FMO5_HUMAN
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 03-AUG-2022, entry version 195.
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 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-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: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 with NADPH as substrate.
CC {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. [P49326-2]
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; P49326; -.
DR PeptideAtlas; P49326; -.
DR PRIDE; P49326; -.
DR ProteomicsDB; 10453; -.
DR ProteomicsDB; 55987; -. [P49326-1]
DR ProteomicsDB; 55988; -. [P49326-2]
DR Antibodypedia; 2436; 212 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 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 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 1071 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 131 other tissues.
DR ExpressionAtlas; P49326; baseline and differential.
DR Genevisible; P49326; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; -; 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 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
