PAOX_HUMAN
ID PAOX_HUMAN Reviewed; 511 AA.
AC Q6QHF9; D3DXI6; Q5VWY0; Q6QHF5; Q6QHF6; Q6QHF7; Q6QHF8; Q6QHG0; Q6QHG1;
AC Q6QHG2; Q6QHG3; Q6QHG4; Q6QHG5; Q6QHG6; Q86WP9; Q8N555; Q8NCX3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
DE EC=1.5.3.13 {ECO:0000269|PubMed:12477380};
DE AltName: Full=Polyamine oxidase;
GN Name=PAOX; Synonyms=PAO; ORFNames=UNQ1923/PRO4398;
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).
RC TISSUE=Liver;
RX PubMed=12660232; DOI=10.1074/jbc.m302149200;
RA Wu T., Yankovskaya V., McIntire W.S.;
RT "Cloning, sequencing, and heterologous expression of the murine peroxisomal
RT flavoprotein, N(1)-acetylated polyamine oxidase.";
RL J. Biol. Chem. 278:20514-20525(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RA Wang Y., Murray-Stewart T., Hacker A., Casero R.A. Jr.;
RT "Polyamine oxidase.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-511 (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=12477380; DOI=10.1042/bj20021779;
RA Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.;
RT "Genomic identification and biochemical characterization of the mammalian
RT polyamine oxidase involved in polyamine back-conversion.";
RL Biochem. J. 370:19-28(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-
CC acetylspermine to spermidine and is thus involved in the polyamine
CC back-conversion (PubMed:12477380). Can also oxidize N(1)-
CC acetylspermidine to putrescine. Substrate specificity: N(1)-
CC acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >>
CC spermine. Does not oxidize spermidine. 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 (PubMed:12477380).
CC {ECO:0000269|PubMed:12477380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:25800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58101; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12477380};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12477380};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1),N(12)-diacetylspermine + O2 = 3-acetamidopropanal +
CC H2O2 + N(1)-acetylspermidine; Xref=Rhea:RHEA:25868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30322, ChEBI:CHEBI:58324, ChEBI:CHEBI:58550; EC=1.5.3.13;
CC Evidence={ECO:0000269|PubMed:12477380};
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 -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
CC {ECO:0000269|PubMed:12477380}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6QHF9-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6QHF9-6; Sequence=VSP_060446, VSP_060447;
CC Name=3;
CC IsoId=Q6QHF9-5; Sequence=VSP_060448, VSP_060449;
CC Name=4;
CC IsoId=Q6QHF9-4; Sequence=VSP_060450, VSP_060451;
CC -!- TISSUE SPECIFICITY: Widely expressed. Not detected in spleen. Expressed
CC at lower level in neoplastic tissues. {ECO:0000269|PubMed:12477380}.
CC -!- INDUCTION: By polyamine analogs.
CC -!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side of
CC their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side
CC of the N(4)-nitrogen (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88784.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAS64377.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAS64379.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAS64380.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAS64381.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAS64382.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAS64383.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAS64384.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF226657; AAN40706.1; -; mRNA.
DR EMBL; AF312698; AAO63265.1; -; mRNA.
DR EMBL; AY541513; AAS64373.1; -; mRNA.
DR EMBL; AY541514; AAS64374.1; -; mRNA.
DR EMBL; AY541515; AAS64375.1; -; mRNA.
DR EMBL; AY541516; AAS64376.1; -; mRNA.
DR EMBL; AY541517; AAS64377.1; ALT_FRAME; mRNA.
DR EMBL; AY541518; AAS64378.1; -; mRNA.
DR EMBL; AY541519; AAS64379.1; ALT_SEQ; mRNA.
DR EMBL; AY541520; AAS64380.1; ALT_SEQ; mRNA.
DR EMBL; AY541521; AAS64381.1; ALT_SEQ; mRNA.
DR EMBL; AY541522; AAS64382.1; ALT_SEQ; mRNA.
DR EMBL; AY541523; AAS64383.1; ALT_SEQ; mRNA.
DR EMBL; AY541524; AAS64384.1; ALT_SEQ; mRNA.
DR EMBL; AY358418; AAQ88784.1; ALT_SEQ; mRNA.
