FMO5_MOUSE
ID FMO5_MOUSE Reviewed; 533 AA.
AC P97872; Q8R1W6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Flavin-containing monooxygenase 5;
DE Short=FMO 5;
DE AltName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5 {ECO:0000305};
DE EC=1.14.13.8 {ECO:0000250|UniProtKB:P49326};
DE AltName: Full=Dimethylaniline oxidase 5;
DE AltName: Full=Hepatic flavin-containing monooxygenase 5;
DE AltName: Full=NADPH oxidase {ECO:0000250|UniProtKB:P49326};
DE EC=1.6.3.1 {ECO:0000250|UniProtKB:P49326};
GN Name=Fmo5 {ECO:0000312|MGI:MGI:1310004};
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], AND COFACTOR.
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=9580872;
RX DOI=10.1002/(sici)1099-0461(1998)12:4<205::aid-jbt2>3.0.co;2-p;
RA Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M.,
RA Levi P.E., Hodgson E.;
RT "Molecular cloning, sequence, and expression of mouse flavin-containing
RT monooxygenases 1 and 5 (FMO1 and FMO5).";
RL J. Biochem. Mol. Toxicol. 12:205-212(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26049045; DOI=10.1016/j.bcp.2015.05.013;
RA Gonzalez Malagon S.G., Melidoni A.N., Hernandez D., Omar B.A., Houseman L.,
RA Veeravalli S., Scott F., Varshavi D., Everett J., Tsuchiya Y., Timms J.F.,
RA Phillips I.R., Shephard E.A.;
RT "The phenotype of a knockout mouse identifies flavin-containing
RT monooxygenase 5 (FMO5) as a regulator of metabolic ageing.";
RL Biochem. Pharmacol. 96:267-277(2015).
RN [7]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY HFD.
RX PubMed=28646079; DOI=10.1124/dmd.117.076612;
RA Scott F., Gonzalez Malagon S.G., O'Brien B.A., Fennema D., Veeravalli S.,
RA Coveney C.R., Phillips I.R., Shephard E.A.;
RT "Identification of Flavin-Containing Monooxygenase 5 (FMO5) as a Regulator
RT of Glucose Homeostasis and a Potential Sensor of Gut Bacteria.";
RL Drug Metab. Dispos. 45:982-989(2017).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=29686991; DOI=10.3389/fmolb.2018.00028;
RA Varshavi D., Scott F.H., Varshavi D., Veeravalli S., Phillips I.R.,
RA Veselkov K., Strittmatter N., Takats Z., Shephard E.A., Everett J.R.;
RT "Metabolic Biomarkers of Ageing in C57BL/6J Wild-Type and Flavin-Containing
RT Monooxygenase 5 (FMO5)-Knockout Mice.";
RL Front. Mol. Biosci. 5:28-28(2018).
CC -!- FUNCTION: Acts as Baeyer-Villiger monooxygenase on a broad range of
CC substrates. Catalyzes the insertion of an oxygen atom into a carbon-
CC carbon bond adjacent to a carbonyl, which converts ketones to esters.
CC Active on diverse carbonyl compounds, whereas soft nucleophiles are
CC mostly non- or poorly reactive. In contrast with other forms of FMO it
CC is non- or poorly active on 'classical' substrates such as drugs,
CC pesticides, and dietary components containing soft nucleophilic
CC heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on
CC an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the
CC absence of substrates, shows slow but yet significant NADPH oxidase
CC activity (By similarity). Acts as a positive modulator of cholesterol
CC biosynthesis as well as glucose homeostasis, promoting metabolic aging
CC via pleiotropic effects (PubMed:26049045, PubMed:28646079).
CC {ECO:0000250|UniProtKB:P49326, ECO:0000269|PubMed:26049045,
CC ECO:0000269|PubMed:28646079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.8;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-2-one + NADPH + O2 = H2O + NADP(+) + pentyl
CC acetate; Xref=Rhea:RHEA:54836, ChEBI:CHEBI:5672, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87362;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = H2O + NADP(+) + pentyl
CC propanoate; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:80946, ChEBI:CHEBI:87373;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = ethyl hexanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:80946, ChEBI:CHEBI:86055;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = ethyl butanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88764, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = H2O + NADP(+) + propyl
CC propanoate; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89828, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-4-one + NADPH + O2 = H2O + NADP(+) + propyl
CC butanoate; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89484, ChEBI:CHEBI:89719;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-
CC 1,5-dien-1-yl formate + H2O + NADP(+); Xref=Rhea:RHEA:54860,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:138375; Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + sulcatone = 4-methylpent-3-en-1-yl acetate
CC + H2O + NADP(+); Xref=Rhea:RHEA:54864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16310,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138373;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC Evidence={ECO:0000250|UniProtKB:P49326};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:9580872};
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P49326}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P49326}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level)
CC (PubMed:26049045). Expressed in the mucosal epithelium of the
CC gastrointestinal tract (PubMed:28646079). {ECO:0000269|PubMed:26049045,
CC ECO:0000269|PubMed:28646079}.
