Reviewed, UniProtKB/Swiss-Prot O60774 (FMO6_HUMAN)

Names and origin

Protein names

Recommended name:
    Putative dimethylaniline monooxygenase [N-oxide-forming] 6
    EC=1.14.13.8
Alternative name(s):
    Flavin-containing monooxygenase 6
      Short name=FMO 6
    Dimethylaniline oxidase 6

Gene names

Name:

FMO6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts.
Catalytic activity	N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
Cofactor	FAD By similarity.
Subcellular location	Microsome membraneBy similarity. Endoplasmic reticulum membraneBy similarity.
Polymorphism	There are two alleles; one major, FMO6X105 (truncated form) and one minor, FMO6Q105, (shown here) (full-length form similar to the protein found in other mammals). A nonsense mutation transforms the Gln-105 into a premature stop codon. The truncated protein is catalytically inactive.
Sequence similarities	Belongs to the FMO family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 539	539	Putative dimethylaniline monooxygenase [N-oxide-forming] 6		PRO_0000147669
Regions
	Transmembrane	518 – 538	21	Potential
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP By similarity
Natural variations
	Natural variant	127	1	V → I		VAR_015371
	Natural variant	257	1	V → I		VAR_015372

Sequences

	Sequence		Length	Mass (Da)
	O60774-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 8E0D15CA4F79FF0C	FASTA	539	61,291
	10 20 30 40 50 60 MSKRVGIIGA GVSGLAAIWC CLEEGLEPTC FERSDDVGGL WKFSDHTEEG RASIYQSVFT 70 80 90 100 110 120 NSSKEMMCFP DFPYPDDYPN YIHHSKLQEY IKTYAQKKDL LRYIQFETLV SGIKKCPSFL 130 140 150 160 170 180 VTGQWVVVTE KDGKQESTIF DAVMICSGHH VYPNLPTDSF PGLDQFRGNY LHSRDYKNPE 190 200 210 220 230 240 AFKGKRVLVI GLGNSGSDIA VELSRLATQV IISTRSASWV MSRVWDDGYP WDMMYVTRFA 250 260 270 280 290 300 SFLRNVLPSF ISDWLYVQKM NTWFKHENYG LMPLNGSLRK EPVFNDELPS RILCGTLSIK 310 320 330 340 350 360 PSVKEFTETS AVFEDGTMFE AIDSVIFATG YDYSYPFLDE TIMKSRNNEV TLFKGIFPPL 370 380 390 400 410 420 MEKPTLAVIG LVQSLGAAIP TADLQAWWAA KVFANSCTLP TTNEMMDDTD EKMGKKLKCM 430 440 450 460 470 480 FSSFFMFGQS QTLQTDYITY VDELGSFIGA KPNIPWLFLT DPRLALEVYF GPCSPYQFRL 490 500 510 520 530 MGPGKWDGAR NAILTQWNRT VKPTRTRVVS EVQRPHPFYN LLKMLSFPLL LLAVTLTFY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase." Hines R.N., Hopp K.A., Franco J., Saeian K., Begun F.P. Mol. Pharmacol. 62:320-325(2002) [PubMed: 12130684] [Abstract] Cited for: ANALYSIS OF SPLICE VARIANTS.
[3]	"Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans." Furnes B., Feng J., Sommer S.S., Schlenk D. Drug Metab. Dispos. 31:187-193(2003) [PubMed: 12527699] [Abstract] Cited for: VARIANTS ILE-127 AND ILE-257, POLYMORPHISM IN POSITION 105.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL021026 Genomic DNA. No translation available.
UniGene	Hs.448988
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	O60774.
Genome annotation databases
Ensembl	ENSG00000117507. Homo sapiens. [Contig view]
Organism-specific databases
HGNC	HGNC:24024. FMO6.
PharmGKB	PA142671753.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	O60774.
HOVERGEN	O60774.
Gene expression databases
ArrayExpress	O60774.
GermOnline	ENSG00000117507. Homo sapiens.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR012143. dManiline_mOase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000960. Flavin_mOase. IPR002255. Flavin_mOase_3. IPR001100. Pyr_nuc-diS_OxRdtase. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00419. ADXRDTASE. PR00368. FADPNR. PR00370. FMOXYGENASE. PR01123. FMOXYGENASE3. PR00411. PNDRDTASEI.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
LinkHub	O60774.

Entry information

Entry name

FMO6_HUMAN

Accession

Primary (citable) accession number: O60774

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	August 1, 1998
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)