N1-acetylspermine (Isoform 1 and isoform 6)
CC {ECO:0000269|PubMed:12141946, ECO:0000269|PubMed:12398765,
CC ECO:0000269|PubMed:18422650};
CC Note=kcat is 27-fold higher with spermine than N1-acetylspermine as
CC substrate for isoform 1 and isoform 6.;
CC pH dependence:
CC Optimum pH is 9.5 with spermine as substrate.
CC {ECO:0000269|PubMed:12141946, ECO:0000269|PubMed:12398765,
CC ECO:0000269|PubMed:18422650};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000269|PubMed:12398765}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=The resultant proteins have different biochemical
CC characteristics and substrate specificity.;
CC Name=1; Synonyms=PAOh1, SMO;
CC IsoId=Q9NWM0-1; Sequence=Displayed;
CC Name=2; Synonyms=PAOh2;
CC IsoId=Q9NWM0-2; Sequence=VSP_011125;
CC Name=3; Synonyms=PAOh3;
CC IsoId=Q9NWM0-3; Sequence=VSP_011124;
CC Name=4; Synonyms=PAOh4;
CC IsoId=Q9NWM0-4; Sequence=VSP_011125, VSP_011126;
CC Name=5;
CC IsoId=Q9NWM0-5; Sequence=VSP_011123, VSP_011126;
CC Name=6; Synonyms=SMO5, SMOX5;
CC IsoId=Q9NWM0-6; Sequence=VSP_011126;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in human tumor cell
CC lines. Isoform 4 is only found in an embryonal kidney cell line.
CC {ECO:0000269|PubMed:18422650}.
CC -!- INDUCTION: By antitumor polyamine analogs.
CC -!- MISCELLANEOUS: [Isoform 1]: Low affinity for acetylated polyamine.
CC -!- MISCELLANEOUS: [Isoform 2]: Low affinity for acetylated polyamine.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Major isoform. Has the highest affinity for
CC the 3 substrates. Has a greater affinity for spermidine and spermine
CC than for N(1)-acetylspermine. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Has the lowest Km values for the different
CC substrates and has the highest affinity for spermidine. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Does not seem to display oxidase activity
CC towards spermidine or N(1)-acetyl-spermine, but this has to be
CC confirmed. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Substrate specificities and affinities
CC comparable to those of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY033889; AAK55763.1; -; mRNA.
DR EMBL; AY033890; AAK55764.1; -; mRNA.
DR EMBL; AY033891; AAK55765.1; -; mRNA.
DR EMBL; AF519179; AAN77119.1; -; mRNA.
DR EMBL; EF032141; ABM01872.1; -; mRNA.
DR EMBL; AY358104; AAQ88471.1; -; mRNA.
DR EMBL; AK000753; BAA91360.1; -; mRNA.
DR EMBL; AK025938; BAB15288.1; -; mRNA.
DR EMBL; AL121675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10460.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10461.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10457.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10458.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10459.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10462.1; -; Genomic_DNA.
DR EMBL; BC000669; AAH00669.1; -; mRNA.
DR EMBL; AL162058; CAB82396.1; -; mRNA.
DR CCDS; CCDS13075.1; -. [Q9NWM0-1]
DR CCDS; CCDS13076.1; -. [Q9NWM0-2]
DR CCDS; CCDS13077.1; -. [Q9NWM0-3]
DR CCDS; CCDS13078.1; -. [Q9NWM0-4]
DR CCDS; CCDS74702.1; -. [Q9NWM0-6]
DR PIR; T47142; T47142.
DR RefSeq; NP_001257620.1; NM_001270691.1. [Q9NWM0-6]
DR RefSeq; NP_787033.1; NM_175839.2. [Q9NWM0-1]
DR RefSeq; NP_787034.1; NM_175840.2. [Q9NWM0-2]
DR RefSeq; NP_787035.1; NM_175841.2. [Q9NWM0-3]
DR RefSeq; NP_787036.1; NM_175842.2. [Q9NWM0-4]
DR RefSeq; XP_011527563.1; XM_011529261.2. [Q9NWM0-6]
DR AlphaFoldDB; Q9NWM0; -.
DR SMR; Q9NWM0; -.
DR BioGRID; 119994; 11.
DR IntAct; Q9NWM0; 7.
DR STRING; 9606.ENSP00000478305; -.
DR BindingDB; Q9NWM0; -.
DR ChEMBL; CHEMBL2176769; -.
DR DrugBank; DB04188; MDL72527.
DR DrugBank; DB00127; Spermine.
DR iPTMnet; Q9NWM0; -.
DR PhosphoSitePlus; Q9NWM0; -.
DR BioMuta; SMOX; -.
DR DMDM; 50401688; -.
DR EPD; Q9NWM0; -.
DR jPOST; Q9NWM0; -.
DR MassIVE; Q9NWM0; -.
DR MaxQB; Q9NWM0; -.
DR PaxDb; Q9NWM0; -.
DR PeptideAtlas; Q9NWM0; -.
DR PRIDE; Q9NWM0; -.
DR ProteomicsDB; 82946; -. [Q9NWM0-1]
DR ProteomicsDB; 82947; -. [Q9NWM0-2]
DR ProteomicsDB; 82948; -. [Q9NWM0-3]
DR ProteomicsDB; 82949; -. [Q9NWM0-4]
DR ProteomicsDB; 82950; -. [Q9NWM0-5]
DR ProteomicsDB; 82951; -. [Q9NWM0-6]
DR Antibodypedia; 23782; 129 antibodies from 19 providers.
DR DNASU; 54498; -.