CC -!- INDUCTION: In the gastrointestinal tract, expression is induced in
CC response to a high-fat diet. {ECO:0000269|PubMed:28646079}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit a lean phenotype, which is age-
CC related, becoming apparent after 20 weeks of age. Despite greater food
CC intake, they weigh less, store less fat in white adipose tissue (WAT),
CC have lower plasma glucose and cholesterol concentrations and enhanced
CC whole-body energy expenditure, due mostly to increased resting energy
CC expenditure, with no increase in physical activity. They show a a
CC higher rate of fatty acid oxidation in WAT (PubMed:26049045,
CC PubMed:29686991). When fed a high-fat diet, they are protected against
CC weight gain and reduction of insulin sensitivity (PubMed:28646079).
CC {ECO:0000269|PubMed:26049045, ECO:0000269|PubMed:28646079,
CC ECO:0000269|PubMed:29686991}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; U90535; AAB50013.1; -; mRNA.
DR EMBL; AK133675; BAE21778.1; -; mRNA.
DR EMBL; CH466620; EDL38939.1; -; Genomic_DNA.
DR EMBL; BC022991; AAH22991.1; -; mRNA.
DR CCDS; CCDS17656.1; -.
DR RefSeq; NP_001155235.1; NM_001161763.1.
DR RefSeq; NP_001155237.1; NM_001161765.1.
DR RefSeq; NP_034362.2; NM_010232.4.
DR RefSeq; XP_006501058.1; XM_006500995.3.
DR AlphaFoldDB; P97872; -.
DR SMR; P97872; -.
DR BioGRID; 199714; 3.
DR IntAct; P97872; 6.
DR STRING; 10090.ENSMUSP00000102665; -.
DR iPTMnet; P97872; -.
DR PhosphoSitePlus; P97872; -.
DR SwissPalm; P97872; -.
DR EPD; P97872; -.
DR jPOST; P97872; -.
DR MaxQB; P97872; -.
DR PaxDb; P97872; -.
DR PeptideAtlas; P97872; -.
DR PRIDE; P97872; -.
DR ProteomicsDB; 271702; -.
DR Antibodypedia; 2436; 212 antibodies from 25 providers.
DR DNASU; 14263; -.
DR Ensembl; ENSMUST00000029729; ENSMUSP00000029729; ENSMUSG00000028088.
DR Ensembl; ENSMUST00000107049; ENSMUSP00000102664; ENSMUSG00000028088.
DR Ensembl; ENSMUST00000107050; ENSMUSP00000102665; ENSMUSG00000028088.
DR GeneID; 14263; -.
DR KEGG; mmu:14263; -.
DR UCSC; uc008qoy.2; mouse.
DR CTD; 2330; -.
DR MGI; MGI:1310004; Fmo5.
DR VEuPathDB; HostDB:ENSMUSG00000028088; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160493; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; P97872; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; P97872; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 3474.
DR BioGRID-ORCS; 14263; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Fmo5; mouse.
DR PRO; PR:P97872; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P97872; protein.
DR Bgee; ENSMUSG00000028088; Expressed in urinary bladder urothelium and 141 other tissues.
DR Genevisible; P97872; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; ISO:MGI.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002257; Flavin_mOase_5.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01125; FMOXYGENASE5.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Lipid metabolism; Membrane;
KW Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..533
FT /note="Flavin-containing monooxygenase 5"
FT /id="PRO_0000147666"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 10..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 41..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 62..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 196..199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT MOD_RES 5
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4C0"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49326"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49326"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49326"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49326"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49326"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 313
FT /note="V -> I (in Ref. 1; AAB50013)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="L -> Q (in Ref. 1; AAB50013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 60001 MW; 4B9B246C4D7EBE34 CRC64;
MAKKRIAVIG AGASGLTCIK CCLEEGLEPV CFERSGDIGG LWRFQEAPEE GRASIYQSVV
INTSKEMMCF SDYPIPDHYP NYMHNSQVLE YFRMYAKEFD LLKYIQFKTT VCSVKKQPDF
STSGQWQVVT ECEGKQQVDV FDGVLVCTGH HTDAHLPLES FPGIEKFKGK YFHSRDYKNP
VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKHGY PIDLLLSSRI
MYYLSRICGP SLKNNYMEKQ MNQRFDHEMF GLKPKHRALS QHPTVNDDLP NRIIAGLVKV
KGNVKEFTET AAVFEDGSRE DGIDVVIFAT GYSFAFPFLE DSVKVVKNKV SLYKKVFPPN
LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KAREEMAKRY
VDSQRHTIQG DYIDTMEEIA DLVGVRPNIL PLVFTDPRLA LRLLLGPCTP VQYRLQGPGK
WAGARKTILT TEDRVRKPLM TRVVERDSSG GSLVTVRVLM LAVAFFAVIL AYF