DR EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471211; EAW61340.1; -; Genomic_DNA.
DR EMBL; CH471211; EAW61341.1; -; Genomic_DNA.
DR EMBL; CH471211; EAW61344.1; -; Genomic_DNA.
DR EMBL; BC032778; AAH32778.1; -; mRNA.
DR EMBL; AL834535; CAD39191.1; -; mRNA.
DR CCDS; CCDS7682.1; -. [Q6QHF9-4]
DR CCDS; CCDS7683.1; -. [Q6QHF9-2]
DR CCDS; CCDS7684.1; -. [Q6QHF9-5]
DR RefSeq; NP_690875.1; NM_152911.3. [Q6QHF9-2]
DR RefSeq; NP_997010.1; NM_207127.2. [Q6QHF9-5]
DR RefSeq; NP_997011.1; NM_207128.2. [Q6QHF9-4]
DR AlphaFoldDB; Q6QHF9; -.
DR SMR; Q6QHF9; -.
DR BioGRID; 128224; 3.
DR STRING; 9606.ENSP00000278060; -.
DR BindingDB; Q6QHF9; -.
DR ChEMBL; CHEMBL2105; -.
DR iPTMnet; Q6QHF9; -.
DR PhosphoSitePlus; Q6QHF9; -.
DR BioMuta; PAOX; -.
DR DMDM; 51316248; -.
DR EPD; Q6QHF9; -.
DR MassIVE; Q6QHF9; -.
DR MaxQB; Q6QHF9; -.
DR PaxDb; Q6QHF9; -.
DR PeptideAtlas; Q6QHF9; -.
DR PRIDE; Q6QHF9; -.
DR ProteomicsDB; 67292; -. [Q6QHF9-2]
DR ProteomicsDB; 67294; -. [Q6QHF9-4]
DR ProteomicsDB; 67295; -. [Q6QHF9-5]
DR ProteomicsDB; 67296; -. [Q6QHF9-6]
DR Antibodypedia; 32666; 221 antibodies from 24 providers.
DR DNASU; 196743; -.
DR Ensembl; ENST00000278060.10; ENSP00000278060.5; ENSG00000148832.16. [Q6QHF9-2]
DR Ensembl; ENST00000356306.9; ENSP00000348654.5; ENSG00000148832.16. [Q6QHF9-5]
DR Ensembl; ENST00000357296.7; ENSP00000349847.3; ENSG00000148832.16. [Q6QHF9-4]
DR Ensembl; ENST00000476834.6; ENSP00000432737.1; ENSG00000148832.16. [Q6QHF9-6]
DR Ensembl; ENST00000480071.2; ENSP00000435514.1; ENSG00000148832.16. [Q6QHF9-5]
DR Ensembl; ENST00000483211.6; ENSP00000434550.1; ENSG00000148832.16. [Q6QHF9-6]
DR Ensembl; ENST00000529585.5; ENSP00000432517.1; ENSG00000148832.16. [Q6QHF9-6]
DR GeneID; 196743; -.
DR KEGG; hsa:196743; -.
DR MANE-Select; ENST00000278060.10; ENSP00000278060.5; NM_152911.4; NP_690875.1.
DR UCSC; uc001lmv.5; human. [Q6QHF9-2]
DR CTD; 196743; -.
DR DisGeNET; 196743; -.
DR GeneCards; PAOX; -.
DR HGNC; HGNC:20837; PAOX.
DR HPA; ENSG00000148832; Tissue enhanced (testis).
DR MIM; 615853; gene.
DR neXtProt; NX_Q6QHF9; -.
DR OpenTargets; ENSG00000148832; -.
DR PharmGKB; PA134907695; -.
DR VEuPathDB; HostDB:ENSG00000148832; -.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000158274; -.
DR HOGENOM; CLU_004498_2_0_1; -.
DR InParanoid; Q6QHF9; -.
DR OMA; LEPGNRW; -.
DR OrthoDB; 508351at2759; -.
DR PhylomeDB; Q6QHF9; -.
DR TreeFam; TF318348; -.
DR BRENDA; 1.5.3.13; 2681.
DR PathwayCommons; Q6QHF9; -.
