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   02-SEP-2026, entry version 182.
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 a 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=N,N-dimethylaniline + NADPH + O2 + H(+) = N,N-dimethylaniline
CC         N-oxide + NADP(+) + H2O; Xref=Rhea:RHEA:24468, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16269,
CC         ChEBI:CHEBI:17735, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.14.13.8; 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=NADPH + O2 + H(+) = 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=heptan-2-one + NADPH + O2 + H(+) = pentyl acetate + NADP(+) +
CC         H2O; 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=octan-3-one + NADPH + O2 + H(+) = pentyl propanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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=octan-3-one + NADPH + O2 + H(+) = ethyl hexanoate + NADP(+) +
CC         H2O; 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=hexan-3-one + NADPH + O2 + H(+) = ethyl butanoate + NADP(+) +
CC         H2O; 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=hexan-3-one + NADPH + O2 + H(+) = propyl propanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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=heptan-4-one + NADPH + O2 + H(+) = propyl butanoate + NADP(+)
CC         + H2O; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         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 + NADPH + O2 + H(+) = (1E)-2,6-
CC         dimethylhepta-1,5-dien-1-yl formate + NADP(+) + H2O;
CC         Xref=Rhea:RHEA:54860, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16980, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:138375;
CC         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=sulcatone + NADPH + O2 + H(+) = 4-methylpent-3-en-1-yl acetate
CC         + NADP(+) + H2O; 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_010232.5.
DR   RefSeq; XP_006501058.1; XM_006500995.5.
DR   AlphaFoldDB; P97872; -.
DR   SMR; P97872; -.
DR   BioGRID; 199714; 3.
DR   FunCoup; P97872; 1425.
DR   IntAct; P97872; 6.
DR   STRING; 10090.ENSMUSP00000102665; -.
DR   GlyGen; P97872; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P97872; -.
DR   PhosphoSitePlus; P97872; -.
DR   SwissPalm; P97872; -.
DR   jPOST; P97872; -.
DR   PaxDb; 10090-ENSMUSP00000102665; -.
DR   PeptideAtlas; P97872; -.
DR   ProteomicsDB; 271702; -.
DR   Antibodypedia; 2436; 210 antibodies from 27 providers.
DR   DNASU; 14263; -.
DR   Ensembl; ENSMUST00000029729.15; ENSMUSP00000029729.9; ENSMUSG00000028088.15.
DR   Ensembl; ENSMUST00000107049.2; ENSMUSP00000102664.2; ENSMUSG00000028088.15.
DR   Ensembl; ENSMUST00000107050.8; ENSMUSP00000102665.2; ENSMUSG00000028088.15.
DR   GeneID; 14263; -.
DR   KEGG; mmu:14263; -.
DR   UCSC; uc008qoy.2; mouse.
DR   AGR; MGI:1310004; -.
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; CCTGYDI; -.
DR   OrthoDB; 66881at2759; -.
DR   PhylomeDB; P97872; -.
DR   BRENDA; 1.14.13.8; 3474.
DR   BioGRID-ORCS; 14263; 4 hits in 76 CRISPR screens.
DR   PRO; PR:P97872; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P97872; protein.
DR   Bgee; ENSMUSG00000028088; Expressed in urinary bladder urothelium and 143 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; 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; ISS:UniProtKB.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR   FunFam; 3.50.50.60:FF:000042; Dimethylaniline monooxygenase [N-oxide-forming]; 1.
DR   FunFam; 3.50.50.60:FF:000073; Dimethylaniline monooxygenase [N-oxide-forming]; 1.
DR   FunFam; 3.50.50.60:FF:000409; Dimethylaniline monooxygenase [N-oxide-forming]; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   InterPro; IPR050346; FMO-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//