ID   FMO5_HUMAN              Reviewed;         533 AA.
AC   P49326; B2RBG1; C9JJD1; Q8IV22;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Flavin-containing monooxygenase 5;
DE            Short=FMO 5;
DE   AltName: Full=Baeyer-Villiger monooxygenase 1 {ECO:0000303|PubMed:28783300};
DE            Short=hBVMO1 {ECO:0000303|PubMed:28783300};
DE            EC=1.14.13.- {ECO:0000269|PubMed:20947616, ECO:0000269|PubMed:26771671, ECO:0000269|PubMed:28783300};
DE   AltName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5 {ECO:0000305};
DE            EC=1.14.13.8 {ECO:0000269|PubMed:7872795};
DE   AltName: Full=Dimethylaniline oxidase 5;
DE   AltName: Full=NADPH oxidase {ECO:0000303|PubMed:20947616};
DE            EC=1.6.3.1 {ECO:0000269|PubMed:26771671};
GN   Name=FMO5 {ECO:0000312|HGNC:HGNC:3773};
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), TISSUE SPECIFICITY, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=7872795; DOI=10.1006/abbi.1995.1163;
RA   Overby L.H., Buckpitt A.R., Lawton M.P., Atta-Asafo-Adjei E., Schulze J.,
RA   Philpot R.M.;
RT   "Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from
RT   human and guinea pig: evidence that the unique catalytic properties of FMO5
RT   are not confined to the rabbit ortholog.";
RL   Arch. Biochem. Biophys. 317:275-284(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver, and Placenta;
RA   Dolphin C.T., Povey S., Shephard E.A., Smith R.L., Phillips I.R.;
RT   "Cloning, primary sequence and chromosomal localisation of human flavin-
RT   containing monooxygenase 5 (FMO5).";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-400 AND SER-506.
RG   NIEHS SNPs program;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Trachea;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; TYR-56; SER-58; SER-280
RP   AND THR-284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20947616; DOI=10.1124/dmd.110.035360;
RA   Lai W.G., Farah N., Moniz G.A., Wong Y.N.;
RT   "A Baeyer-Villiger oxidation specifically catalyzed by human flavin-
RT   containing monooxygenase 5.";
RL   Drug Metab. Dispos. 39:61-70(2011).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=26771671; DOI=10.1021/acschembio.5b01016;
RA   Fiorentini F., Geier M., Binda C., Winkler M., Faber K., Hall M.,
RA   Mattevi A.;
RT   "Biocatalytic Characterization of Human FMO5: Unearthing Baeyer-Villiger
RT   Reactions in Humans.";
RL   ACS Chem. Biol. 11:1039-1048(2016).
RN   [12]
RP   FUNCTION.
RX   PubMed=28783300; DOI=10.1021/acschembio.7b00470;
RA   Fiorentini F., Romero E., Fraaije M.W., Faber K., Hall M., Mattevi A.;
RT   "Baeyer-Villiger Monooxygenase FMO5 as Entry Point in Drug Metabolism.";
RL   ACS Chem. Biol. 12:2379-2387(2017).
RN   [13]
RP   VARIANT LEU-457.
RX   PubMed=12527699; DOI=10.1124/dmd.31.2.187;
RA   Furnes B., Feng J., Sommer S.S., Schlenk D.;
RT   "Identification of novel variants of the flavin-containing monooxygenase
RT   gene family in African Americans.";
RL   Drug Metab. Dispos. 31:187-193(2003).
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       (PubMed:28783300, PubMed:26771671, PubMed:20947616). Active on diverse
CC       carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly
CC       reactive (PubMed:26771671, PubMed:7872795). In contrast with other
CC       forms of FMO it is non- or poorly active on 'classical' substrates such
CC       as drugs, pesticides, and dietary components containing soft
CC       nucleophilic heteroatoms (Probable) (PubMed:7872795). Able to oxidize
CC       drug molecules bearing a carbonyl group on an aliphatic chain, such as
CC       nabumetone and pentoxifylline (PubMed:28783300). Also, in the absence
CC       of substrates, shows slow but yet significant NADPH oxidase activity
CC       (PubMed:26771671). Acts as a positive modulator of cholesterol
CC       biosynthesis as well as glucose homeostasis, promoting metabolic aging
CC       via pleiotropic effects (By similarity). {ECO:0000250|UniProtKB:P97872,
CC       ECO:0000269|PubMed:20947616, ECO:0000269|PubMed:26771671,
CC       ECO:0000269|PubMed:28783300, ECO:0000269|PubMed:7872795,
CC       ECO:0000305|PubMed:26771671}.
