ID FMO5_HUMAN Reviewed; 533 AA. AC P49326; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-DEC-2008, entry version 78. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5; DE EC=1.14.13.8; DE AltName: Full=Hepatic flavin-containing monooxygenase 5; DE Short=FMO 5; DE AltName: Full=Dimethylaniline oxidase 5; GN Name=FMO5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=95177663; PubMed=7872795; DOI=10.1006/abbi.1995.1163; RA Overby L.H., Buckpitt A.R., Lawton M.P., Atta-Asafo-Adjei E., RA Schulze J., Philpot R.M.; RT "Characterization of flavin-containing monooxygenase 5 (FMO5) cloned RT from human and guinea pig: evidence that the unique catalytic RT properties of FMO5 are not confined to the rabbit ortholog."; RL Arch. Biochem. Biophys. 317:275-284(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 RT flavin-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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [5] RP VARIANT LEU-457. RX MEDLINE=22414999; 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 RT monooxygenase gene family in African Americans."; RL Drug Metab. Dispos. 31:187-193(2003). CC -!- FUNCTION: In contrast with other forms of FMO it does not seem to CC be a drug-metabolizing enzyme. CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum CC membrane. CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult liver. CC -!- SIMILARITY: Belongs to the FMO family. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/fmo5/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L37080; AAA67849.1; -; mRNA. DR EMBL; Z47553; CAA87633.1; -; mRNA. DR EMBL; AY902236; AAW69390.1; -; Genomic_DNA. DR EMBL; AL356378; CAH72648.1; -; Genomic_DNA. DR PIR; S51131; S51131. DR PIR; S71618; S71618. DR RefSeq; NP_001452.1; -. DR UniGene; Hs.642706; -. DR PhosphoSite; P49326; -. DR PRIDE; P49326; -. DR Ensembl; ENSG00000131781; Homo sapiens. DR GeneID; 2330; -. DR KEGG; hsa:2330; -. DR GeneCards; GC01M145124; -. DR HGNC; HGNC:3773; FMO5. DR HPA; HPA012373; -. DR MIM; 603957; gene. DR PharmGKB; PA28189; -. DR HOGENOM; P49326; -. DR HOVERGEN; P49326; -. DR NextBio; 9457; -. DR ArrayExpress; P49326; -. DR CleanEx; HS_FMO5; -. DR GermOnline; ENSG00000131781; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro. DR GO; GO:0005792; C:microsome; NAS:UniProtKB. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0004499; F:flavin-containing monooxygenase activity; NAS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR012143; dManiline_mOase. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR002257; Flavin_mOase_5. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01125; FMOXYGENASE5. DR ProDom; PD000139; FAD_pyr_redox; 1. PE 2: Evidence at transcript level; KW Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Polymorphism; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 533 Dimethylaniline monooxygenase [N-oxide- FT forming] 5. FT /FTId=PRO_0000147665. FT NP_BIND 10 15 FAD (Potential). FT NP_BIND 192 197 NADP (By similarity). FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 5 5 Omega-N-methylated arginine (By FT similarity). FT VARIANT 400 400 P -> A. FT /FTId=VAR_022308. FT VARIANT 457 457 P -> L. FT /FTId=VAR_015370. FT VARIANT 506 506 R -> S. FT /FTId=VAR_022309. FT CONFLICT 351 351 S -> P (in Ref. 2; CAA87633). 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 //