ID   FMO6_HUMAN              Reviewed;         539 AA.
AC   O60774;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   07-JUL-2009, entry version 69.
DE   RecName: Full=Putative dimethylaniline monooxygenase [N-oxide-forming] 6;
DE            EC=1.14.13.8;
DE   AltName: Full=Flavin-containing monooxygenase 6;
DE            Short=FMO 6;
DE   AltName: Full=Dimethylaniline oxidase 6;
GN   Name=FMO6;
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 [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   [2]
RP   ANALYSIS OF SPLICE VARIANTS.
RX   MEDLINE=22126689; PubMed=12130684; DOI=10.1124/mol.62.2.320;
RA   Hines R.N., Hopp K.A., Franco J., Saeian K., Begun F.P.;
RT   "Alternative processing of the human FMO6 gene renders transcripts
RT   incapable of encoding a functional flavin-containing monooxygenase.";
RL   Mol. Pharmacol. 62:320-325(2002).
RN   [3]
RP   VARIANTS ILE-127 AND ILE-257, AND POLYMORPHISM IN POSITION 105.
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: It is probable that this protein is only produced in
CC       very small quantity or not at all as the gene coding for it seems
CC       to be unable to produce full length transcripts.
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity).
CC       Endoplasmic reticulum membrane (By similarity).
CC   -!- POLYMORPHISM: There are two alleles; one major, FMO6X105
CC       (truncated form) and one minor, FMO6Q105, (shown here) (full-
CC       length form similar to the protein found in other mammals). A
CC       nonsense mutation transforms the Gln-105 into a premature stop
CC       codon. The truncated protein is catalytically inactive.
CC   -!- SIMILARITY: Belongs to the FMO family.
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DR   EMBL; AL021026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00012190; -.
DR   UniGene; Hs.448988; -.
DR   PRIDE; O60774; -.
DR   Ensembl; ENSG00000117507; Homo sapiens.
DR   GeneCards; GC01P169375; -.
DR   HGNC; HGNC:24024; FMO6.
DR   PharmGKB; PA142671753; -.
DR   HOGENOM; O60774; -.
DR   HOVERGEN; O60774; -.
DR   OMA; O60774; MGKKLKC.
DR   BRENDA; 1.14.13.8; 247.
DR   ArrayExpress; O60774; -.
DR   Bgee; O60774; -.
DR   GermOnline; ENSG00000117507; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004499; F:flavin-containing monooxygenase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012143; dManiline_mOase.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR002255; Flavin_mOase_3.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
KW   Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism;
KW   Transmembrane.
FT   CHAIN         1    539       Putative dimethylaniline monooxygenase
FT                                [N-oxide-forming] 6.
FT                                /FTId=PRO_0000147669.
FT   TRANSMEM    518    538       Potential.
FT   NP_BIND       9     14       FAD (Potential).
FT   NP_BIND     191    196       NADP (By similarity).
FT   VARIANT     127    127       V -> I.
FT                                /FTId=VAR_015371.
FT   VARIANT     257    257       V -> I.
FT                                /FTId=VAR_015372.
SQ   SEQUENCE   539 AA;  61291 MW;  8E0D15CA4F79FF0C CRC64;
     MSKRVGIIGA GVSGLAAIWC CLEEGLEPTC FERSDDVGGL WKFSDHTEEG RASIYQSVFT
     NSSKEMMCFP DFPYPDDYPN YIHHSKLQEY IKTYAQKKDL LRYIQFETLV SGIKKCPSFL
     VTGQWVVVTE KDGKQESTIF DAVMICSGHH VYPNLPTDSF PGLDQFRGNY LHSRDYKNPE
     AFKGKRVLVI GLGNSGSDIA VELSRLATQV IISTRSASWV MSRVWDDGYP WDMMYVTRFA
     SFLRNVLPSF ISDWLYVQKM NTWFKHENYG LMPLNGSLRK EPVFNDELPS RILCGTLSIK
     PSVKEFTETS AVFEDGTMFE AIDSVIFATG YDYSYPFLDE TIMKSRNNEV TLFKGIFPPL
     MEKPTLAVIG LVQSLGAAIP TADLQAWWAA KVFANSCTLP TTNEMMDDTD EKMGKKLKCM
     FSSFFMFGQS QTLQTDYITY VDELGSFIGA KPNIPWLFLT DPRLALEVYF GPCSPYQFRL
     MGPGKWDGAR NAILTQWNRT VKPTRTRVVS EVQRPHPFYN LLKMLSFPLL LLAVTLTFY
//