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:0000269|PubMed:7872795};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC         Evidence={ECO:0000305|PubMed:7872795};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC         Evidence={ECO:0000305|PubMed:26771671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-
CC         dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+);
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC         Evidence={ECO:0000305|PubMed:26771671};
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:0000269|PubMed:26771671};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC         Evidence={ECO:0000305|PubMed:26771671};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=59 uM for NADPH {ECO:0000269|PubMed:26771671};
CC         Note=kcat is 11.84 min(-1) for the NADPH oxidase activity releasing
CC         hydrogen peroxide from O2. {ECO:0000269|PubMed:26771671};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305|PubMed:20947616}.
CC       Endoplasmic reticulum membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P49326-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P49326-2; Sequence=VSP_042729, VSP_042730;
CC       Name=3;
CC         IsoId=P49326-3; Sequence=VSP_045616, VSP_045617;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal and adult liver.
CC       {ECO:0000269|PubMed:7872795, ECO:0000305|PubMed:20947616}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fmo5/";
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DR   EMBL; L37080; AAA67849.1; -; mRNA.
DR   EMBL; Z47553; CAA87633.1; -; mRNA.
DR   EMBL; AY902236; AAW69390.1; -; Genomic_DNA.
DR   EMBL; AK314647; BAG37208.1; -; mRNA.
DR   EMBL; AK225739; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL356378; CAH72648.1; -; Genomic_DNA.
DR   EMBL; AL356378; CAH72649.1; -; Genomic_DNA.
DR   EMBL; CH471223; EAW50939.1; -; Genomic_DNA.
DR   EMBL; CH471223; EAW50940.1; -; Genomic_DNA.
DR   EMBL; BC035687; AAH35687.1; -; mRNA.
DR   CCDS; CCDS44209.1; -. [P49326-3]
DR   CCDS; CCDS44210.1; -. [P49326-2]
DR   CCDS; CCDS926.1; -. [P49326-1]
DR   PIR; S51131; S51131.
DR   PIR; S71618; S71618.
DR   RefSeq; NP_001138301.1; NM_001144829.2. [P49326-3]
DR   RefSeq; NP_001138302.1; NM_001144830.2. [P49326-2]
DR   RefSeq; NP_001452.2; NM_001461.3. [P49326-1]
DR   RefSeq; XP_005273003.1; XM_005272946.4. [P49326-1]
DR   RefSeq; XP_005273004.1; XM_005272947.4. [P49326-1]
DR   RefSeq; XP_005273005.1; XM_005272948.4. [P49326-1]
DR   RefSeq; XP_006711308.1; XM_006711245.3.
DR   RefSeq; XP_011507652.1; XM_011509350.2. [P49326-1]
DR   AlphaFoldDB; P49326; -.
DR   SMR; P49326; -.
DR   BioGRID; 108617; 54.
DR   IntAct; P49326; 5.
DR   STRING; 9606.ENSP00000254090; -.
DR   ChEMBL; CHEMBL3430871; -.
DR   SwissLipids; SLP:000001774; -.
DR   GlyGen; P49326; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P49326; -.
DR   PhosphoSitePlus; P49326; -.
DR   BioMuta; FMO5; -.
DR   DMDM; 1346021; -.
DR   jPOST; P49326; -.
DR   MassIVE; P49326; -.
DR   MaxQB; P49326; -.
DR   PaxDb; 9606-ENSP00000254090; -.
DR   PeptideAtlas; P49326; -.
DR   ProteomicsDB; 10453; -.
DR   ProteomicsDB; 55987; -. [P49326-1]
DR   ProteomicsDB; 55988; -. [P49326-2]
DR   Antibodypedia; 2436; 238 antibodies from 25 providers.
DR   DNASU; 2330; -.
DR   Ensembl; ENST00000254090.9; ENSP00000254090.4; ENSG00000131781.13. [P49326-1]
DR   Ensembl; ENST00000369272.7; ENSP00000358277.3; ENSG00000131781.13. [P49326-2]
DR   Ensembl; ENST00000441068.6; ENSP00000416011.2; ENSG00000131781.13. [P49326-3]
DR   Ensembl; ENST00000578284.5; ENSP00000462062.2; ENSG00000131781.13. [P49326-3]
DR   GeneID; 2330; -.
DR   KEGG; hsa:2330; -.