DR Reactome; R-HSA-141334; PAOs oxidise polyamines to amines.
DR Reactome; R-HSA-351200; Interconversion of polyamines.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q6QHF9; -.
DR UniPathway; UPA00826; -.
DR BioGRID-ORCS; 196743; 17 hits in 1077 CRISPR screens.
DR GeneWiki; PAOX; -.
DR GenomeRNAi; 196743; -.
DR Pharos; Q6QHF9; Tchem.
DR PRO; PR:Q6QHF9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6QHF9; protein.
DR Bgee; ENSG00000148832; Expressed in sperm and 132 other tissues.
DR Genevisible; Q6QHF9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0052899; F:N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) 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:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:UniProtKB.
DR GO; GO:1901307; P:positive regulation of spermidine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009446; P:putrescine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IDA:UniProtKB.
DR GO; GO:0046203; P:spermidine catabolic process; IDA:UniProtKB.
DR GO; GO:0046208; P:spermine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..511
FT /note="Peroxisomal N(1)-acetyl-spermine/spermidine oxidase"
FT /id="PRO_0000099875"
FT MOTIF 509..511
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 69..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 472
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 481..482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 62..69
FT /note="GVVEVGAH -> AIKDSQTA (in isoform 2)"
FT /id="VSP_060446"
FT VAR_SEQ 70..511
FT /note="Missing (in isoform 2)"
FT /id="VSP_060447"
FT VAR_SEQ 291..325
FT /note="FLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFL -> LSTFSVGSLPDLS
FT LSSWRLCRMKKYFCVSPKCSGE (in isoform 3)"
FT /id="VSP_060448"
FT VAR_SEQ 326..511
FT /note="Missing (in isoform 3)"
FT /id="VSP_060449"
FT VAR_SEQ 412..486
FT /note="GNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAGA
FT QLQILFAGEATHRTFYSTTHGAL -> APDPVCGGSHTSHVLLHDARGSAVGMEGGRPP
FT PQSVGPAGAAAQAQALAGPSLLCSTRVGGRLGPSFLLTDFSLA (in isoform 4)"
FT /id="VSP_060450"
FT VAR_SEQ 487..511
FT /note="Missing (in isoform 4)"
FT /id="VSP_060451"
FT CONFLICT 23
FT /note="I -> M (in Ref. 2; AAS64378)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="H -> Q (in Ref. 2; AAS64378)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="R -> Q (in Ref. 1; AAN40706)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> V (in Ref. 1; AAN40706)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="E -> G (in Ref. 2; AAS64376)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="E -> K (in Ref. 2; AAS64373)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="L -> F (in Ref. 2; AAS64381)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="V -> G (in Ref. 1; AAN40706)"
FT /evidence="ECO:0000305"
FT CONFLICT Q6QHF9-4:457
FT /note="Q -> E (in Ref. 2; AAS64376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 55513 MW; BF1A6E43AA09965A CRC64;
MESTGSVGEA PGGPRVLVVG GGIAGLGAAQ RLCGHSAFPH LRVLEATARA GGRIRSERCF
GGVVEVGAHW IHGPSRGNPV FQLAAEYGLL GEKELSQENQ LVETGGHVGL PSVSYASSGA
SVSLQLVAEM ATLFYGLIDQ TREFLHAAET PVPSVGEYLK KEIGQHVAGW TEDEETRKLK
LAVLNSFFNL ECCVSGTHSM DLVALAPFGE YTVLPGLDCT FSKGYQGLTN CMMAALPEDT
VVFEKPVKTI HWNGSFQEAA FPGETFPVSV ECEDGDRFPA HHVIVTVPLG FLREHLDTFF
DPPLPAEKAE AIRKIGFGTN NKIFLEFEEP FWEPDCQLIQ LVWEDTSPLE DAAPELQDAW
FRKLIGFVVL PAFASVHVLC GFIAGLESEF METLSDEEVL LCLTQVLRRV TGNPRLPAPK
SVLRSRWHSA PYTRGSYSYV AVGSTGGDLD LLAQPLPADG AGAQLQILFA GEATHRTFYS
TTHGALLSGW READRLLSLW APQVQQPRPR L