DR Ensembl; ENST00000278795.7; ENSP00000278795.3; ENSG00000088826.18. [Q9NWM0-4]
DR Ensembl; ENST00000305958.9; ENSP00000307252.4; ENSG00000088826.18. [Q9NWM0-1]
DR Ensembl; ENST00000339123.10; ENSP00000344595.6; ENSG00000088826.18. [Q9NWM0-2]
DR Ensembl; ENST00000346595.6; ENSP00000341775.2; ENSG00000088826.18. [Q9NWM0-3]
DR Ensembl; ENST00000379460.6; ENSP00000368773.2; ENSG00000088826.18. [Q9NWM0-1]
DR Ensembl; ENST00000621355.4; ENSP00000478305.1; ENSG00000088826.18. [Q9NWM0-6]
DR GeneID; 54498; -.
DR KEGG; hsa:54498; -.
DR MANE-Select; ENST00000305958.9; ENSP00000307252.4; NM_175839.3; NP_787033.1.
DR UCSC; uc002wkk.2; human. [Q9NWM0-1]
DR CTD; 54498; -.
DR DisGeNET; 54498; -.
DR GeneCards; SMOX; -.
DR HGNC; HGNC:15862; SMOX.
DR HPA; ENSG00000088826; Tissue enhanced (brain).
DR MIM; 615854; gene.
DR neXtProt; NX_Q9NWM0; -.
DR OpenTargets; ENSG00000088826; -.
DR PharmGKB; PA25701; -.
DR VEuPathDB; HostDB:ENSG00000088826; -.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000157511; -.
DR HOGENOM; CLU_004498_2_3_1; -.
DR InParanoid; Q9NWM0; -.
DR OMA; IPKPHKV; -.
DR OrthoDB; 508351at2759; -.
DR PhylomeDB; Q9NWM0; -.
DR TreeFam; TF318348; -.
DR BioCyc; MetaCyc:HS01609-MON; -.
DR BRENDA; 1.5.3.16; 2681.
DR PathwayCommons; Q9NWM0; -.
DR Reactome; R-HSA-141334; PAOs oxidise polyamines to amines. [Q9NWM0-3]
DR Reactome; R-HSA-351200; Interconversion of polyamines. [Q9NWM0-3]
DR SABIO-RK; Q9NWM0; -.
DR SignaLink; Q9NWM0; -.
DR UniPathway; UPA00211; -.
DR BioGRID-ORCS; 54498; 10 hits in 1085 CRISPR screens.
DR ChiTaRS; SMOX; human.
DR GeneWiki; SMOX; -.
DR GenomeRNAi; 54498; -.
DR Pharos; Q9NWM0; Tbio.
DR PRO; PR:Q9NWM0; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NWM0; protein.
DR Bgee; ENSG00000088826; Expressed in amygdala and 172 other tissues.
DR ExpressionAtlas; Q9NWM0; baseline and differential.
DR Genevisible; Q9NWM0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; TAS:Reactome.
DR GO; GO:0006596; P:polyamine biosynthetic process; TAS:Reactome.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:UniProtKB.
DR GO; GO:0046208; P:spermine catabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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_0000099877"
FT REGION 271..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..306
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 1..196
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011123"
FT VAR_SEQ 146..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12398765"
FT /id="VSP_011124"
FT VAR_SEQ 282..334
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12398765,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011125"
FT VAR_SEQ 510
FT /note="A -> AHGSSTKQQPGHLFSSKCPEQPLDANRGAVK (in isoform 4,
FT isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12398765,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:18422650"
FT /id="VSP_011126"
FT VARIANT 301
FT /note="R -> P (in dbSNP:rs6084654)"
FT /id="VAR_059114"
FT VARIANT 340
FT /note="Q -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036546"
FT VARIANT 522
FT /note="H -> Y"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_019531"
FT MUTAGEN 320
FT /note="C->R: No change in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12141946"
FT CONFLICT 16
FT /note="S -> R (in Ref. 2; AAK55764)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="I -> V (in Ref. 2; AAK55765)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="H -> Y (in Ref. 2; AAK55764)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="T -> A (in Ref. 5; BAB15288)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="C -> R (in Ref. 1; AAK55763 and 3; ABM01872)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="F -> L (in Ref. 2; AAN77119)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="E -> G (in Ref. 2; AAN77119 and 3; ABM01872)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="T -> A (in Ref. 2; AAK55764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 61819 MW; BDBEA65ECE9F45BF CRC64;
MQSCESSGDS ADDPLSRGLR RRGQPRVVVI GAGLAGLAAA KALLEQGFTD VTVLEASSHI
GGRVQSVKLG HATFELGATW IHGSHGNPIY HLAEANGLLE ETTDGERSVG RISLYSKNGV
ACYLTNHGRR IPKDVVEEFS DLYNEVYNLT QEFFRHDKPV NAESQNSVGV FTREEVRNRI
RNDPDDPEAT KRLKLAMIQQ YLKVESCESS SHSMDEVSLS AFGEWTEIPG AHHIIPSGFM
RVVELLAEGI PAHVIQLGKP VRCIHWDQAS ARPRGPEIEP RGEGDHNHDT GEGGQGGEEP
RGGRWDEDEQ WSVVVECEDC ELIPADHVIV TVSLGVLKRQ YTSFFRPGLP TEKVAAIHRL
GIGTTDKIFL EFEEPFWGPE CNSLQFVWED EAESHTLTYP PELWYRKICG FDVLYPPERY
GHVLSGWICG EEALVMEKCD DEAVAEICTE MLRQFTGNPN IPKPRRILRS AWGSNPYFRG
SYSYTQVGSS GADVEKLAKP LPYTESSKTA PMQVLFSGEA THRKYYSTTH GALLSGQREA
ARLIEMYRDL FQQGT