DR   MANE-Select; ENST00000254090.9; ENSP00000254090.4; NM_001461.4; NP_001452.2.
DR   UCSC; uc001eph.5; human. [P49326-1]
DR   AGR; HGNC:3773; -.
DR   CTD; 2330; -.
DR   DisGeNET; 2330; -.
DR   GeneCards; FMO5; -.
DR   HGNC; HGNC:3773; FMO5.
DR   HPA; ENSG00000131781; Tissue enriched (liver).
DR   MIM; 603957; gene.
DR   neXtProt; NX_P49326; -.
DR   OpenTargets; ENSG00000131781; -.
DR   PharmGKB; PA28189; -.
DR   VEuPathDB; HostDB:ENSG00000131781; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   GeneTree; ENSGT00940000160493; -.
DR   HOGENOM; CLU_006909_8_0_1; -.
DR   InParanoid; P49326; -.
DR   OMA; FMEWEHH; -.
DR   OrthoDB; 2079054at2759; -.
DR   PhylomeDB; P49326; -.
DR   TreeFam; TF105285; -.
DR   BRENDA; 1.14.13.8; 2681.
DR   PathwayCommons; P49326; -.
DR   SABIO-RK; P49326; -.
DR   SignaLink; P49326; -.
DR   BioGRID-ORCS; 2330; 9 hits in 1151 CRISPR screens.
DR   ChiTaRS; FMO5; human.
DR   GeneWiki; FMO5; -.
DR   GenomeRNAi; 2330; -.
DR   Pharos; P49326; Tbio.
DR   PRO; PR:P49326; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P49326; Protein.
DR   Bgee; ENSG00000131781; Expressed in right lobe of liver and 132 other cell types or tissues.
DR   ExpressionAtlas; P49326; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IBA:GO_Central.
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; IDA:UniProtKB.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF78; FLAVIN-CONTAINING MONOOXYGENASE 5; 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.
DR   Genevisible; P49326; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; FAD; Flavoprotein;
KW   Lipid metabolism; Membrane; Methylation; Microsome; Monooxygenase; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..533
FT                   /note="Flavin-containing monooxygenase 5"
FT                   /id="PRO_0000147665"
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:0007744|PubMed:24275569"
FT   MOD_RES         56
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         284
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97872"
FT   VAR_SEQ         278..285
FT                   /note="ALSQHPTL -> SKDIALTE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042729"
FT   VAR_SEQ         286..533
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042730"
FT   VAR_SEQ         419..464
FT                   /note="RYVESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLL -> SL
FT                   TMRKTSDKPKLKNILQIPDYLKTVKIINKESLRNCPGIKGPKET (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_045616"
FT   VAR_SEQ         465..533
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_045617"
FT   VARIANT         400
FT                   /note="P -> A (in dbSNP:rs28381218)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_022308"
FT   VARIANT         457
FT                   /note="P -> L (in dbSNP:rs72549314)"
FT                   /evidence="ECO:0000269|PubMed:12527699"
FT                   /id="VAR_015370"
FT   VARIANT         506
FT                   /note="R -> S (in dbSNP:rs28381223)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_022309"
FT   CONFLICT        351
FT                   /note="S -> P (in Ref. 2; CAA87633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  60221 MW;  F9D9F092F1DD71DA CRC64;
     MTKKRIAVIG GGVSGLSSIK CCVEEGLEPV CFERTDDIGG LWRFQENPEE GRASIYKSVI
     INTSKEMMCF SDYPIPDHYP NFMHNAQVLE YFRMYAKEFD LLKYIRFKTT VCSVKKQPDF
     ATSGQWEVVT ESEGKKEMNV FDGVMVCTGH HTNAHLPLES FPGIEKFKGQ YFHSRDYKNP
     EGFTGKRVII IGIGNSGGDL AVEISQTAKQ VFLSTRRGAW ILNRVGDYGY PADVLFSSRL
     THFIWKICGQ SLANKYLEKK INQRFDHEMF GLKPKHRALS QHPTLNDDLP NRIISGLVKV
     KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKI SLYKKVFPPN
     LERPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKTLP SQSEMMAEIS KAQEEIDKRY
     VESQRHTIQG DYIDTMEELA DLVGVRPNLL SLAFTDPKLA LHLLLGPCTP IHYRVQGPGK
     WDGARKAILT TDDRIRKPLM TRVVERSSSM TSTMTIGKFM LALAFFAIII AYF
//